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        <title>Journal of Industrial Microbiology and Biotechnology via MedWorm.com</title>
        <description>MedWorm.com provides a medical RSS filtering service. Over 6000 RSS medical sources are combined and output via different filters. This feed contains the latest items from the 'Journal of Industrial Microbiology and Biotechnology' source.</description>
        <link><![CDATA[http://www.medworm.com/rss/search.php?qu=Journal+of+Industrial+Microbiology+and+Biotechnology&t=Journal+of+Industrial+Microbiology+and+Biotechnology&s=Search&f=source]]></link>
        <lastBuildDate>Thu, 09 Feb 2012 21:35:02 +0100</lastBuildDate>
        <item>
            <title>Characterization of polyhydroxyalkanoates (PHAs) biosynthesis by isolated Novosphingobium sp. THA_AIK7 using crude glycerol.</title>
            <link>http://www.medworm.com/index.php?rid=5658219&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22286712%26dopt%3DAbstract</link>
            <description>Authors: Teeka J, Imai T, Reungsang A, Cheng X, Yuliani E, Thiantanankul J, Poomipuk N, Yamaguchi J, Jeenanong A, Higuchi T, Yamamoto K, Sekine M
    Abstract
    Biodiesel-contaminated wastewater was used to screen for PHAs-producing bacteria by using crude glycerol as the sole carbon source. A gram-negative THA_AIK7 isolate was chosen as a potential PHAs producer. The 16S rRNA phylogeny indicated that THA_AIK7 isolate is a member of Novosphingobium genus which is supported by a bootstrap percentage of 100% with Novosphingobium capsulatum. The 1,487 bp of 16S rRNA gene sequence of THA_AIK7 isolate has been deposited in the GenBank database under the accession number HM031593. Polymer content of 45% cell dry weight was achieved in 72 h with maximum product yield coefficient of 0.29 g PH...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5658219</comments>
            <pubDate>Sun, 29 Jan 2012 05:00:00 +0100</pubDate>
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        <item>
            <title>An alkaline-active and alkali-stable pectate lyase from Streptomyces sp. S27 with potential in textile industry.</title>
            <link>http://www.medworm.com/index.php?rid=5658220&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22278674%26dopt%3DAbstract</link>
            <description>Authors: Yuan P, Meng K, Shi P, Luo H, Huang H, Tu T, Yang P, Yao B
    Abstract
    A pectate lyase gene (pl-str) was cloned from Streptomyces sp. S27 and expressed in Escherichia coli Rosetta. The full-length pl-str consists of 972 bp and encodes for a protein of 323 amino acids without signal peptide that belongs to family PF00544. The recombinant enzyme (r-PL-STR) was purified to electrophoretic homogeneity using Ni(2+)-NTA chromatography and showed apparent molecular mass of ~35 kDa. The pH optimum of r-PL-STR was found to be 10.0, and it exhibited &amp;gt;70% of the maximal activity at pH 12.0. After incubation at 37°C for 1 h without substrate, the enzyme retained more than 55% activity at pH 7.0-12.0. Compared with the commercial complex enzyme Scourzyme(@)301L from Novozymes, pur...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5658220</comments>
            <pubDate>Thu, 26 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5658220</guid>        </item>
        <item>
            <title>A genome shuffling-generated Saccharomyces cerevisiae isolate that ferments xylose and glucose to produce high levels of ethanol.</title>
            <link>http://www.medworm.com/index.php?rid=5658224&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22270888%26dopt%3DAbstract</link>
            <description>This report describes optimized conditions for protoplast preparation, regeneration, inactivation, and fusion using the Saccharomyces cerevisiae W5 strain. Ethanol production was confirmed by TTC (triphenyl tetrazolium chloride) screening and high-performance liquid chromatography (HPLC). A genetically stable, high ethanol-producing strain that fermented xylose and glucose was obtained following three rounds of genome shuffling. After fermentation for 84 h, the high ethanol-producing S. cerevisiae GS3-10 strain (which utilized 69.48 and 100% of the xylose and glucose stores, respectively) produced 26.65 g/L ethanol, i.e., 47.08% higher than ethanol production by S. cerevisiae W5 (18.12 g/L). The utilization ratios of xylose and glucose were 69.48 and 100%, compared to 14.83 and 100% for...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5658224</comments>
            <pubDate>Tue, 24 Jan 2012 05:00:00 +0100</pubDate>
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        <item>
            <title>Identification and characterization of a novel cold-adapted esterase from a metagenomic library of mountain soil.</title>
            <link>http://www.medworm.com/index.php?rid=5658222&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22270890%26dopt%3DAbstract</link>
            <description>Authors: Ko KC, Rim SO, Han Y, Shin BS, Kim GJ, Choi JH, Song JJ
    Abstract
    A novel lipolytic enzyme was isolated from a metagenomic library after demonstration of lipolytic activity on an LB agar plate containing 1% (w/v) tributyrin. A novel esterase gene (estIM1), encoding a lipolytic enzyme (EstIM1), was cloned using a shotgun method from a pFosEstIM1 clone of the metagenomic library, and the enzyme was characterized. The estIM1 gene had an open reading frame (ORF) of 936 base pairs and encoded a protein of 311 amino acids with a molecular mass 34 kDa and a pI value of 4.32. The deduced amino acid sequence was 62% identical to that of an esterase from an uncultured bacterium (ABQ11271). The amino acid sequence indicated that EstIM1 was a member of the family IV of lipolytic enzym...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5658222</comments>
            <pubDate>Tue, 24 Jan 2012 05:00:00 +0100</pubDate>
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        <item>
            <title>Influence of a triazine derivative-based biocide on microbial biofilms of cutting fluids in contact with different substrates.</title>
            <link>http://www.medworm.com/index.php?rid=5658221&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22270891%26dopt%3DAbstract</link>
            <description>Authors: Lucchesi EG, Eguchi SY, Moraes AM
    Abstract
    Although biofilms are often associated with hospital infection problems owing to their high resistance to antimicrobial agents, in recent years biofilms have also been studied in the industrial sector, mainly because they are a major cause of contamination outbreaks in facilities and products. The aim of this study was to investigate whether different materials commonly found in the metalworking industries have different biofilm formation characteristics when in contact with contaminated cutting fluid as well as to establish an optimal concentration of a triazine-based antimicrobial agent to protect the oil/water emulsion and also to delay or interrupt the development of biofilms. Biofilms grown on the surface of carbon steel, sta...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5658221</comments>
            <pubDate>Sun, 22 Jan 2012 05:00:00 +0100</pubDate>
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        <item>
            <title>Co-transformation of Panax major ginsenosides Rb(1) and Rg          (1) to minor ginsenosides C-K and F          (1) by Cladosporium cladosporioides.</title>
            <link>http://www.medworm.com/index.php?rid=5658225&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22270887%26dopt%3DAbstract</link>
            <description>Co-transformation of Panax major ginsenosides Rb(1) and Rg     (1) to minor ginsenosides C-K and F     (1) by Cladosporium cladosporioides.
    J Ind Microbiol Biotechnol. 2012 Jan 20;
    Authors: Wu L, Jin Y, Yin C, Bai L
    Abstract
    Rb(1) and Rg(1) are the major ginsenosides in protopanaxadiol and protopanaxatriol. Their content in ginsenosides was 23.8 and 17.6%, respectively. A total of 22 isolates of β-glucosidase producing microorganisms were isolated from the soil of a ginseng field using Esculin-R2A agar. Among these isolates, the strain GH21 showed the strongest activities to convert ginsenoside Rb(1) and Rg(1) to minor ginsenosides compound-K and F(1), respectively. Ginsenosides Rb(1) and Rg(1) bioconversion rates were 74.2 and 89.3%, respectively. Meanwhile, the results d...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5658225</comments>
            <pubDate>Fri, 20 Jan 2012 05:00:00 +0100</pubDate>
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        <item>
            <title>Kinetics of sugars consumption and ethanol inhibition in carob pulp fermentation by Saccharomyces cerevisiae in batch and fed-batch cultures.</title>
            <link>http://www.medworm.com/index.php?rid=5658223&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22270889%26dopt%3DAbstract</link>
            <description>Authors: Lima-Costa ME, Tavares C, Raposo S, Rodrigues B, Peinado JM
    Abstract
    The waste materials from the carob processing industry are a potential resource for second-generation bioethanol production. These by-products are small carob kibbles with a high content of soluble sugars (45-50%). Batch and fed-batch Saccharomyces cerevisiae fermentations of high density sugar from carob pods were analyzed in terms of the kinetics of sugars consumption and ethanol inhibition. In all the batch runs, 90-95% of the total sugar was consumed and transformed into ethanol with a yield close to the theoretical maximum (0.47-0.50 g/g), and a final ethanol concentration of 100-110 g/l. In fed-batch runs, fresh carob extract was added when glucose had been consumed. This addition and the subseque...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5658223</comments>
            <pubDate>Fri, 20 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5658223</guid>        </item>
        <item>
            <title>Chemometric modeling and two-dimensional fluorescence analysis of bioprocess with a new strain of Klebsiella pneumoniae to convert residual glycerol into 1,3-propanediol.</title>
            <link>http://www.medworm.com/index.php?rid=5620798&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22252443%26dopt%3DAbstract</link>
            <description>Authors: Rossi DM, Solle D, Hitzmann B, Ayub MA
    Abstract
    The goal of this study was to show that the metabolism of Klebsiella pneumoniae under different aeration strategies could be monitored and predicted by the application of chemometric models and fluorescence spectroscopy. Multi-wavelength fluorescence was applied to the on-line monitoring of process parameters for K.           pneumoniae cultivations. Differences observed in spectra collected under aerobiosis and anaerobiosis can be explained by the different metabolic states of the cells. To predict process variables such as biomass, glycerol, and 1,3-propanediol (1,3-PD), chemometric models were developed on the basis of the acquired fluorescence spectra, which were measured continuously. Although glycerol and 1,3-PD are not...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5620798</comments>
            <pubDate>Wed, 18 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5620798</guid>        </item>
        <item>
            <title>Industrial production of recombinant therapeutics in Escherichia coli and its recent advancements.</title>
            <link>http://www.medworm.com/index.php?rid=5620796&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22252444%26dopt%3DAbstract</link>
            <description>Authors: Huang CJ, Lin H, Yang X
    Abstract
    Nearly 30% of currently approved recombinant therapeutic proteins are produced in Escherichia coli. Due to its well-characterized genetics, rapid growth and high-yield production, E. coli has been a preferred choice and a workhorse for expression of non-glycosylated proteins in the biotech industry. There is a wealth of knowledge and comprehensive tools for E. coli systems, such as expression vectors, production strains, protein folding and fermentation technologies, that are well tailored for industrial applications. Advancement of the systems continues to meet the current industry needs, which are best illustrated by the recent drug approval of E. coli produced antibody fragments and Fc-fusion proteins by the FDA. Even more, recent progre...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5620796</comments>
            <pubDate>Wed, 18 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5620796</guid>        </item>
        <item>
            <title>Minimal polyketide pathway expression in an actinorhodin cluster-deleted and regulation-stimulated Streptomyces coelicolor.</title>
            <link>http://www.medworm.com/index.php?rid=5620795&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22252445%26dopt%3DAbstract</link>
            <description>In this study, we generated a polyketide non-producing strain by deleting the entire actinorhodin cluster from the chromosome of a previously generated S. coelicolor mutant strain, which was shown to stimulate actinorhodin biosynthesis through deletion of two antibiotic downregulators as well as a polyketide precursor flux downregulator (Kim et al. in Appl Environ Microbiol 77:1872-1877, 2011). Using this engineered S. coelicolor mutant strain as a surrogate host, a model minimal polyketide pathway for aloesaponarin II, an actinorhodin shunt product, was cloned in a high-copy conjugative plasmid, followed by functional pathway expression and quantitative metabolite analysis. Aloesaponarin II production was detected only in the presence of a pathway-specific regulatory gene, actII-ORF4, and...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5620795</comments>
            <pubDate>Wed, 18 Jan 2012 05:00:00 +0100</pubDate>
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        <item>
            <title>Extractive fermentation for enhanced production of thailandepsin A from Burkholderia thailandensis E264 using polyaromatic adsorbent resin Diaion HP-20.</title>
            <link>http://www.medworm.com/index.php?rid=5620800&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22246221%26dopt%3DAbstract</link>
            <description>Authors: Liu B, Hui J, Cheng YQ, Zhang X
    Abstract
    Thailandepsin A is natural product of Burkholderia thailandensis E264 with potent histone deacetylase inhibitory activities and promising anticancer activities. The titer of thailandepsin A is very low (less than 10 mg/l) from limited empirical fermentation. To facilitate preclinical evaluations and potentially clinical development of thailandepsin A, systematic optimization and extractive fermentation of thailandepsin A from B. thailandensis E264 culture in flasks were investigated in this pilot study. The main fermentation parameters-28°C, pH 7.0, inoculum ratio 1% (v/v), incubation duration 60 h, medium volume 26%, shaking speed 170 rpm, and chloroform as extracting solvent-were determined by single factor experiments. Polyar...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5620800</comments>
            <pubDate>Sat, 14 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5620800</guid>        </item>
        <item>
            <title>Cloning and characterization of two new thermostable and alkalitolerant α-amylases from the Anoxybacillus species that produce high levels of maltose.</title>
            <link>http://www.medworm.com/index.php?rid=5620799&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22246222%26dopt%3DAbstract</link>
            <description>Authors: Chai YY, Rahman RN, Illias RM, Goh KM
    Abstract
    Two genes that encode α-amylases from two Anoxybacillus species were cloned and expressed in Escherichia coli. The genes are 1,518 bp long and encode 506 amino acids. Both sequences are 98% similar but are distinct from other well-known α-amylases. Both of the recombinant enzymes, ASKA and ADTA, were purified using an α-CD-Sepharose column. They exhibited an optimum activity at 60°C and pH 8. Both amylases were stable at pH 6-10. At 60°C in the absence of Ca(2+), negligible reduction in activity for up to 48 h was observed. The activity half-life at 65°C was 48 and 3 h for ASKA and ADTA, respectively. In the presence of Ca(2+) ions, both amylases were highly stable for at least 48 h and had less than a 10% decrease i...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5620799</comments>
            <pubDate>Sat, 14 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5620799</guid>        </item>
        <item>
            <title>Yeast culture collections of the world: meeting the needs of industrial researchers.</title>
            <link>http://www.medworm.com/index.php?rid=5620801&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22231720%26dopt%3DAbstract</link>
            <description>This article provides information on dozens of yeast collections of the world, profiles of selected yeast culture collections, and the services that they provide: e.g., strain preservation for patent or safe deposit purposes, species identification service, training workshops, and consulting on yeast identification and physiology. Utilization of these services can save industrial researchers valuable time and resources.
    PMID: 22231720 [PubMed - as supplied by publisher] (Source: Journal of Industrial Microbiology and Biotechnology)</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5620801</comments>
            <pubDate>Tue, 10 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5620801</guid>        </item>
        <item>
            <title>Fermentation of crude glycerol from biodiesel production by Clostridium pasteurianum.</title>
            <link>http://www.medworm.com/index.php?rid=5577969&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22212343%26dopt%3DAbstract</link>
            <description>Authors: Jensen TO, Kvist T, Mikkelsen MJ, Christensen PV, Westermann P
    Abstract
    Clostridium pasteurianum can utilize glycerol as the sole carbon source for the production of butanol and 1,3-propanediol. Crude glycerol derived from biodiesel production has been shown to be toxic to the organism even in low concentrations. By examination of different pretreatments we found that storage combined with activated stone carbon addition facilitated the utilization of crude glycerol. A pH-controlled reactor with in situ removal of butanol by gas stripping was used to evaluate the performance. The fermentation pattern on pretreated crude glycerol was quite similar to that on technical grade glycerol. C. pasteurianum was able to utilize 111 g/l crude glycerol. The average consumption rate w...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5577969</comments>
            <pubDate>Tue, 03 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5577969</guid>        </item>
        <item>
            <title>Optimization of ethanol, citric acid, and α-amylase production from date wastes by strains of Saccharomyces cerevisiae, Aspergillus niger, and Candida guilliermondii.</title>
            <link>http://www.medworm.com/index.php?rid=5548877&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22193823%26dopt%3DAbstract</link>
            <description>Authors: Acourene S, Ammouche A
    Abstract
    The present study deals with submerged ethanol, citric acid, and α-amylase fermentation by Saccharomyces cerevisiae SDB, Aspergillus niger ANSS-B5, and Candida guilliermondii CGL-A10, using date wastes as the basal fermentation medium. The physical and chemical parameters influencing the production of these metabolites were optimized. As for the ethanol production, the optimum yield obtained was 136.00 ± 0.66 g/l under optimum conditions of an incubation period of 72 h, inoculum content of 4% (w/v), sugars concentration of 180.0 g/l, and ammonium phosphate concentration of 1.0 g/l. Concerning citric acid production, the cumulative effect of temperature (30°C), sugars concentration of 150.0 g/l, methanol concentration of 3.0%, initi...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5548877</comments>
            <pubDate>Fri, 23 Dec 2011 05:00:00 +0100</pubDate>
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        <item>
            <title>Hydrogen peroxide (H(2)O          (2)) supply significantly improves xanthan gum production mediated by Xanthomonas campestris in vitro.</title>
            <link>http://www.medworm.com/index.php?rid=5533478&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22183692%26dopt%3DAbstract</link>
            <description>Hydrogen peroxide (H(2)O     (2)) supply significantly improves xanthan gum production mediated by Xanthomonas campestris in vitro.
    J Ind Microbiol Biotechnol. 2011 Dec 20;
    Authors: Cheng R, Lin L, Zhang Y
    Abstract
    To improve xanthan gum productivity, a strategy of adding hydrogen peroxide (H(2)O(2)) was studied. The method could intensify oxygen supply through degradation of H(2)O(2) to oxygen (O(2)). In shake flask testing, the xanthan gum yield reached 2.8% (improved by 39.4%) when adding 12.5 mM H(2)O(2) after 24 h of fermentation. In fermentor testing, it was obvious that the oxygen conditions varied with the H(2)O(2) addition time. Eventually, gum yield of 4.2% (w/w) was achieved (increased by 27.3%). Compared with the method of intense mixing and increasing the air...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5533478</comments>
            <pubDate>Tue, 20 Dec 2011 05:00:00 +0100</pubDate>
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        <item>
            <title>Gene cloning, expression, and biochemical characterization of an alkali-tolerant β-mannanase from Humicola                   insolens Y1.</title>
            <link>http://www.medworm.com/index.php?rid=5533480&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22179540%26dopt%3DAbstract</link>
            <description>Gene cloning, expression, and biochemical characterization of an alkali-tolerant β-mannanase from Humicola          insolens Y1.
    J Ind Microbiol Biotechnol. 2011 Dec 18;
    Authors: Luo H, Wang K, Huang H, Shi P, Yang P, Yao B
    Abstract
    In this article, we firstly report a highly alkali-tolerant fungal β-mannanase from Humicola           insolens Y1. The full-length cDNA of the β-mannanase, designated as man5A, has an open reading frame of 1,233 bp that encodes a 411-amino acid polypeptide (Man5A) with a calculated molecular mass of 42.3 kDa. The deduced sequence of Man5A comprises a putative 20-residue signal peptide and a catalytic domain belonging to glycoside hydrolase family 5, and displays 61-85% identities with hypothetical proteins and 32-39% with experimentally ve...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5533480</comments>
            <pubDate>Sun, 18 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5533480</guid>        </item>
        <item>
            <title>Strategies for dephenolization of raw olive mill wastewater by means of Pleurotus ostreatus.</title>
            <link>http://www.medworm.com/index.php?rid=5533479&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22179541%26dopt%3DAbstract</link>
            <description>Authors: Olivieri G, Russo ME, Giardina P, Marzocchella A, Sannia G, Salatino P
    Abstract
    The reduction of polyphenols content in olive mill wastewater (OMW) is a major issue in olive oil manufacturing. Although researchers have pointed out the potential of white-rot fungus in dephenolizing OMW, the results available in the literature mainly concern pretreated (sterilized) OMW. This paper deals with the reduction of polyphenols content in untreated OMW by means of a white-rot fungus, Pleurotus ostreatus. Dephenolization was performed both in an airlift bioreactor and in aerated flasks. The process was carried out under controlled non-sterile conditions, with different operating configurations (batch, continuous, biomass recycling) representative of potential industrial operations. T...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5533479</comments>
            <pubDate>Sun, 18 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5533479</guid>        </item>
        <item>
            <title>Reducing acid in dilute acid pretreatment and the impact on enzymatic saccharification.</title>
            <link>http://www.medworm.com/index.php?rid=5533481&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22167347%26dopt%3DAbstract</link>
            <description>In this study, a dilute acid pretreatment process was developed for the pretreatment of corn stover. The pretreatment was conducted at lower acid levels than the conventional process reported in the literature while using longer residence times. The study indicates that a 50% reduction in acid consumption can be achieved without compromising pretreatment efficiency when the pretreatment time was extended from 1-5 min to 15-20 min. To avoid undesirable sugar degradation and inhibitor generation, temperatures should be controlled below 170°C. When the sulfuric acid-to-lignocellulosic biomass ratio was kept at 0.025 g acid/g dry biomass, a cellulose-to-glucose conversion of 72.7% can be achieved at an enzyme loading of 0.016 g/g corn stover. It was also found that acid loading based on t...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5533481</comments>
            <pubDate>Wed, 14 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5533481</guid>        </item>
        <item>
            <title>Streptomyces temperate bacteriophage integration systems for stable genetic engineering of actinomycetes (and other organisms).</title>
            <link>http://www.medworm.com/index.php?rid=5533482&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22160317%26dopt%3DAbstract</link>
            <description>Authors: Baltz RH
    Abstract
    ϕC31, ϕBT1, R4, and TG1 are temperate bacteriophages with broad host specificity for species of the genus Streptomyces. They form lysogens by integrating site-specifically into diverse attB sites located within individual structural genes that map to the conserved core region of streptomycete linear chromosomes. The target genes containing the ϕC31, ϕBT1, R4, and TG1 attB sites encode a pirin-like protein, an integral membrane protein, an acyl-CoA synthetase, and an aminotransferase, respectively. These genes are highly conserved within the genus Streptomyces, and somewhat conserved within other actinomycetes. In each case, integration is mediated by a large serine recombinase that catalyzes unidirectional recombination between the bacteriophage attP ...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5533482</comments>
            <pubDate>Tue, 13 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5533482</guid>        </item>
        <item>
            <title>Role of peroxisomes in the biosynthesis and secretion of β-lactams and other secondary metabolites.</title>
            <link>http://www.medworm.com/index.php?rid=5533484&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22160272%26dopt%3DAbstract</link>
            <description>This article focuses on new aspects of the metabolic processes occurring in peroxisomes, namely the degradation and detoxification processes that lead to the biosynthesis and secretion of secondary metabolites.
    PMID: 22160272 [PubMed - as supplied by publisher] (Source: Journal of Industrial Microbiology and Biotechnology)</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5533484</comments>
            <pubDate>Sun, 11 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5533484</guid>        </item>
        <item>
            <title>Influence of growth manner on nitrifying bacterial communities and nitrification kinetics in three lab-scale bioreactors.</title>
            <link>http://www.medworm.com/index.php?rid=5533483&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22160273%26dopt%3DAbstract</link>
            <description>Authors: Wang F, Liu Y, Wang J, Zhang Y, Yang H
    Abstract
    The effects of growth type, including attached growth, suspended growth, and combined growth, on the characteristics of communities of ammonia-oxidizing bacteria (AOB) and nitrite-oxidizing bacteria (NOB) were studied in three lab-scale Anaerobic/Anoxic(m)-Oxic(n) (AmOn) systems. These systems amplified activated sludge, biofilms, and a mixture of activated sludge and biofilm (AS-BF). Identical inocula were adopted to analyze the selective effects of mixed growth patterns on nitrifying bacteria. Fluctuations in the concentration of nitrifying bacteria over the 120 days of system operation were analyzed, as was the composition of nitrifying bacterial community in the stabilized stage. Analysis was conducted using polymerase c...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5533483</comments>
            <pubDate>Sun, 11 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5533483</guid>        </item>
        <item>
            <title>Recurrent Aspergillus contamination in a biomedical research facility: a case study.</title>
            <link>http://www.medworm.com/index.php?rid=5533486&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22143434%26dopt%3DAbstract</link>
            <description>Authors: Cornelison CT, Stubblefield B, Gilbert E, Crow SA
    Abstract
    Fungal contamination of biomedical processes and facilities can result in major revenue loss and product delay. A biomedical research facility (BRF) culturing human cell lines experienced recurring fungal contamination of clean room incubators over a 3-year period. In 2010, as part of the plan to mitigate contamination, 20 fungal specimens were isolated by air and swab samples at various locations within the BRF. Aspergillus niger and Aspergillus fumigatus were isolated from several clean-room incubators. A. niger and A. fumigatus were identified using sequence comparison of the 18S rRNA gene. To determine whether the contaminant strains isolated in 2010 were the same as or different from strains isolated between 2...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5533486</comments>
            <pubDate>Tue, 06 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5533486</guid>        </item>
        <item>
            <title>Effects of Tween 80 and pH on mycelial pellets and exopolysaccharide production in liquid culture of a medicinal fungus.</title>
            <link>http://www.medworm.com/index.php?rid=5533485&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22143435%26dopt%3DAbstract</link>
            <description>This study investigated the effects of surfactant additives and medium pH on mycelial morphology and exopolysaccharide (EPS) production in liquid culture of a valuable medicinal fungus Cordyceps sinensis Cs-HK1. In the medium containing 20 g l(-1) glucose and 6 g l(-1) peptone as the sole nitrogen source, the Cs-HK1 fungal mycelia formed smooth and spherical pellets about 1.8-mm mean diameter. The mycelial pellets became less uniform at pH (4.0-5.0) lower than the optimum (pH 6.0) or turned to filamentous form at higher pH (8-9). Surfactants added to the medium inhibited pellet formation, resulting in smaller and looser pellets. Tween 80 exhibited a remarkable promoting effect on EPS production, increasing the EPS yield more than twofold at 1.5% (w/v), which was most probably attribute...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5533485</comments>
            <pubDate>Tue, 06 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5533485</guid>        </item>
        <item>
            <title>Engineered glucose isomerase from Streptomyces sp. SK is resistant to Ca(2+) inhibition and Co          (2+) independent.</title>
            <link>http://www.medworm.com/index.php?rid=5533487&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22139345%26dopt%3DAbstract</link>
            <description>Engineered glucose isomerase from Streptomyces sp. SK is resistant to Ca(2+) inhibition and Co     (2+) independent.
    J Ind Microbiol Biotechnol. 2011 Dec 4;
    Authors: Ben Hlima H, Aghajari N, Ben Ali M, Haser R, Bejar S
    Abstract
    The role of two amino acid residues linked to the two catalytic histidines His54 and His220 in kinetics and physicochemical properties of the Streptomyces sp. SK glucose isomerase (SKGI) was investigated by site-directed mutagenesis and molecular modeling. Two single mutations, F53L and G219D, and a double mutation F53L/G219D was introduced into the xylA SKGI gene. The F53L mutation increases the thermostability and the catalytic efficiency and also slightly shifts the optimum pH from 6.5 to 7, but displays a profile being similar to that of the wild...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5533487</comments>
            <pubDate>Sun, 04 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5533487</guid>        </item>
        <item>
            <title>Ethanol production from alkali-treated rice straw via simultaneous saccharification and fermentation using newly isolated thermotolerant Pichia kudriavzevii HOP-1.</title>
            <link>http://www.medworm.com/index.php?rid=5533488&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22131104%26dopt%3DAbstract</link>
            <description>In this study, simultaneous saccharification and fermentation (SSF) was employed to produce ethanol from 1% sodium hydroxide-treated rice straw in a thermostatically controlled glass reactor using 20 FPU gds(-1) cellulase, 50 IU gds(-1) β-glucosidase, 15 IU gds(-1) pectinase and a newly isolated thermotolerant Pichia kudriavzevii HOP-1 strain. Scanning electron micrograph images showed that the size of the P. kudriavzevii cells ranged from 2.48 to 6.93 μm in diameter while the shape of the cells varied from oval, ellipsoidal to elongate. Pichia kudriavzevii cells showed extensive pseudohyphae formation after 5 days of growth and could assimilate sugars like glucose, sucrose, galactose, fructose, and mannose but the cells could not assimilate xylose, arabinose, cellobiose, raffinose,...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5533488</comments>
            <pubDate>Thu, 01 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5533488</guid>        </item>
        <item>
            <title>Comparative metabolic profiling to investigate the contribution of O. oeni MLF starter cultures to red wine composition.</title>
            <link>http://www.medworm.com/index.php?rid=5533491&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22120647%26dopt%3DAbstract</link>
            <description>This study provided insight into metabolism in O. oeni starter cultures during MLF in red wine.
    PMID: 22120647 [PubMed - as supplied by publisher] (Source: Journal of Industrial Microbiology and Biotechnology)</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5533491</comments>
            <pubDate>Sat, 26 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5533491</guid>        </item>
        <item>
            <title>Microwave-assisted enzymatic synthesis of beef tallow biodiesel.</title>
            <link>http://www.medworm.com/index.php?rid=5533490&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22120648%26dopt%3DAbstract</link>
            <description>Authors: Da Rós PC, de Castro HF, Carvalho AK, Soares CM, de Moraes FF, Zanin GM
    Abstract
    Optimal conditions for the microwave-assisted enzymatic synthesis of biodiesel have been developed by a full 2(2) factorial design leading to a set of seven runs with different combinations of molar ratio and temperature. The main goal was to reduce the reaction time preliminarily established by a process of conventional heating. Reactions yielding biodiesel, in which beef tallow and ethanol used as raw materials were catalyzed by lipase from Burkholderia cepacia immobilized on silica-PVA and microwave irradiations within the range of 8-15 W were performed to reach the reaction temperature. Under optimized conditions (1:6 molar ratio of beef tallow to ethanol molar ratio at 50°C) almost tot...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5533490</comments>
            <pubDate>Sat, 26 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5533490</guid>        </item>
        <item>
            <title>Green and efficient production of octyl hydroxyphenylpropionate using an ultrasound-assisted packed-bed bioreactor.</title>
            <link>http://www.medworm.com/index.php?rid=5533489&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22120649%26dopt%3DAbstract</link>
            <description>Authors: Lee CC, Chen HC, Ju HY, Chen JH, Kuo CH, Chung YL, Liu YC, Shieh CJ
    Abstract
    A solvent-free system to produce octyl hydroxyphenylpropionate (OHPP) from p-hydroxyphenylpropionic acid (HPPA) and octanol using immobilized lipase (Novozym(®) 435) as a catalyst in an ultrasound-assisted packed-bed bioreactor was investigated. Response-surface methodology (RSM) and a three-level-three-factor Box-Behnken design were employed to evaluate the effects of reaction temperature (x           (1)), flow rate (x           (2)) and ultrasonic power (x           (3)) on the percentage of molar production of OHPP. The results indicate that the reaction temperature and flow rate were the most important variables in optimizing the production of OHPP. Based on a ridge max analysis, the optimum...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5533489</comments>
            <pubDate>Sat, 26 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5533489</guid>        </item>
        <item>
            <title>Bacterial glyphosate resistance conferred by overexpression of an E. coli membrane efflux transporter.</title>
            <link>http://www.medworm.com/index.php?rid=5439832&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22089966%26dopt%3DAbstract</link>
            <description>We report here that an alternative mode of glyphosate resistance in E. coli is due to reduced accumulation of glyphosate in cells that overexpress this membrane transporter and discuss the implications for potential alternative resistance mechanisms in other organisms such as plants.
    PMID: 22089966 [PubMed - as supplied by publisher] (Source: Journal of Industrial Microbiology and Biotechnology)</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5439832</comments>
            <pubDate>Thu, 17 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5439832</guid>        </item>
        <item>
            <title>Hydrothermal pretreatment of sugarcane bagasse using response surface methodology improves digestibility and ethanol production by SSF.</title>
            <link>http://www.medworm.com/index.php?rid=5419033&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22080307%26dopt%3DAbstract</link>
            <description>Authors: da Cruz SH, Dien BS, Nichols NN, Saha BC, Cotta MA
    Abstract
    Sugarcane bagasse was characterized as a feedstock for the production of ethanol using hydrothermal pretreatment. Reaction temperature and time were varied between 160 and 200°C and 5-20 min, respectively, using a response surface experimental design. The liquid fraction was analyzed for soluble carbohydrates and furan aldehydes. The solid fraction was analyzed for structural carbohydrates and Klason lignin. Pretreatment conditions were evaluated based on enzymatic extraction of glucose and xylose and conversion to ethanol using a simultaneous saccharification and fermentation scheme. SSF experiments were conducted with the washed pretreated biomass. The severity of the pretreatment should be sufficient to drive...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5419033</comments>
            <pubDate>Sat, 12 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5419033</guid>        </item>
        <item>
            <title>Optical mapping and sequencing of the Escherichia coli KO11 genome reveal extensive chromosomal rearrangements, and multiple tandem copies of the Zymomonas mobilis                   pdc and adhB genes.</title>
            <link>http://www.medworm.com/index.php?rid=5419035&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22075923%26dopt%3DAbstract</link>
            <description>Optical mapping and sequencing of the Escherichia coli KO11 genome reveal extensive chromosomal rearrangements, and multiple tandem copies of the Zymomonas mobilis          pdc and adhB genes.
    J Ind Microbiol Biotechnol. 2011 Nov 11;
    Authors: Turner PC, Yomano LP, Jarboe LR, York SW, Baggett CL, Moritz BE, Zentz EB, Shanmugam KT, Ingram LO
    Abstract
    Escherichia coli KO11 (ATCC 55124) was engineered in 1990 to produce ethanol by chromosomal insertion of the Zymomonas mobilis           pdc and adhB genes into E. coli W (ATCC 9637). KO11FL, our current laboratory version of KO11, and its parent E. coli W were sequenced, and contigs assembled into genomic sequences using optical NcoI restriction maps as templates. E. coli W contained plasmids pRK1 (102.5 kb) and pRK2 (5.4 kb),...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5419035</comments>
            <pubDate>Fri, 11 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5419035</guid>        </item>
        <item>
            <title>Effect of modified glucose catabolism on xanthan production in Xanthomonas oryzae pv. oryzae.</title>
            <link>http://www.medworm.com/index.php?rid=5419034&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22075924%26dopt%3DAbstract</link>
            <description>In this study, the glucose 6-phosphate dehydrogenase gene (XOO2314) was inactivated in order to modulate the intracellular glucose 6-phosphate, and its effects on xanthan production in a wild-type strain of Xanthomonas oryzae were evaluated. The intracellular glucose 6-phosphate was increased from 17.6 to 99.4 μmol g(-1) (dry cell weight) in the gene-disrupted mutant strain. The concomitant increase in the glucose 6-phosphate was accompanied by an increase in xanthan production of up to 2.23 g l(-1) (culture medium). However, in defined medium supplemented with 0.4% glucose, the growth rate of the mutant strain was reduced to 52.9% of the wild-type level. Subsequently, when a family B ATP-dependent phosphofructokinase from Escherichia coli was overexpressed in the mutant strain, the g...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5419034</comments>
            <pubDate>Fri, 11 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5419034</guid>        </item>
        <item>
            <title>Production of multiple extracellular enzyme activities by novel submerged culture of Aspergillus kawachii for ethanol production from raw cassava flour.</title>
            <link>http://www.medworm.com/index.php?rid=5419038&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22072435%26dopt%3DAbstract</link>
            <description>Authors: Sugimoto T, Makita T, Watanabe K, Shoji H
    Abstract
    Cassava is a starch-containing root crop that is widely used as a raw material in a variety of industrial applications, most recently in the production of fuel ethanol. In the present study, ethanol production from raw (uncooked) cassava flour by simultaneous saccharification and fermentation (SSF) using a preparation consisting of multiple enzyme activities from Aspergillus kawachii FS005 was investigated. The multi-activity preparation was obtained from a novel submerged fermentation broth of A. kawachii FS005 grown on unmilled crude barley as a carbon source. The preparation was found to consist of glucoamylase, acid-stable α-amylase, acid carboxypeptidase, acid protease, cellulase and xylanase activities, and exhibite...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5419038</comments>
            <pubDate>Thu, 10 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5419038</guid>        </item>
        <item>
            <title>Characterization of alginate lyase gene using a metagenomic library constructed from the gut microflora of abalone.</title>
            <link>http://www.medworm.com/index.php?rid=5419037&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22072436%26dopt%3DAbstract</link>
            <description>Authors: Sim SJ, Baik KS, Park SC, Choe HN, Seong CN, Shin TS, Woo HC, Cho JY, Kim D
    Abstract
    A metagenomic fosmid library was constructed using a genomic DNA mixture extracted from the gut microflora of abalone. The library gave an alginate lyase positive clone (AlyDW) harboring a 31.7-kbp insert. The AlyDW insert consisted of 22 open reading frames (ORFs). The deduced amino acid sequences of ORFs 11-13 were similar to those of known alginate lyase genes, which are found adjacent in the genome of Klebsiella pneumoniae subsp. aerogenes, Vibrio splendidus, and Vibrio sp. belonging to the phylum Gammaproteobacteria. Among the three recombinant proteins expressed from the three ORFs, alginate lyase activity was only observed in the recombinant protein (AlyDW11) coded by ORF 11. The ex...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5419037</comments>
            <pubDate>Thu, 10 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5419037</guid>        </item>
        <item>
            <title>Alginate production and alg8 gene expression by Azotobacter vinelandii in continuous cultures.</title>
            <link>http://www.medworm.com/index.php?rid=5419036&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22072437%26dopt%3DAbstract</link>
            <description>The objective of this study was to evaluate the effects of agitation rate and inlet sucrose concentrations (ISC) on alginate production and the expression of the genes encoding for alginate-lyases (algL) and the catalytic subunit of the alginate polymerase complex (alg8) in chemostat cultures of Azotobacter vinelandii ATCC 9046. Increased alginate production (2.4 g l(-1)) and a higher specific alginate production rate (0.1 g g(-1) h(-1)) were obtained at an ISC of 15 g l(-1). Carbon recovery of about 100% was obtained at an ISC of 10 g l(-1), whereas it was close to 50% at higher ISCs, suggesting that cells growing at lower sucrose feed rates utilize the carbon source more efficiently. In each of the steady states evaluated, an increase in algL gene expression was not related to a...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5419036</comments>
            <pubDate>Thu, 10 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5419036</guid>        </item>
        <item>
            <title>Kinetic modeling of rapid enzymatic hydrolysis of crystalline cellulose after pretreatment by NMMO.</title>
            <link>http://www.medworm.com/index.php?rid=5379359&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22052078%26dopt%3DAbstract</link>
            <description>Authors: Khodaverdi M, Jeihanipour A, Karimi K, Taherzadeh MJ
    Abstract
    Pretreatment of cellulose with an industrial cellulosic solvent, N-methylmorpholine-N-oxide, showed promising results in increasing the rate of subsequent enzymatic hydrolysis. Cotton linter was used as high crystalline cellulose. After the pretreatment, the cellulose was almost completely hydrolyzed in less than 12 h, using low enzyme loading (15 FPU/g cellulose). The pretreatment significantly decreased the total crystallinity of cellulose from 7.1 to 3.3, and drastically increased the enzyme adsorption capacity of cellulose by approximately 42 times. A semi-mechanistic model was used to describe the relationship between the cellulose concentration and the enzyme loading. In this model, two reactions for het...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5379359</comments>
            <pubDate>Fri, 04 Nov 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5379359</guid>        </item>
        <item>
            <title>Recombinatorial biosynthesis of polyketides.</title>
            <link>http://www.medworm.com/index.php?rid=5379360&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22042517%26dopt%3DAbstract</link>
            <description>Authors: Starcevic A, Wolf K, Diminic J, Zucko J, Ruzic IT, Long PF, Hranueli D, Cullum J
    Abstract
    Modular polyketide synthases (PKSs) from Streptomyces and related genera of bacteria produce many important pharmaceuticals. A program called CompGen was developed to carry out in silico homologous recombination between gene clusters encoding PKSs and determine whether recombinants have cluster architectures compatible with the production of polyketides. The chemical structure of recombinant polyketides was also predicted. In silico recombination was carried out for 47 well-characterised clusters. The predicted recombinants would produce 11,796 different polyketide structures. The molecular weights and average degree of reduction of the chemical structures are dispersed around the par...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5379360</comments>
            <pubDate>Tue, 01 Nov 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5379360</guid>        </item>
        <item>
            <title>Prediction of ketoacyl synthase family using reduced amino acid alphabets.</title>
            <link>http://www.medworm.com/index.php?rid=5379361&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22042516%26dopt%3DAbstract</link>
            <description>Authors: Chen W, Feng P, Lin H
    Abstract
    Ketoacyl synthases are enzymes involved in fatty acid synthesis and can be classified into five families based on primary sequence similarity. Different families have different catalytic mechanisms. Developing cost-effective computational models to identify the family of ketoacyl synthases will be helpful for enzyme engineering and in knowing individual enzymes' catalytic mechanisms. In this work, a support vector machine-based method was developed to predict ketoacyl synthase family using the n-peptide composition of reduced amino acid alphabets. In jackknife cross-validation, the model based on the 2-peptide composition of a reduced amino acid alphabet of size 13 yielded the best overall accuracy of 96.44% with average accuracy of 93.36%, w...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5379361</comments>
            <pubDate>Wed, 26 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5379361</guid>        </item>
        <item>
            <title>Freshwater diatoms as a source of lipids for biofuels.</title>
            <link>http://www.medworm.com/index.php?rid=5360988&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22009056%26dopt%3DAbstract</link>
            <description>We examined four genera (Cyclotella, Aulacoseira, Fragilaria, Synedra) of common freshwater diatoms (Bacillariophyceae) for growth and lipid content in defined medium (sD11) that replicates hypereutrophic conditions in lakes and wastewater treatment plant effluents and optimized the medium for silicon content. Cyclotella and Aulacoseira produced the highest levels of total lipids, 60 and 43 μg total lipids/ml, respectively. Both diatoms are rich in fatty acids C14, C16, C16:1, C16:2,7,10, and C22:5n3. Of the diatoms examined, Cyclotella reached the highest population density (&amp;gt;2.5 × 10(6) cells/ml) in stationary phase when many of the cells appeared to be filled entirely with oil. Silicon enrichment studies indicated that for optimal utilization of phosphorus and nitrogen by diatom...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5360988</comments>
            <pubDate>Wed, 19 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5360988</guid>        </item>
        <item>
            <title>Heterologous and homologous expression of the arginine biosynthetic argC~H cluster from Corynebacterium                   crenatum for improvement of L: -arginine production.</title>
            <link>http://www.medworm.com/index.php?rid=5360987&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22009057%26dopt%3DAbstract</link>
            <description>This study provides a kind of Corynebacteria with improved L: -arginine-producing ability and an efficient elevation for producing amino acid. Moreover, the promoter Parg would be used as a valid promoter to express objective genes for metabolic engineering in Corynebacteria.
    PMID: 22009057 [PubMed - as supplied by publisher] (Source: Journal of Industrial Microbiology and Biotechnology)</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5360987</comments>
            <pubDate>Wed, 19 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5360987</guid>        </item>
        <item>
            <title>An investigation of agitation speed as a factor affecting the quantity and monomer distribution of alginate from Azotobacter vinelandii ATCC(®) 9046.</title>
            <link>http://www.medworm.com/index.php?rid=5360986&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22009058%26dopt%3DAbstract</link>
            <description>Authors: Kıvılcımdan Moral C, Sanin FD
    Abstract
    Alginate is a copolymer of β-D: -mannuronic and α-L: -guluronic acids. Distribution of these monomers in the alginate structure is one of the important characteristics that affect the commercial value of the polymer. In the present work, the effect of agitation speed in the range of 200-700 rpm on alginate production by Azotobacter vinelandii ATCC(®) 9046 was investigated at a dissolved oxygen tension of 5% of air saturation. Experiments were conducted in a fermentor operated in batch mode for 72 h while the production of biomass and alginate, the consumption of substrate and the change in culture broth viscosity and monomer distribution of the polymer were monitored. Results showed that the growth rate of the bacteria increas...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5360986</comments>
            <pubDate>Wed, 19 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5360986</guid>        </item>
        <item>
            <title>Optimization of glucose feeding approaches for enhanced glucosamine and N-acetylglucosamine production by an engineered Escherichia coli.</title>
            <link>http://www.medworm.com/index.php?rid=5360985&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22009059%26dopt%3DAbstract</link>
            <description>Authors: Chen X, Liu L, Li J, Liu J, Du G, Chen J
    Abstract
    In this work, a recombinant Escherichia coli was constructed by overexpressing glucosamine (GlcN) synthase and GlcN-6-P N-acetyltransferase for highly efficient production of GlcN and N-acetylglucosamine (GlcNAc). For further enhancement of GlcN and GlcNAc production, the effects of different glucose feeding strategies including constant-rate feeding, interval feeding, and exponential feeding on GlcN and GlcNAc production were investigated. The results indicated that exponential feeding resulted in relatively high cell growth rate and low acetate formation rate, while constant feeding contributed to the highest specific GlcN and GlcNAc production rate. Based on this, a multistage glucose supply approach was proposed to enha...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5360985</comments>
            <pubDate>Wed, 19 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5360985</guid>        </item>
        <item>
            <title>Protein engineering towards natural product synthesis and diversification.</title>
            <link>http://www.medworm.com/index.php?rid=5360989&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22006344%26dopt%3DAbstract</link>
            <description>Authors: Zabala AO, Cacho RA, Tang Y
    Abstract
    A dazzling array of enzymes is used by nature in making structurally complex natural products. These enzymes constitute a molecular toolbox that may be used in the construction and fine-tuning of pharmaceutically active molecules. Aided by technological advancements in protein engineering, it is now possible to tailor the activities and specificities of these enzymes as biocatalysts in the production of both natural products and their unnatural derivatives. These efforts are crucial in drug discovery and development, where there is a continuous quest for more potent agents. Both rational and random evolution techniques have been utilized in engineering these enzymes. This review will highlight some examples from several large families o...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5360989</comments>
            <pubDate>Tue, 18 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5360989</guid>        </item>
        <item>
            <title>Soluble expression of recombinant human CD137 ligand in Escherichia coli by co-expression of chaperones.</title>
            <link>http://www.medworm.com/index.php?rid=5325861&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21997275%26dopt%3DAbstract</link>
            <description>In this study, the effects of five different chaperone teams on the soluble expression of recombinant human CD137L protein were explored and analyzed. The poor expression of CD137L in the cytoplasm of E. coli was improved significantly by co-expression of chaperone GroES-GroEL-Tf. After dual induction and affinity chromatography, purified recombinant CD137L was obtained at a yield of 3 mg protein per liter with purity greater than 98% from original undetectable level. Additionally, the purified recombinant CD137L could bind CD137-positive cells in a dose-dependent manner, markedly promote the growth of activated mice T cells, and elevate the release of IL-2. The present work provides an effective system for soluble expression of functional human co-stimulatory molecule CD137L, which will ...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5325861</comments>
            <pubDate>Sat, 15 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5325861</guid>        </item>
        <item>
            <title>Production of polyhydroxyalkanoates by Burkholderia cepacia ATCC 17759 using a detoxified sugar maple hemicellulosic hydrolysate.</title>
            <link>http://www.medworm.com/index.php?rid=5277416&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21953365%26dopt%3DAbstract</link>
            <description>Authors: Pan W, Perrotta JA, Stipanovic AJ, Nomura CT, Nakas JP
    Abstract
    Sugar maple hemicellulosic hydrolysate containing 71.9 g/l of xylose was used as an inexpensive feedstock to produce polyhydroxyalkanoates (PHAs) by Burkholderia cepacia ATCC 17759. Several inhibitory compounds present in wood hydrolysate were analyzed for effects on cell growth and PHA production with strong inhibition observed at concentrations of 1 g/l furfural, 2 g/l vanillin, 7 g/l levulinic acid, and 1 M acetic acid. Gradual catabolism of lower concentrations of these inhibitors was observed in this study. To increase the fermentability of wood hydrolysate, several detoxification methods were tested. Overliming combined with low-temperature sterilization resulted in the highest removal of total inhi...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5277416</comments>
            <pubDate>Wed, 28 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5277416</guid>        </item>
        <item>
            <title>Microbial utilization of crude glycerol for the production of value-added products.</title>
            <link>http://www.medworm.com/index.php?rid=5277417&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21948485%26dopt%3DAbstract</link>
            <description>Authors: Dobson R, Gray V, Rumbold K
    Abstract
    Energy fuels for transportation and electricity generation are mainly derived from finite and declining reserves of fossil hydrocarbons. Fossil hydrocarbons are also used to produce a wide range of organic carbon-based chemical products. The current global dependency on fossil hydrocarbons will not be environmentally or economically sustainable in the long term. Given the future pessimistic prospects regarding the complete dependency on fossil fuels, political and economic incentives to develop carbon neutral and sustainable alternatives to fossil fuels have been increasing throughout the world. For example, interest in biodiesel has undergone a revival in recent times. However, the disposal of crude glycerol contaminated with methanol,...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5277417</comments>
            <pubDate>Sun, 25 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5277417</guid>        </item>
        <item>
            <title>Cloning and bioinformatics analysis of an endoglucanase gene (Aucel12A) from Aspergillus usamii and its functional expression in Pichia pastoris.</title>
            <link>http://www.medworm.com/index.php?rid=5246279&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21935697%26dopt%3DAbstract</link>
            <description>Authors: Shi H, Yin X, Wu M, Tang C, Zhang H, Li J
    Abstract
    Using 3' and 5' rapid amplification of cDNA ends methods, the full-length cDNA sequence encoding an endo-1,4-β-glucanase of Aspergillus usamii E001 (abbreviated as AuCel12A) was amplified from the total RNA. The clone cDNA sequence of the gene encoding the AuCel12A, named as Aucel12A, is 1,027 bp in length harboring 5' and 3' non-coding regions, as well as a 720 bp of open reading frame that encodes a 16-aa signal peptide, and a 223-aa mature AuCel12A with a theoretical M.W. of 24,294 Da, a calculated pI of 4.15, and one putative N-glycosylation site. The complete DNA sequence of the gene Aucel12A was amplified from the genomic DNA of A. usamii E001 by using the conventional PCR and pUCm-T vector-mediated PCR initially...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5246279</comments>
            <pubDate>Wed, 21 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5246279</guid>        </item>
        <item>
            <title>Diatomaceous earth as a protective vehicle for bacteria applied for self-healing concrete.</title>
            <link>http://www.medworm.com/index.php?rid=5246280&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21927907%26dopt%3DAbstract</link>
            <description>Authors: Wang JY, De Belie N, Verstraete W
    Abstract
    Crack repair is crucial since cracks are the main cause for the decreased service life of concrete structures. An original and promising way to repair cracks is to pre-incorporate healing agents inside the concrete matrix to heal cracks the moment they appear. Thus, the concrete obtains self-healing properties. The goal of our research is to apply bacterially precipitated CaCO(3) to heal cracks in concrete since the microbial calcium carbonate is more compatible with the concrete matrix and more environmentally friendly relative to the normally used polymeric materials. Diatomaceous earth (DE) was used in this study to protect bacteria from the high-pH environment of concrete. The experimental results showed that DE had a very goo...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5246280</comments>
            <pubDate>Sat, 17 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5246280</guid>        </item>
        <item>
            <title>Enhanced enzyme production with the pelleted form of D. squalens in laboratory bioreactors using added natural lignin inducer.</title>
            <link>http://www.medworm.com/index.php?rid=5229080&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21922328%26dopt%3DAbstract</link>
            <description>Authors: Babič J, Pavko A
    Abstract
    White-rot fungi are extensively used in various submerged biotechnology processes to produce ligninolytic enzymes. Transfer of the process from the laboratory to the industrial level requires optimization of the cultivation conditions on the laboratory scale. An interesting area of optimization is pellet growth since this morphological form solves problems such as the decreased oxygen concentration, limited heat, and nutrient transport, which usually occur in dispersed mycelium cultures. Many submerged fermentations with basidiomycetes in pellet form were done with Phanerochaete, Trametes, and Bjerkandera species, among others. In our study, another promising basidiomycete, D. squalens, was used for ligninolytic enzyme production. With the additi...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5229080</comments>
            <pubDate>Fri, 16 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5229080</guid>        </item>
        <item>
            <title>Introduction of subdivisions.</title>
            <link>http://www.medworm.com/index.php?rid=5218562&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21909700%26dopt%3DAbstract</link>
            <description>Authors: Schwartz RD
    PMID: 21909700 [PubMed - as supplied by publisher] (Source: Journal of Industrial Microbiology and Biotechnology)</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5218562</comments>
            <pubDate>Sat, 10 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5218562</guid>        </item>
        <item>
            <title>Increasing recombinant protein production in Escherichia coli through metabolic and genetic engineering.</title>
            <link>http://www.medworm.com/index.php?rid=5218563&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21901404%26dopt%3DAbstract</link>
            <description>Authors: Waegeman H, Soetaert W
    Abstract
    Different hosts have been used for recombinant protein production, ranging from simple bacteria, such as Escherichia coli and Bacillus subtilis, to more advanced eukaryotes as Saccharomyces cerevisiae and Pichia pastoris, to very complex insect and animal cells. All have their advantages and drawbacks and not one seems to be the perfect host for all purposes. In this review we compare the characteristics of all hosts used in commercial applications of recombinant protein production, both in the area of biopharmaceuticals and industrial enzymes. Although the bacterium E. coli remains a very often used organism, several drawbacks limit its possibility to be the first-choice host. Furthermore, we show what E. coli strains are typically used in ...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5218563</comments>
            <pubDate>Thu, 08 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5218563</guid>        </item>
        <item>
            <title>Screening, cultivation, and biocatalytic performance of Rhodococcus boritolerans FW815 with strong 2,2-dimethylcyclopropanecarbonitrile hydratase activity.</title>
            <link>http://www.medworm.com/index.php?rid=5218565&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21892773%26dopt%3DAbstract</link>
            <description>Authors: Wang YJ, Liu ZQ, Zheng RC, Xue YP, Zheng YG
    Abstract
    In this work, a mild, efficient bioconversion of 2,2-dimethylcyclopropanecarbonitrile (DMCPCN) to 2,2-dimethylcyclopropanecarboxamide (DMCPCA) in distilled water system was developed. The isolate FW815 was screened using the enrichment culture technique, displaying strong DMCPCN hydratase activity, and was identified as Rhodococcus boritolerans based on morphological, physiological, biochemical tests and 16S rRNA gene sequencing. Cultivation outcomes indicated that R. boritolerans FW815 was a neutrophile, with a growth optimum of 28-32°C; its DMCPCN hydratase belonged to the Fe-type family, and was most active at 38-42°C, pH 7.0, with maximal activity of 4.51 × 10(4) U g(-1) DCW. R. boritolerans FW815 was found t...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5218565</comments>
            <pubDate>Sun, 04 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5218565</guid>        </item>
        <item>
            <title>Characterization of Candida sp. NY7122, a novel pentose-fermenting soil yeast.</title>
            <link>http://www.medworm.com/index.php?rid=5218564&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21898112%26dopt%3DAbstract</link>
            <description>Authors: Watanabe I, Ando A, Nakamura T
    Abstract
    Yeasts that ferment both hexose and pentose are important for cost-effective ethanol production. We found that the soil yeast strain NY7122 isolated from a blueberry field in Tsukuba (East Japan) could ferment both hexose and pentose (D: -xylose and L: -arabinose). NY7122 was closely related to Candida subhashii on the basis of the results of molecular identification using the sequence in the D1/D2 domains of 26S rDNA and 5.8S-internal transcribed spacer region. NY7122 produced at least 7.40 and 3.86 g l(-1) ethanol from 20 g l(-1) D: -xylose and L: -arabinose within 24 h. NY7122 could produce ethanol from pentose and hexose sugars at 37°C. The highest ethanol productivity of NY7122 was achieved under a low pH condition (pH 3.5...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5218564</comments>
            <pubDate>Sun, 04 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5218564</guid>        </item>
        <item>
            <title>Microalgae as platforms for production of recombinant proteins and valuable compounds: progress and prospects.</title>
            <link>http://www.medworm.com/index.php?rid=5192566&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21882013%26dopt%3DAbstract</link>
            <description>Authors: Gong Y, Hu H, Gao Y, Xu X, Gao H
    Abstract
    Over the last few years microalgae have gained increasing interest as a natural source of valuable compounds and as bioreactors for recombinant protein production. Natural high-value compounds including pigments, long-chain polyunsaturated fatty acids, and polysaccharides, which have a wide range of applications in the food, feed, cosmetics, and pharmaceutical industries, are currently produced with nontransgenic microalgae. However, transgenic microalgae can be used as bioreactors for the production of therapeutic and industrially relevant recombinant proteins. This technology shows great promise to simplify the production process and significantly decrease the production costs. To date, a variety of recombinant proteins have been...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5192566</comments>
            <pubDate>Wed, 31 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5192566</guid>        </item>
        <item>
            <title>Biotransformation of puerarin into puerarin-6″-O-phosphate by Bacillus cereus.</title>
            <link>http://www.medworm.com/index.php?rid=5192565&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21882014%26dopt%3DAbstract</link>
            <description>Authors: Yu L, Gao F, Yang L, Xu L, Wang Z, Ye H
    Abstract
    The biotransformation of puerarin catalyzed by Bacillus cereus NT02 was studied. A primary screening was carried out using 307 strains of bacteria isolated from soil which were able to grow in the presence of puerarin. Strain NT02, identified as B. cereus, was able to convert puerarin into puerarin-6″-O-phosphate. Under the optimum conditions, resting cells of B. cereus NT02 converted 27% of added 0.4 g/l puerarin into puerarin-6″-O-phosphate that was characterized by MS, (13)C NMR, (31)P NMR. The activity of puerarin-6″-O-phosphate was 25 times higher than that of puerarin in the 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical-scavenging system. The water solubility of puerarin-6″-O-phosphate was 85.4 times higher tha...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5192565</comments>
            <pubDate>Wed, 31 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5192565</guid>        </item>
        <item>
            <title>Scale-down assessment of the sensitivity of Yarrowia lipolytica to oxygen transfer and foam management in bioreactors: investigation of the underlying physiological mechanisms.</title>
            <link>http://www.medworm.com/index.php?rid=5192568&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21879355%26dopt%3DAbstract</link>
            <description>Authors: Kar T, Destain J, Thonart P, Delvigne F
    Abstract
    A scale-down investigation of the impact of local dissolved oxygen limitation on lipase production by Y. lipolytica has been performed. One of the major issues encountered during this kind of process is foam formation, requiring a reduction of the overall oxygen transfer efficiency of the system in order to keep antifoam consumption to a reasonable level. A regulation strategy involving oxygen enrichment of the air flow through the reactor has allowed this issue to be partly overcome. For a second time, the scale dependency of the process operated with air enrichment has been investigated by a combination of scale-down and pilot-scale cultivation tests. The scale-down apparatus considered in this work comprised a well-mixed...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5192568</comments>
            <pubDate>Tue, 30 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5192568</guid>        </item>
        <item>
            <title>Encapsulation of R. planticola Rs-2 from alginate-starch-bentonite and its controlled release and swelling behavior under simulated soil conditions.</title>
            <link>http://www.medworm.com/index.php?rid=5192567&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21879356%26dopt%3DAbstract</link>
            <description>Authors: Wu Z, Guo L, Qin S, Li C
    Abstract
    The plant growth-promoting bacteria (PGPR) Raoultella planticola Rs-2 was encapsulated with the various blends of alginate, starch, and bentonite for development of controlled-release formulations. The stability and release characteristics of these different capsule formulations were evaluated. The entrapment efficiency of Rs-2 in the beads (capsules) was more than 99%. The diameter of dry beads ranged from 0.98 to 1.41 mm. The bacteria release efficiency, swelling ratio, and biodegradability of the different bead formulations were enhanced by increasing the starch or alginate contents, but were impeded by higher bentonite content. The release kinetics of viable cells from capsules and the swelling ratio of capsules were studied in simula...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5192567</comments>
            <pubDate>Tue, 30 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5192567</guid>        </item>
        <item>
            <title>Immobilization of Candida rugosa lipase on poly(3-hydroxybutyrate-co-hydroxyvalerate): a new eco-friendly support.</title>
            <link>http://www.medworm.com/index.php?rid=5175031&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21870100%26dopt%3DAbstract</link>
            <description>Authors: Cabrera-Padilla RY, Lisboa MC, Fricks AT, Franceschi E, Lima AS, Silva DP, Soares CM
    Abstract
    The overall objective of this study is to evaluate the morphological [scanning electron microscopy (SEM)], physicochemical [differential scanning calorimetry (DSC), thermogravimetric analysis (TGA), chemical composition analysis, Fourier-transform infrared spectroscopy (FTIR), nuclear magnetic resonance (NMR)], and biochemical properties of Candida rugosa lipase (CRL) immobilized on a natural biopolymer poly(3-hydroxybutyrate-co-hydroxyvalerate) (PHBV) in aqueous solution. CRL was immobilized by physical adsorption with efficiency of 30%. Compared with free CRL enzyme, there were slight changes in immobilized CRL activity as a function of temperature (from 37°C to 45°C), but a s...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5175031</comments>
            <pubDate>Thu, 25 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5175031</guid>        </item>
        <item>
            <title>Expression of cefF significantly decreased deacetoxycephalosporin C formation during cephalosporin C production in Acremonium chrysogenum.</title>
            <link>http://www.medworm.com/index.php?rid=5175032&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21866341%26dopt%3DAbstract</link>
            <description>In this study, the DAOC hydroxylase gene cefF was cloned from Streptomyces clavuligerus and introduced into Acremonium chrysogenum through Agrobacterium tumefaciens-mediated transformation. When cefF was expressed under the promoter of pcbC, the ratio of DAOC/CPC in the fermentation broth significantly decreased. These results suggested that introduction of cefF could function quite well in Acremonium chrysogenum and successfully reduce the content of DAOC in the CPC fermentation broth. This work offered a practical way to improve the CPC purification and reduce its production cost.
    PMID: 21866341 [PubMed - as supplied by publisher] (Source: Journal of Industrial Microbiology and Biotechnology)</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5175032</comments>
            <pubDate>Wed, 24 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5175032</guid>        </item>
        <item>
            <title>Comparison of microbial hosts and expression systems for mammalian CYP1A1 catalysis.</title>
            <link>http://www.medworm.com/index.php?rid=5175033&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21863302%26dopt%3DAbstract</link>
            <description>In this study, the potential of different recombinant microorganisms expressing rat and human cyp1a1 genes is evaluated for such applications. The maximum specific activity for 7-ethoxyresorufin O-deethylation and gene expression levels were used as parameters to judge biocatalyst performance. Under comparable conditions, E. coli is shown to be superior over the use of S. cerevisiae and P. putida as hosts for biocatalysis. Of all tested E. coli strains, E. coli DH5α and E. coli JM101 harboring rat CYP1A1 showed the highest activities (0.43 and 0.42 U g (CDW) (-1) , respectively). Detection of active CYP1A1 in cell-free E. coli extracts was found to be difficult and only for E. coli DH5α, expression levels could be determined (41 nmol g (CDW) (-1) ). The presented results show that eff...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5175033</comments>
            <pubDate>Tue, 23 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5175033</guid>        </item>
        <item>
            <title>Global transcriptome analysis of the tetrachloroethene-dechlorinating bacterium Desulfitobacterium hafniense Y51 in the presence of various electron donors and terminal electron acceptors.</title>
            <link>http://www.medworm.com/index.php?rid=5175034&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21861158%26dopt%3DAbstract</link>
            <description>This study paves the way to understanding the physiology of D. hafniense, optimizing this microbe as a bioremediation agent, and designing bioarray sensors to monitor the presence of dechlorinating organisms in the environment.
    PMID: 21861158 [PubMed - as supplied by publisher] (Source: Journal of Industrial Microbiology and Biotechnology)</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5175034</comments>
            <pubDate>Mon, 22 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5175034</guid>        </item>
        <item>
            <title>Microbial processes in the Athabasca Oil Sands and their potential applications in microbial enhanced oil recovery.</title>
            <link>http://www.medworm.com/index.php?rid=5175036&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21853326%26dopt%3DAbstract</link>
            <description>This article reviews the microbiology of the Athabasca Oil Sands and the mechanisms bacteria use to tolerate low water and high hydrocarbon availability in oil reservoirs and oilfields, and potential applications in MEOR.
    PMID: 21853326 [PubMed - as supplied by publisher] (Source: Journal of Industrial Microbiology and Biotechnology)</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5175036</comments>
            <pubDate>Thu, 18 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5175036</guid>        </item>
        <item>
            <title>Potential for industrial products from the halophilic Archaea.</title>
            <link>http://www.medworm.com/index.php?rid=5175035&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21853327%26dopt%3DAbstract</link>
            <description>Authors: Litchfield CD
    Abstract
    The halophilic Archaea are a group of microorganisms that have not been extensively considered for biotechnological applications. This review describes some of the enzymes and products and the potential applications of this unique group of microorganisms to various industrial processes. Specifically, the characteristics of the glycosyl hydrolases, lipases and esterases, proteases, biopolymers and surfactants, as well as some miscellaneous other activities will be described.
    PMID: 21853327 [PubMed - as supplied by publisher] (Source: Journal of Industrial Microbiology and Biotechnology)</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5175035</comments>
            <pubDate>Thu, 18 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5175035</guid>        </item>
        <item>
            <title>Clostridium beijerinckii mutant with high inhibitor tolerance obtained by low-energy ion implantation.</title>
            <link>http://www.medworm.com/index.php?rid=5097692&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21789489%26dopt%3DAbstract</link>
            <description>Authors: Guo T, Tang Y, Zhang QY, Du TF, Liang DF, Jiang M, Ouyang PK
    Clostridium beijerinckii mutant strain IB4, which has a high level of inhibitor tolerance, was screened by low-energy ion implantation and used for butanol fermentation from a non-detoxified hemicellulosic hydrolysate of corn fiber treated with dilute sulfuric acid (SAHHC). Evaluation of toxicity showed C. beijerinckii IB4 had a higher level of tolerance than parent strain C. beijerinckii NCIMB 8052 for five out of six phenolic compounds tested (the exception was vanillin). Using glucose as carbon source, C. beijerinckii IB4 produced 9.1 g l(-1) of butanol with an acetone/butanol/ethanol (ABE) yield of 0.41 g g(-1). When non-detoxified SAHHC was used as carbon source, C. beijerinckii NCIMB 8052 grew well but ABE ...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5097692</comments>
            <pubDate>Mon, 25 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5097692</guid>        </item>
        <item>
            <title>Wine flavor and aroma.</title>
            <link>http://www.medworm.com/index.php?rid=5097693&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21786136%26dopt%3DAbstract</link>
            <description>Authors: Styger G, Prior B, Bauer FF
    The perception of wine flavor and aroma is the result of a multitude of interactions between a large number of chemical compounds and sensory receptors. Compounds interact and combine and show synergistic (i.e., the presence of one compound enhances the perception of another) and antagonistic (a compound suppresses the perception of another) interactions. The chemical profile of a wine is derived from the grape, the fermentation microflora (in particular the yeast Saccharomyces cerevisiae), secondary microbial fermentations that may occur, and the aging and storage conditions. Grape composition depends on the varietal and clonal genotype of the vine and on the interaction of the genotype and its phenotype with many environmental factors which, in wi...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5097693</comments>
            <pubDate>Sat, 23 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5097693</guid>        </item>
        <item>
            <title>Transcriptome analysis of probiotic Lactobacillus casei Zhang during fermentation in soymilk.</title>
            <link>http://www.medworm.com/index.php?rid=5097694&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21779970%26dopt%3DAbstract</link>
            <description>Authors: Wang JC, Zhang WY, Zhong Z, Wei AB, Bao QH, Zhang Y, Sun TS, Postnikoff A, Meng H, Zhang HP
    Lactobacillus casei Zhang is a widely recognized probiotic bacterium, which is being commercially used in China. To study the gene expression dynamics of L. casei Zhang during fermentation in soymilk, a whole genome microarray was used to screen for differentially expressed genes when grown to the lag phase, the late logarithmic phase, and the stationary phase. Comparisons of different transcripts next to each other revealed 162 and 63 significantly induced genes in the late logarithmic phase and stationary phase, of which the expression was at least threefold up-regulated and down-regulated, respectively. Approximately 38.4% of the up-regulated genes were associated with amino acid tra...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5097694</comments>
            <pubDate>Thu, 21 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5097694</guid>        </item>
        <item>
            <title>Isolation and optimisation of the oleaginous yeast Sporobolomyces roseus for biosynthesis of (13)C isotopically labelled 18-carbon unsaturated fatty acids and trans 18:1 and 18:2 derivatives through synthesis.</title>
            <link>http://www.medworm.com/index.php?rid=5097691&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21809096%26dopt%3DAbstract</link>
            <description>Authors: Cui Y, Fraser C, Gardner G, Huang CJ, Reith M, Windust AJ
    An oleaginous and psychrotrophic strain (F38-3) of Sporobolomyces roseus Kluyver &amp; van Niel was isolated from a salt marsh environment in Nova Scotia, Canada following a screening program to select for high producers of 18-carbon unsaturated fatty acids. Fatty acid production was characterised as a function of temperature at 20 g glucose L(-1), and optimal yields were obtained at 14°C, achieving 5.7 g dw biomass and 39.2% total fatty acids by dry weight, with 18:1, 18:2 and 18:3 all-cis fatty acids accounting for 49.4%, 14.3% and 6.7% of total fatty acids (TFA), respectively-the highest reported for this species. Production of 18:3 was inversely correlated to growth temperature, rising from 2% of TFA at 30°C...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5097691</comments>
            <pubDate>Mon, 18 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5097691</guid>        </item>
        <item>
            <title>Improvement of lipid production in the marine strains Alexandrium minutum and Heterosigma akashiwo by utilizing abiotic parameters.</title>
            <link>http://www.medworm.com/index.php?rid=5051677&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21766212%26dopt%3DAbstract</link>
            <description>Authors: Fuentes-Grünewald C, Garcés E, Alacid E, Sampedro N, Rossi S, Camp J
    Two different strains of microalgae, one raphidophyte and one dinoflagellate, were tested under different abiotic conditions with the goal of enhancing lipid production. Whereas aeration was crucial for biomass production, nitrogen deficiency and temperature were found to be the main abiotic parameters inducing the high-level cellular accumulation of neutral lipids. Net neutral lipid production and especially triacylglycerol (TAG) per cell were higher in microalgae (&amp;gt;200% in Alexandrium minutum, and 30% in Heterosigma akashiwo) under treatment conditions (25°C; 330 μM NaNO(3)) than under control conditions (20°C; 880 μM NaNO(3)). For both algal species, oil production (free fatty acids plus TAG fra...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5051677</comments>
            <pubDate>Fri, 15 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5051677</guid>        </item>
        <item>
            <title>Random UV-C mutagenesis of Scheffersomyces (formerly Pichia) stipitis NRRL Y-7124 to improve anaerobic growth on lignocellulosic sugars.</title>
            <link>http://www.medworm.com/index.php?rid=5051678&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21748309%26dopt%3DAbstract</link>
            <description>Authors: Hughes SR, Gibbons WR, Bang SS, Pinkelman R, Bischoff KM, Slininger PJ, Qureshi N, Kurtzman CP, Liu S, Saha BC, Jackson JS, Cotta MA, Rich JO, Javers JE
    Scheffersomyces (formerly Pichia) stipitis NRRL Y-7124 was mutagenized using UV-C irradiation to produce yeast strains for anaerobic conversion of lignocellulosic sugars to ethanol. UV-C irradiation potentially produces large numbers of random mutations broadly and uniformly over the whole genome to generate unique strains. Wild-type cultures of S. stipitis NRRL Y-7124 were subjected to UV-C (234 nm) irradiation targeted at approximately 40% cell survival. When surviving cells were selected in sufficient numbers via automated plating strategies and cultured anaerobically on xylose medium for 5 months at 28°C, five novel mut...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5051678</comments>
            <pubDate>Mon, 11 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5051678</guid>        </item>
        <item>
            <title>Effects of physical culture parameters on bacteriocin production by Mexican strains of Bacillus thuringiensis after cellular induction.</title>
            <link>http://www.medworm.com/index.php?rid=5051679&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21743998%26dopt%3DAbstract</link>
            <description>Authors: Martínez-Cardeñas JA, de la Fuente-Salcido NM, Salcedo-Hernández R, Bideshi DK, Barboza-Corona JE
    We have shown previously that in the presence of inducer Bacillus cereus 183, significant increases in bacteriocin production and bactericidal activity of B. thuringiensis occur when the latter is cultivated at pH 7.2, 28°C, and 180 rpm. Here we show that this activity can be further improved when B. thuringiensis is induced with B. cereus 183 and then cultivated with modification of pH, temperature, and agitation. Five native strains of B. thuringiensis, LBIT 269, LBIT 287, LBIT 404, LBIT 420, and LBIT 524 which synthesize, respectively, morricin 269, kurstacin 287, kenyacin 404, entomocin 420, and tolworthcin 524, were cultivated in four different fermentation media. Of the...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5051679</comments>
            <pubDate>Fri, 08 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5051679</guid>        </item>
        <item>
            <title>Bioconversion of ovine scotta into lactic acid with pure and mixed cultures of lactic acid bacteria.</title>
            <link>http://www.medworm.com/index.php?rid=5051680&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21739193%26dopt%3DAbstract</link>
            <description>Authors: Secchi N, Giunta D, Pretti L, García MR, Roggio T, Mannazzu I, Catzeddu P
    Scotta is the main by-product in the making of ricotta cheese. It is widely produced in southern Europe and particularly in Italy where it represents a serious environmental pollutant due to its high lactose content. With the aim of evaluating whether scotta bioconversion into lactic acid can be considered as an alternative to its disposal, besides providing it with an added value, here the growth, fermentative performances, and lactic acid productions of pure and mixed cultures of Lactobacillus casei, Lactobacillus helveticus, and Streptococcus thermophilus were evaluated on ovine scotta-based media, without and with the addition of nutritional supplements. The outcomes indicate that ovine scotta can b...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5051680</comments>
            <pubDate>Thu, 07 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5051680</guid>        </item>
        <item>
            <title>Biochemical and kinetic characterization of GH43 β-D: -xylosidase/α-L: -arabinofuranosidase and GH30 α-L: -arabinofuranosidase/β-D: -xylosidase from rumen metagenome.</title>
            <link>http://www.medworm.com/index.php?rid=5002239&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21720773%26dopt%3DAbstract</link>
            <description>Authors: Zhou J, Bao L, Chang L, Zhou Y, Lu H
    The present study focuses on characterization of two hemicellulases, RuXyn1 and RuXyn2, from rumen bacterial metagenome and their capabilities for degradation of xylans. Glycosyl hydrolase (GH) family 43 β-D: -xylosidase/α-L: -arabinofuranosidase RuXyn1 can hydrolyze p-nitrophenyl-β-D: -xylopyranoside (pNPX), p-nitrophenyl-α-L: -arabinofuranoside (pNPA), and xylo-oligosaccharide substrates, while GH30 1,5-α-L: -arabinofuranosidase/β-D: -xylosidase RuXyn2, the first α-L: -arabinofuranosidase assigned to this GH family, shows activities towards 1,5-α-L: -arabinobiose and pNPX substrates but no activity for pNPA. Kinetic analysis for aryl-glycosides revealed that RuXyn2 had higher catalytic efficiency than RuXyn1 toward pNPX substrate...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5002239</comments>
            <pubDate>Fri, 01 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5002239</guid>        </item>
        <item>
            <title>Enzymatic production of 2-amino-2,3-dimethylbutyramide by cyanide-resistant nitrile hydratase.</title>
            <link>http://www.medworm.com/index.php?rid=5002238&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21720774%26dopt%3DAbstract</link>
            <description>Authors: Lin ZJ, Zheng RC, Wang YJ, Zheng YG, Shen YC
    A novel enzymatic route for the synthesis of 2-amino-2,3-dimethylbutyramide (ADBA), important intermediate of highly potent and broad-spectrum imidazolinone herbicides, from 2-amino-2,3-dimethylbutyronitrile (ADBN) was developed. Strain Rhodococcus boritolerans CCTCC M 208108 harboring nitrile hydratase (NHase) towards ADBN was screened through a sophisticated colorimetric screening method and was found to be resistant to cyanide (5 mM). Resting cells of R. boritolerans CCTCC M 208108 also proved to be tolerant against high product concentration (40 g l(-1)) and alkaline pH (pH 9.3). A preparative scale process for continuous production of ADBA in both aqueous and biphasic systems was developed and some key parameters of the bioc...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5002238</comments>
            <pubDate>Fri, 01 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5002238</guid>        </item>
        <item>
            <title>Poly(β-L-malic acid) production by diverse phylogenetic clades of Aureobasidium pullulans.</title>
            <link>http://www.medworm.com/index.php?rid=5002237&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21720775%26dopt%3DAbstract</link>
            <description>In this study, we examined PMA production by 56 strains of the fungus Aureobasidium pullulans representing genetically diverse phylogenetic clades. Thirty-six strains were isolated from various locations in Iceland and Thailand. All strains from Iceland belonged to a newly recognized clade 13, while strains from Thailand were distributed among 8 other clades, including a novel clade 14. Thirty of these isolates, along with 26 previously described strains, were examined for PMA production in medium containing 5% glucose. Most strains produced at least 4 g PMA/L, and several strains in clades 9, 11, and 13 made 9-11 g PMA/L. Strains also produced both pullulan and heavy oil, but PMA isolated by differential precipitation in ethanol exhibited up to 72% purity with no more than 12% contamina...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5002237</comments>
            <pubDate>Fri, 01 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5002237</guid>        </item>
        <item>
            <title>Pseudoxanthomonas bacteria that drive deposit formation of wood extractives can be flocculated by cationic polyelectrolytes.</title>
            <link>http://www.medworm.com/index.php?rid=5002236&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21720776%26dopt%3DAbstract</link>
            <description>We describe here that Pseudoxanthomonas taiwanensis, a wide-spread and abundant bacterium in paper machine water circuits, aggregated dispersions of wood extractives (&quot;pitch&quot;) and resin acid, under conditions prevailing in machine water circuits (10(9) cfu ml(-1), pH 8, 45°C). The aggregates were large enough (up to 50 μm) so that they could be expected to clog wires and felts and to reduce dewatering of the fiber web. The Pseudoxanthomonas bacteria were negatively charged over a pH range of 3.2-10. Cationic polyelectrolytes of the types used as retention aids or fixatives to flocculate &quot;anionic trash&quot; in paper machines were effective in flocculating the Pseudoxanthomonas bacteria. The polyelectrolyte most effective for this purpose was of high molecular weight (7-8 × 10(6) g mol...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5002236</comments>
            <pubDate>Fri, 01 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5002236</guid>        </item>
        <item>
            <title>Specific PCR to identify the heavy-metal-resistant bacterium Cupriavidus metallidurans.</title>
            <link>http://www.medworm.com/index.php?rid=5002240&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21720772%26dopt%3DAbstract</link>
            <description>Authors: Ryan MP, Adley CC
    The aim of this study is to develop a polymerase chain reaction (PCR) assay for rapid detection of Cupriavidus metallidurans. PCR primers targeting the Signal transduction histidine kinase gene were designed and designated Cm-F1/Cm-R1. Strains of C. metallidurans were positively identified. The size of the PCR products was 437 bp, as expected. This PCR method enables monitoring of industrial, environmental and clinical sources for presence of C. metallidurans.
    PMID: 21720772 [PubMed - as supplied by publisher] (Source: Journal of Industrial Microbiology and Biotechnology)</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5002240</comments>
            <pubDate>Thu, 30 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5002240</guid>        </item>
        <item>
            <title>Improvement of L: -valine production at high temperature in Brevibacterium flavum by overexpressing ilvEBN(r)C genes.</title>
            <link>http://www.medworm.com/index.php?rid=5002241&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21706252%26dopt%3DAbstract</link>
            <description>Authors: Hou X, Ge X, Wu D, Qian H, Zhang W
    Brevibacterium flavum ATCC14067 was engineered for L: -valine production by overexpression of different ilv genes; the ilvEBN(r)C genes from B. flavum NV128 provided the best candidate for L: -valine production. In traditional fermentation, L: -valine production reached 30.08 ± 0.92 g/L at 31°C in 72 h with a low conversion efficiency of 0.129 g/g. To further improve the L: -valine production and conversion efficiency based on the optimum temperatures of L: -valine biosynthesis enzymes (above 35°C) and the thermotolerance of B. flavum, the fermentation temperature was increased to 34, 37, and 40°C. As a result, higher metabolic rate and L: -valine biosynthesis enzymes activity were obtained at high temperature, and the maximum L: -va...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5002241</comments>
            <pubDate>Fri, 24 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5002241</guid>        </item>
        <item>
            <title>Efficient expression of a Paenibacillus barcinonensis endoglucanase in Saccharomyces cerevisiae.</title>
            <link>http://www.medworm.com/index.php?rid=5002242&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21701899%26dopt%3DAbstract</link>
            <description>Authors: Mormeneo M, Pastor FJ, Zueco J
    The endoglucanase coded by celA (GenBank Access No. Y12512) from Paenibacillus barcinonensis, an enzyme with good characteristics for application on paper manufacture from agricultural fibers, was expressed in Saccharomyces cerevisiae by using different domains of the cell wall protein Pir4 as translational fusion partners, to achieve either secretion or cell wall retention of the recombinant enzyme. Given the presence of five potential N-glycosylation sites in the amino acid sequence coded by celA, the effect of glycosylation on the enzymatic activity of the recombinant enzyme was investigated by expressing the recombinant fusion proteins in both, standard and glycosylation-deficient strains of S. cerevisiae. Correct targeting of the recombinant...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5002242</comments>
            <pubDate>Thu, 23 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5002242</guid>        </item>
        <item>
            <title>Improvement of robustness and ethanol production of ethanologenic Saccharomyces cerevisiae under co-stress of heat and inhibitors.</title>
            <link>http://www.medworm.com/index.php?rid=5002243&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21698486%26dopt%3DAbstract</link>
            <description>Authors: Lu Y, Cheng YF, He XP, Guo XN, Zhang BR
    Bioethanol is an attractive alternative to fossil fuels. Saccharomyces cerevisiae is the most important ethanol producer. However, yeast cells are challenged by various environmental stresses during the industrial process of ethanol production. The robustness under heat, acetic acid, and furfural stresses was improved for ethanologenic S. cerevisiae in this work using genome shuffling. Recombinant yeast strain R32 could grow at 45°C, and resist 0.55% (v/v) acetic acid and 0.3% (v/v) furfural at 40°C. When ethanol fermentation was conducted at temperatures ranging from 30 to 42°C, recombinant strain R32 always gave high ethanol production. After 42 h of fermentation at 42°C, 187.6 ± 1.4 g/l glucose was utilized by recombinant str...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5002243</comments>
            <pubDate>Wed, 22 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5002243</guid>        </item>
        <item>
            <title>Very high gravity (VHG) ethanolic brewing and fermentation: a research update.</title>
            <link>http://www.medworm.com/index.php?rid=5002245&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21695540%26dopt%3DAbstract</link>
            <description>Authors: Puligundla P, Smogrovicova D, Obulam VS, Ko S
    There have been numerous developments in ethanol fermentation technology since the beginning of the new millennium as ethanol has become an immediate viable alternative to fast-depleting crude reserves as well as increasing concerns over environmental pollution. Nowadays, although most research efforts are focused on the conversion of cheap cellulosic substrates to ethanol, methods that are cost-competitive with gasoline production are still lacking. At the same time, the ethanol industry has engaged in implementing potential energy-saving, productivity and efficiency-maximizing technologies in existing production methods to become more viable. Very high gravity (VHG) fermentation is an emerging, versatile one among such technologi...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5002245</comments>
            <pubDate>Tue, 21 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5002245</guid>        </item>
        <item>
            <title>Expression and fermentation optimization of oxidized polyvinyl alcohol hydrolase in E. coli.</title>
            <link>http://www.medworm.com/index.php?rid=5002244&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21695541%26dopt%3DAbstract</link>
            <description>In this study, the OPH gene from Sphingopyxis sp. 113P3 was modified, by artificial synthesis, for overexpression in Escherichia coli. The OPH gene, lacking the sequence encoding the original signal peptide, was inserted into pET-20b (+) expression vector, which was then used to transform E. coli BL21 (DE3). OPH expression was detected in culture medium in which the transformed E. coli BL21 (DE3) was grown. Nutritional and environmental conditions were investigated for improved production of OPH protein by the recombinant strain. The highest OPH activity measured was 47.54 U/mL and was reached after 84 h under optimal fermentation conditions; this level is 2.64-fold higher that obtained under sub-optimal conditions. The productivity of recombinant OPH reached 565.95 U/L/h. The effect of...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5002244</comments>
            <pubDate>Tue, 21 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5002244</guid>        </item>
        <item>
            <title>Enhanced production of alkaline thermostable keratinolytic protease from calcium alginate immobilized cells of thermoalkalophilic Bacillus halodurans JB 99 exhibiting dehairing activity.</title>
            <link>http://www.medworm.com/index.php?rid=4958362&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21691794%26dopt%3DAbstract</link>
            <description>Authors: Shrinivas D, Kumar R, Naik GR
    The thermoalkalophilic Bacillus halodurans JB 99 cells known for production of novel thermostable alkaline keratinolytic protease were immobilized in calcium alginate matrix. Batch and repeated batch cultivation using calcium alginate immobilized cells were studied for alkaline protease production in submerged fermentation. Immobilized cells with 2.5% alginate and 350 beads/flask of initial cell loading showed enhanced production of alkaline protease by 23.2% (5,275 ± 39.4 U/ml) as compared to free cells (4,280 ± 35.4 U/ml) after 24 h. In the semicontinuous mode of cultivation, immobilized cells under optimized conditions produced an appreciable level of alkaline protease in up to nine cycles and reached a maximal value of 5,975 U/ml af...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4958362</comments>
            <pubDate>Mon, 20 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4958362</guid>        </item>
        <item>
            <title>Autochthonous fermentation starters for the industrial production of Negroamaro wines.</title>
            <link>http://www.medworm.com/index.php?rid=4958361&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21691795%26dopt%3DAbstract</link>
            <description>Authors: Tristezza M, Vetrano C, Bleve G, Grieco F, Tufariello M, Quarta A, Mita G, Spano G, Grieco F
    The aim of the present study was to establish a new procedure for the oenological selection of Saccharomyces cerevisiae strains isolated from natural must fermentations of an important Italian grape cultivar, denoted as &quot;Negroamaro&quot;. For this purpose, 108 S. cerevisiae strains were selected as they did not produce H(2)S and then assayed by microfermentation tests. The adopted procedure made it possible to identify 10 strains that were low producers of acetic acid and hydrogen sulphide and showed that they completed sugar consumption during fermentation. These strains were characterized for their specific oenological and technological properties and, two of them, strains 6993 and 6920, ...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4958361</comments>
            <pubDate>Mon, 20 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4958361</guid>        </item>
        <item>
            <title>Detection of dichloromethane with a bioluminescent (lux) bacterial bioreporter.</title>
            <link>http://www.medworm.com/index.php?rid=4958363&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21688172%26dopt%3DAbstract</link>
            <description>Authors: Lopes N, Hawkins SA, Jegier P, Menn FM, Sayler GS, Ripp S
    The focus of this research effort was to develop an autonomous, inducible, lux-based bioluminescent bioreporter for the real-time detection of dichloromethane. Dichloromethane (DCM), also known as methylene chloride, is a volatile organic compound and one of the most commonly used halogenated solvents in the U.S., with applications ranging from grease and paint stripping to aerosol propellants and pharmaceutical tablet coatings. Predictably, it is released into the environment where it contaminates air and water resources. Due to its classification as a probable human carcinogen, hepatic toxin, and central nervous system effector, DCM must be carefully monitored and controlled. Methods for DCM detection usually rely on ...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4958363</comments>
            <pubDate>Sat, 18 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4958363</guid>        </item>
        <item>
            <title>Purification and properties of phenolic acid decarboxylase from Candida guilliermondii.</title>
            <link>http://www.medworm.com/index.php?rid=4958365&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21681484%26dopt%3DAbstract</link>
            <description>Authors: Huang HK, Tokashiki M, Maeno S, Onaga S, Taira T, Ito S
    A heat-labile phenolic acid decarboxylase from Candida guilliermondii (an anamorph of Pichia guilliermondii) was purified to homogeneity by simple successive column chromatography within 3 days. The molecular mass was 20 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and 36 kDa by gel-filtration chromatography, suggesting that the purified enzyme is a homodimer. The optimal pH and temperature were approximately 6.0 and 25°C. Characteristically, more than 50% of the optimal activity was observed at 0°C, suggesting that this enzyme is cold-adapted. The enzyme converted p-coumaric acid, ferulic acid, and caffeic acid to corresponding products with high specific activities of approximately 600, 530, and...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4958365</comments>
            <pubDate>Thu, 16 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4958365</guid>        </item>
        <item>
            <title>Isolation and characterization of an arsenate-reducing bacterium and its application for arsenic extraction from contaminated soil.</title>
            <link>http://www.medworm.com/index.php?rid=4958364&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21681485%26dopt%3DAbstract</link>
            <description>Authors: Chang YC, Nawata A, Jung K, Kikuchi S
    A Gram-negative anaerobic bacterium, Citrobacter sp. NC-1, was isolated from soil contaminated with arsenic at levels as high as 5,000 mg As kg(-1). Strain NC-1 completely reduced 20 mM arsenate within 24 h and exhibited arsenate-reducing activity at concentrations as high as 60 mM. These results indicate that strain NC-1 is superior to other dissimilatory arsenate-reducing bacteria with respect to arsenate reduction, particularly at high concentrations. Strain NC-1 was also able to effectively extract arsenic from contaminated soils via the reduction of solid-phase arsenate to arsenite, which is much less adsorptive than arsenate. To characterize the reductase systems in strain NC-1, arsenate and nitrate reduction activities were in...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4958364</comments>
            <pubDate>Thu, 16 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4958364</guid>        </item>
        <item>
            <title>Correlation between pellet morphology and glycopeptide antibiotic balhimycin production by Amycolatopsis balhimycina DSM 5908.</title>
            <link>http://www.medworm.com/index.php?rid=4909452&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21643706%26dopt%3DAbstract</link>
            <description>In this study, we first characterized the effect of varying concentrations of phosphate and ammonia in defined media on pellet morphology for an actinomycete Amycolatopsis balhimycina DSM 5908, which produces balhimycin, a glycopeptide antibiotic. Our results show that higher balhimycin productivity is correlated with the following morphological features: (1) higher pellet fraction in the biomass, (2) small elongated pellets, and (3) shorter filaments in hyphal growth in the periphery of the pellets. The correlation between morphology and product formation was also observed in industrially relevant complex media. Although balhimycin production starts after 72 h with maximum production around 168 h, the morphological changes in pellets are observed as early as 24 h after commencing of th...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4909452</comments>
            <pubDate>Fri, 03 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4909452</guid>        </item>
        <item>
            <title>Production of bioactive sheep β-defensin-1 in Pichia pastoris.</title>
            <link>http://www.medworm.com/index.php?rid=4909451&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21643707%26dopt%3DAbstract</link>
            <description>Authors: Zhao P, Cao G
    Previous research has shown that sheep β-defensin-1 (sBD-1), a small cationic peptide with a broad range of antimicrobial activities, could inhibit the growth of both Gram-positive and Gram-negative bacteria as well as that of fungi. In order to increase the yield of current ovine defensin purification methods, mature sBD-1 (msBD-1) was added with a 6-His tag on the C-terminus (msBD-1-T) and expressed in Pichia pastoris in the presented work. The msBD-1 and msBD-1-T were expressed in the Pichia pastoris. Both msBD-1 and msBD-1-T were purification, and the two peptides were used to inhibit Escherichia coli, Staphylococcus aureus, Proteus vulgaris, Pseudomonas aeruginosa, and Shigella flexneri. The antimicrobial activity of the 6-His tagged msBD-1-T peptide was no...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4909451</comments>
            <pubDate>Fri, 03 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4909451</guid>        </item>
        <item>
            <title>Enzymatic deinking of secondary fibers: cellulases/hemicellulases versus laccase-mediator system.</title>
            <link>http://www.medworm.com/index.php?rid=4909450&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21643708%26dopt%3DAbstract</link>
            <description>This study compares the use of cellulases/hemicellulases versus the laccase-mediator system for deinking printed fibers from newspapers and magazines. For this purpose, two commercial enzyme preparations with endoglucanase and endoxylanase activities (Viscozyme Wheat from Aspergillus oryzae and Ultraflo L from Humicola insolens, Novozymes) and a commercial laccase (NS51002 from Trametes villosa, Novozymes), the latter in the presence of synthetic or natural (lignin-related) mediators, were evaluated. The enzymatic treatments were studied at the laboratory scale using a standard chemical deinking sequence consisting of a pulping stage; an alkaline stage using NaOH, sodium silicate and fatty acid soap; and a bleaching stage using hydrogen peroxide. The handsheets were then prepared and their...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4909450</comments>
            <pubDate>Fri, 03 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4909450</guid>        </item>
        <item>
            <title>Identification of a xylose reductase gene in the xylose metabolic pathway of Kluyveromyces marxianus NBRC1777.</title>
            <link>http://www.medworm.com/index.php?rid=4909449&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21643709%26dopt%3DAbstract</link>
            <description>Authors: Zhang B, Zhang L, Wang D, Gao X, Hong J
    Kluyveromyces marxianus is thermotolerant yeast that is able to utilize a wider range of substrates and has greater thermal tolerance than most other yeast species. K. marxianus can assimilate xylose, but its ability to produce ethanol from xylose in oxygen-limited environments is poor. In the present study, the K. marxianus xylose reductase (KmXR) gene (Kmxyl1) was cloned and the recombinant enzyme was characterized to clarify the factors that limit xylose fermentation in K. marxianus NBRC1777. KmXR is a key enzyme in the xylose metabolism of K. marxianus, which was verified by disruption of the Kmxyl1 gene. The Km of the recombinant KmXR for NADPH is 65.67 μM and KmXR activity is 1.295 U/mg, which is lower than those of most reporte...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4909449</comments>
            <pubDate>Fri, 03 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4909449</guid>        </item>
        <item>
            <title>Electrochemical behavior of the 316L steel type in a marine culture of microalgae (Porphyridium purpureum) under the 12/12 h photoperiod and effect of different working electrode exposure conditions on the biofilm-metal interface.</title>
            <link>http://www.medworm.com/index.php?rid=4909448&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21643710%26dopt%3DAbstract</link>
            <description>Authors: Djemai-Zoghlache Y, Isambert A, Belhaneche-Bensemra N
    The industrial crops of microalgae use processes calling upon the presence of parts of metal nature such as steel 316L type. The goal of this study is to test the electrochemical behavior of this material in a marine culture of microalgae. Porphyridium purpureum was used under a photoperiod of alternation darkness/light 12/12 h, in order to apprehend the problems of biocorrosion involved in the biofouling. The evolution of the free potential of corrosion, according to the position of the samples and for different surface roughness, observations of the surface quality under the electron microscope with sweeping were carried out. The results showed that, overall, the strain P. purpureum does not have a corrosive effect on the...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4909448</comments>
            <pubDate>Fri, 03 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4909448</guid>        </item>
        <item>
            <title>Structure and dynamics of microbial community in full-scale activated sludge reactors.</title>
            <link>http://www.medworm.com/index.php?rid=4909453&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21633845%26dopt%3DAbstract</link>
            <description>Authors: Yi T, Lee EH, Kang S, Shin J, Cho KS
    Phospholipid fatty acid (PLFA) profiles in four full-scale activated sludge reactors (ASR1 ~ 4) treating municipal wastewater, South Korea, were monitored to evaluate the influence of influent water quality on microbial community structure (MCS) and the effect of the MCS on effluent water quality. In ASR1 ~ 3, PLFA profiles were very similar, regardless of the influent water quality and seasonal differences, and 16:17c/15:0iso2OH and 16:0 were dominant. PLFA profiles in ASR4 during summer and autumn were very similar to those in ASR1 ~ 3, but increases in specific fatty acids, 16:1ω5c, 11methyl18:1ω7c and 15:0iso3OH, were found in ASR4 during winter and spring, with relatively high total suspended solid (TSS) concentrations in the efflu...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4909453</comments>
            <pubDate>Wed, 01 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4909453</guid>        </item>
        <item>
            <title>Screening of the common culture conditions affecting crystallinity of bacterial cellulose.</title>
            <link>http://www.medworm.com/index.php?rid=4909454&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21630052%26dopt%3DAbstract</link>
            <description>Authors: Zeng X, Liu J, Chen J, Wang Q, Li Z, Wang H
    By analyzing with X-ray diffraction and FT-IR spectroscopy, the main effective factors among common culture conditions on crystallinity index and I (α) fraction of cellulose produced by Gluconacetobacter xylinus were examined with Plackett-Burman design experiment. Varying pH value in the medium by adjusting the composition of citrate buffer or by adding HCl/NaOH solution indicates it is the content of citrate buffer rather than its function of pH buffering that gives the influence on crystallinity. Further experiment reveals that Na(+) concentration of 0.174 mol/l in medium with citrate buffer added would decrease the crystallinity index significantly. Comparison of carbon sources shows that fructose leads to a higher crystallinit...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4909454</comments>
            <pubDate>Tue, 31 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4909454</guid>        </item>
        <item>
            <title>Production of xylanolytic enzymes by Aspergillus terricola in stirred tank and airlift tower loop bioreactors.</title>
            <link>http://www.medworm.com/index.php?rid=4909457&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21626207%26dopt%3DAbstract</link>
            <description>Authors: Michelin M, Polizeli MD, Silva DP, Ruzene DS, Vicente AA, Jorge JA, Terenzi HF, Teixeira JA
    Fungi producing high xylanase levels have attracted considerable attention because of their potential industrial applications. Batch cultivations of Aspergillus terricola fungus were evaluated in stirred tank and airlift bioreactors, by using wheat bran particles suspended in the cultivation medium as substrate for xylanase and β-xylosidase production. In the stirred tank bioreactor, in physical conditions of 30°C, 300 rpm, and aeration of 1 vvm (1 l min(-1)), with direct inoculation of fungal spores, 7,475 U l(-1) xylanase was obtained after 36 h of operation, remaining constant after 24 h. In the absence of air injection in the stirred tank reactor, limited xylanase producti...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4909457</comments>
            <pubDate>Mon, 30 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4909457</guid>        </item>
        <item>
            <title>Engineering Saccharomyces cerevisiae to produce feruloyl esterase for the release of ferulic acid from switchgrass.</title>
            <link>http://www.medworm.com/index.php?rid=4909456&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21626208%26dopt%3DAbstract</link>
            <description>Authors: Wong DW, Chan VJ, Batt SB, Sarath G, Liao H
    The Aspergillus niger feruloyl esterase gene (faeA) was cloned into Saccharomyces cerevisiae via a yeast expression vector, resulting in efficient expression and secretion of the enzyme in the medium with a yield of ~2 mg/l. The recombinant enzyme was purified to homogeneity by anion-exchange and hydrophobic interaction chromatography. The specific activity was determined to be 8,200 U/μg (pH 6.5, 20°C, 3.5 mM 4-nitrophenyl ferulate). The protein had a correct N-terminal sequence of ASTQGISEDLY, indicating that the signal peptide was properly processed. The FAE exhibited an optimum pH of 6-7 and operated optimally at 50°C using ground switchgrass as the substrate. The yeast clone was demonstrated to catalyze the release of feru...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4909456</comments>
            <pubDate>Mon, 30 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4909456</guid>        </item>
        <item>
            <title>Editorial.</title>
            <link>http://www.medworm.com/index.php?rid=4909458&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21626206%26dopt%3DAbstract</link>
            <description>Authors: Schwartz RD
    
    PMID: 21626206 [PubMed - as supplied by publisher] (Source: Journal of Industrial Microbiology and Biotechnology)</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4909458</comments>
            <pubDate>Fri, 27 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4909458</guid>        </item>
        <item>
            <title>Intrinsic and inducible resistance to hydrogen peroxide in Bifidobacterium species.</title>
            <link>http://www.medworm.com/index.php?rid=4909455&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21626209%26dopt%3DAbstract</link>
            <description>Authors: Oberg TS, Steele JL, Ingham SC, Smeianov VV, Briczinski EP, Abdalla A, Broadbent JR
    Interest in, and use of, bifidobacteria as a probiotic delivered in functional foods has increased dramatically in recent years. As a result of their anaerobic nature, oxidative stress can pose a major challenge to maintaining viability of bifidobacteria during functional food storage. To better understand the oxidative stress response in two industrially important bifidobacteria species, we examined the response of three strains of B. longum and three strains of B. animalis subsp. lactis to hydrogen peroxide (H(2)O(2)). Each strain was exposed to a range of H(2)O(2) concentrations (0-10 mM) to evaluate and compare intrinsic resistance to H(2)O(2). Next, strains were tested for the presence of...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4909455</comments>
            <pubDate>Fri, 27 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4909455</guid>        </item>
        <item>
            <title>Indigestible dextrin stimulates glucoamylase production in submerged culture of Aspergillus kawachii.</title>
            <link>http://www.medworm.com/index.php?rid=4909459&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21618143%26dopt%3DAbstract</link>
            <description>Authors: Sugimoto T, Horaguchi K, Shoji H
    Submerged batch cultures of Aspergillus kawachii grown on indigestible dextrin were investigated for potential improvements in glucoamylase (GA) production. In flask culture, specific GA productivities per dry weight biomass using dextrin and indigestible dextrin were 11.0 and 56.1 mU/mg-DW, respectively. Indigestible dextrin was a poor substrate for enzymatic hydrolysis. Rates of glucose formation from dextrin and indigestible dextrin by enzymatic hydrolysis were 0.477 and 0.100 mg-glucose/ml/h, respectively. For this reason, residual glucose concentrations in batch cultures grown on indigestible dextrin remained below 1.32 mg/ml where glucose-limiting conditions were easily maintained. Batch culture using indigestible dextrin had the same ...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4909459</comments>
            <pubDate>Thu, 26 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4909459</guid>        </item>
        <item>
            <title>Separation of gamma-aminobutyric acid from fermented broth.</title>
            <link>http://www.medworm.com/index.php?rid=4909461&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21614609%26dopt%3DAbstract</link>
            <description>This study aimed to find a separation method for getting high-purity GABA from a fermented broth. Firstly, a fermented broth with a high content of GABA (reaching 997 ± 51 mM) was prepared by fermentation with Lactobacillus brevis NCL912. GABA purification was conducted by successive centrifugation, filtration, decoloration, desalination, ion-exchange chromatography (IEC), and crystallization. Inorganic salt (Na(2)SO(4)) was removed from the both by desalination with 70% ethanol solution. A ninhydrin test strip was designed for the real-time detection of GABA during IEC. The recovery rate for the whole purification process was about 50%. The purified product was characterized by thin-layer chromatography and HPLC, and its purity reached 98.66 ± 2.36%.
    PMID: 21614609 [PubMed - as...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4909461</comments>
            <pubDate>Wed, 25 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4909461</guid>        </item>
        <item>
            <title>Overcoming inhibitors in a hemicellulosic hydrolysate: improving fermentability by feedstock detoxification and adaptation of Pichia stipitis.</title>
            <link>http://www.medworm.com/index.php?rid=4909460&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21614610%26dopt%3DAbstract</link>
            <description>Authors: Stoutenburg RM, Perrotta JA, Nakas JP
    In order to improve the fermentative efficiency of sugar maple hemicellulosic hydrolysates for fuel ethanol production, various methods to mitigate the effects of inhibitory compounds were employed. These methods included detoxification treatments utilizing activated charcoal, anion exchange resin, overliming, and ethyl acetate extraction. Results demonstrated the greatest fermentative improvement of 50% wood hydrolysate (v/v) by Pichia stipitis with activated charcoal treatment. Another method employed to reduce inhibition was an adaptation procedure to produce P. stipitis stains more tolerant of inhibitory compounds. This adaptation resulted in yeast variants capable of improved fermentation of 75% untreated wood hydrolysate (v/v), one o...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4909460</comments>
            <pubDate>Wed, 25 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4909460</guid>        </item>
        <item>
            <title>Purification and structural characterization of fengycin homologues produced by Bacillus subtilis LSFM-05 grown on raw glycerol.</title>
            <link>http://www.medworm.com/index.php?rid=4859056&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21607611%26dopt%3DAbstract</link>
            <description>Authors: de Faria AF, Stéfani D, Vaz BG, Silva IS, Garcia JS, Eberlin MN, Grossman MJ, Alves OL, Durrant LR
    Raw glycerol is a byproduct of biodiesel production that currently has low to negative value for biodiesel producers. One option for increasing the value of raw glycerol is to use it as a feedstock for microbial production. Bacillus subtilis LSFM 05 was used for the production of fengycin in a mineral medium containing raw glycerol as the sole carbon source. Fengycin was isolated by acid precipitation at pH 2 and purified by silica gel column chromatography and characterized using electrospray ionization (ESI) Fourier transform ion cyclotron resonance mass spectrometry (ESI FT-ICR MS) with collision-induced dissociation (CID). The mass spectrum revealed the presence of the ions ...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4859056</comments>
            <pubDate>Mon, 23 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4859056</guid>        </item>
        <item>
            <title>Identification and characterization of CbeI, a novel thermostable restriction enzyme from Caldicellulosiruptor bescii DSM 6725 and a member of a new subfamily of HaeIII-like enzymes.</title>
            <link>http://www.medworm.com/index.php?rid=4859057&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21604181%26dopt%3DAbstract</link>
            <description>Authors: Chung DH, Huddleston JR, Farkas J, Westpheling J
    Potent HaeIII-like DNA restriction activity was detected in cell-free extracts of Caldicellulosiruptor bescii DSM 6725 using plasmid DNA isolated from Escherichia coli as substrate. Incubation of the plasmid DNA in vitro with HaeIII methyltransferase protected it from cleavage by HaeIII nuclease as well as cell-free extracts of C. bescii. The gene encoding the putative restriction enzyme was cloned and expressed in E. coli with a His-tag at the C-terminus. The purified protein was 38 kDa as predicted by the 981-bp nucleic acid sequence, was optimally active at temperatures between 75°C and 85°C, and was stable for more than 1 week when stored at 35°C. The cleavage sequence was determined to be 5'-GG/CC-3', indicating tha...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4859057</comments>
            <pubDate>Sat, 21 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4859057</guid>        </item>
        <item>
            <title>Sponge swabs increase sensitivity of sterility testing of processed bone and tendon allografts.</title>
            <link>http://www.medworm.com/index.php?rid=4859058&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21603957%26dopt%3DAbstract</link>
            <description>Authors: Nguyen H, Morgan DA, Cull S, Benkovich M, Forwood MR
    Sterility testing is the final, and critical, step in quality control of tissue banking. It informs the decision whether to release the tissue allografts for clinical use, or not. The most common method for sterility testing of structural bone and tendon allografts is to swab using cotton tip streaks. This method provides low recovery efficiency; and therefore may pass allografts with low bioburden, providing false negatives. Our pilot data revealed organism recovery efficiencies of 60, 30 and 100% from cotton swab, membrane filtration and sponge swaps, respectively. Our aim was to develop a high sensitivity sterility test for structural bone and tendon allografts using a sponge sampling method. Eighty-one bone and tendon al...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4859058</comments>
            <pubDate>Fri, 20 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4859058</guid>        </item>
        <item>
            <title>Overexpression of a recombinant amidase in a complex auto-inducing culture: purification, biochemical characterization, and regio- and stereoselectivity.</title>
            <link>http://www.medworm.com/index.php?rid=4859059&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21562846%26dopt%3DAbstract</link>
            <description>In this study, an amidase gene from R. erythropolis AJ270 was cloned and expressed in Escherichia coli BL21 (DE3). The activity reached the highest level of 22.04 U/ml in a complex auto-inducing medium using a simplified process of fermentation operation. The recombinant amidase was purified to more than 95% from the crude lysate using Ni-NTA affinity chromatography and Superose S10-300 gel filtration. The V (max) and K (m) values of the purified enzyme with acetamide (50 mM) were 6.89 μmol/min/mg protein and 4.12 mM, respectively, which are similar to those of the enzyme from the wild-type cell. The enzyme converted racemic α-substituted amides, O-benzylated β-hydroxy amides, and N-benzylated β-amino amides to the corresponding (S)-acids with remarkably high enantioselectivity. Th...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4859059</comments>
            <pubDate>Wed, 11 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4859059</guid>        </item>
        <item>
            <title>Purification and characterization of an arginine regulatory protein, ArgR, in Corynebacterium glutamicum.</title>
            <link>http://www.medworm.com/index.php?rid=4859061&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21559975%26dopt%3DAbstract</link>
            <description>In this report, we show the effect of the C. glutamicum ArgR repressor on argC and argG promoters by overexpressing or disrupting the argR gene. Gel filtration assay results indicate that native ArgR is a hexamer of equal subunits with molecular mass of 110 kDa. Protein sequence analysis revealed the presence of an &quot;SR&quot; (Ser(57)-Arg(58)) motif for the DNA binding site at the N-terminal region and the &quot;GTIAGDDTV&quot; motif for arginine binding and its oligomerization at the C-terminal region. An argC or argG promoter-lacZ fusion reporter assay and argR mutational analysis showed that transcription of the argCJBDFR arginine biosynthesis genes is regulated from the argC promoter by ArgR in cooperation with L: -arginine in C. glutamicum. This finding was supported by the gel mobility-shift assa...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4859061</comments>
            <pubDate>Tue, 10 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4859061</guid>        </item>
        <item>
            <title>Cell physiology rather than enzyme kinetics can determine the efficiency of cytochrome P450-catalyzed C-H-oxyfunctionalization.</title>
            <link>http://www.medworm.com/index.php?rid=4859060&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21559976%26dopt%3DAbstract</link>
            <description>Authors: Cornelissen S, Liu S, Deshmukh AT, Schmid A, Bühler B
    Cell physiology is a critical factor determining the efficiency of reactions performed by microbial biocatalysts. In order to develop an efficient biotransformation procedure for the hydroxylation of (S)-limonene to (S)-perillyl alcohol by recombinant Pseudomonas putida cells harboring the cytochrome P450 monooxygenase CYP153A6, physiological parameters were optimized. The previously reported synthesis of (S)-perillyl alcohol by P. putida GPo12 was based on complex and sensitive octane feeding strategies (van Beilen et al. in Appl Environ Microbiol 71:1737-1744, 2005), indicating the pivotal role of cell physiology. In contrast to previous findings, the screening of different carbon sources showed that glycerol and citrate...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4859060</comments>
            <pubDate>Tue, 10 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4859060</guid>        </item>
        <item>
            <title>Effect of Zn(II) on the reduction and accumulation of Cr(VI) by Arthrobacter species.</title>
            <link>http://www.medworm.com/index.php?rid=4804497&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21547698%26dopt%3DAbstract</link>
            <description>This study assessed the potential of two Gram-positive, Cr(VI)-reducing, aerobic bacterial strains belonging to Arthrobacter genera, which were isolated from basalt samples taken from the most polluted region of the Republic of Georgia, to remediate Cr(VI) in environments in the presence of Zn(II). Our batch experiments revealed that the addition of Zn(II) to the tested bacterial cells significantly enhanced the accumulation of Cr. According to electron spin resonance (ESR) measurements, the presence of Zn(II) ions did not change the nature of Cr(V) and Cr(III) complexes generated during the microbial reduction of Cr(VI). The efficiency of Cr(VI) reduction also remained unchanged after the addition of 50 mg/l of Zn(II) to the bacterial cells. However, at high concentrations of Zn(II) (hig...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4804497</comments>
            <pubDate>Thu, 05 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4804497</guid>        </item>
        <item>
            <title>Development of L: -tryptophan production strains by defined genetic modification in Escherichia coli.</title>
            <link>http://www.medworm.com/index.php?rid=4804498&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21541714%26dopt%3DAbstract</link>
            <description>Authors: Zhao ZJ, Zou C, Zhu YX, Dai J, Chen S, Wu D, Wu J, Chen J
    Construction and improvement of industrial strains play a central role in the commercial development of microbial fermentation processes. L: -tryptophan producers have usually been developed by classical random mutagenesis due to its complicated metabolic network and regulatory mechanism. However, in the present study, an L: -tryptophan overproducing Escherichia coli strain was developed by defined genetic modification methodology. Feedback inhibitions of 3-deoxy-D: -arabinoheptulosonate 7-phosphate synthase (AroF) and anthranilate synthase (TrpED) were eliminated by site-directed mutagenesis. Expression of deregulated AroF and TrpED was achieved by using a temperature-inducible expression plasmid pSV. Transcriptional r...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4804498</comments>
            <pubDate>Tue, 03 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4804498</guid>        </item>
        <item>
            <title>Alcoholic fermentation by wild-type Hansenula polymorpha and Saccharomyces cerevisiae versus recombinant strains with an elevated level of intracellular glutathione.</title>
            <link>http://www.medworm.com/index.php?rid=4804501&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21528412%26dopt%3DAbstract</link>
            <description>Authors: Grabek-Lejko D, Kurylenko OO, Sibirny VA, Ubiyvovk VM, Penninckx M, Sibirny AA
    The ability of baker's yeast Saccharomyces cerevisiae and of the thermotolerant methylotrophic yeast Hansenula polymorpha to produce ethanol during alcoholic fermentation of glucose was compared between wild-type strains and recombinant strains possessing an elevated level of intracellular glutathione (GSH) due to overexpression of the first gene of GSH biosynthesis, gamma-glutamylcysteine synthetase, or of the central regulatory gene of sulfur metabolism, MET4. The analyzed strains of H. polymorpha with an elevated pool of intracellular GSH were found to accumulate almost twice as much ethanol as the wild-type strain during glucose fermentation, in contrast to GSH1-overexpressing S. cerevisiae st...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4804501</comments>
            <pubDate>Thu, 28 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4804501</guid>        </item>
        <item>
            <title>Engineering lower inhibitor affinities in β-D: -xylosidase of Selenomonas ruminantium by site-directed mutagenesis of Trp145.</title>
            <link>http://www.medworm.com/index.php?rid=4804500&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21528413%26dopt%3DAbstract</link>
            <description>Authors: Jordan DB, Wagschal K, Fan Z, Yuan L, Braker JD, Heng C
    β-D: -Xylosidase/α-L: -arabinofuranosidase from Selenomonas ruminantium is the most active enzyme reported for catalyzing hydrolysis of 1,4-β-D: -xylooligosaccharides to D: -xylose. One property that could use improvement is its relatively high affinities for D: -glucose and D: -xylose (K (i) ~ 10 mM), which would impede its performance as a catalyst in the saccharification of lignocellulosic biomass for the production of biofuels and other value-added products. Previously, we discovered that the W145G variant expresses K (i) ( d-glucose) and K (i) ( d-xylose) twofold and threefold those of the wild-type enzyme. However, in comparison to the wild type, the variant expresses 11% lower k (cat) ( d-xylobiose) and much ...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4804500</comments>
            <pubDate>Thu, 28 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4804500</guid>        </item>
        <item>
            <title>Effect of biostimulation on the microbial community in PCB-contaminated sediments through periodic amendment of sediment with iron.</title>
            <link>http://www.medworm.com/index.php?rid=4804499&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21528414%26dopt%3DAbstract</link>
            <description>In this study, the effect of periodic amendment of sediment with various dosages of iron on the microbial community present in sediment was investigated using phospholipid fatty acid analysis (PLFA) over a period of 18 months. Three PCB-contaminated sediments (two freshwater lake sediments and one marine sediment) were used. Signature biomarker analysis of the microbial community present in all three sediments revealed the enrichment of Dehalococcoides species, the population of which was sustained for a longer period of time when the sediment microcosms were amended with the lower dosage of iron (0.01 g iron per g dry sediment) every 6 months as compared to the blank system (without iron). Lower microbial stress levels were reported for the system periodically amended with 0.01 g of i...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4804499</comments>
            <pubDate>Thu, 28 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4804499</guid>        </item>
        <item>
            <title>Engineering microbial factories for synthesis of value-added products.</title>
            <link>http://www.medworm.com/index.php?rid=4804502&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21526386%26dopt%3DAbstract</link>
            <description>Authors: Du J, Shao Z, Zhao H
    Microorganisms have become an increasingly important platform for the production of drugs, chemicals, and biofuels from renewable resources. Advances in protein engineering, metabolic engineering, and synthetic biology enable redesigning microbial cellular networks and fine-tuning physiological capabilities, thus generating industrially viable strains for the production of natural and unnatural value-added compounds. In this review, we describe the recent progress on engineering microbial factories for synthesis of valued-added products including alkaloids, terpenoids, flavonoids, polyketides, non-ribosomal peptides, biofuels, and chemicals. Related topics on lignocellulose degradation, sugar utilization, and microbial tolerance improvement will also be di...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4804502</comments>
            <pubDate>Wed, 27 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4804502</guid>        </item>
        <item>
            <title>Bioethanol production from tension and opposite wood of Eucalyptus globulus using organosolv pretreatment and simultaneous saccharification and fermentation.</title>
            <link>http://www.medworm.com/index.php?rid=4804503&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21523448%26dopt%3DAbstract</link>
            <description>Authors: Muñoz C, Baeza J, Freer J, Mendonça RT
    During tree growth, hardwoods can initiate the formation of tension wood, which is a strongly stressed wood on the upper side of the stem and branches. In Eucalyptus globulus, tension wood presents wider and thicker cell walls with low lignin, similar glucan and high xylan content, as compared to opposite wood. In this work, tension and opposite wood of E. globulus trees were separated and evaluated for the production of bioethanol using ethanol/water delignification as pretreatment followed by simultaneous saccharification and fermentation (SSF). Low residual lignin and high glucan retention was obtained in organosolv pulps of tension wood as compared to pulps from opposite wood at the same H-factor of reaction. The faster delignificat...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4804503</comments>
            <pubDate>Tue, 26 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4804503</guid>        </item>
        <item>
            <title>Metabolic engineering of Escherichia coli for improving L: -3,4-dihydroxyphenylalanine (L: -DOPA) synthesis from glucose.</title>
            <link>http://www.medworm.com/index.php?rid=4804504&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21512819%26dopt%3DAbstract</link>
            <description>Authors: Muñoz AJ, Hernández-Chávez G, de Anda R, Martínez A, Bolívar F, Gosset G
    L: -3,4-dihydroxyphenylalanine (L: -DOPA) is an aromatic compound employed for the treatment of Parkinson's disease. Metabolic engineering was applied to generate Escherichia coli strains for the production of L: -DOPA from glucose by modifying the phosphoenolpyruvate:sugar phosphotransferase system (PTS) and aromatic biosynthetic pathways. Carbon flow was directed to the biosynthesis of L: -tyrosine (L: -Tyr), an L: -DOPA precursor, by transforming strains with compatible plasmids carrying genes encoding a feedback-inhibition resistant version of 3-deoxy-D: -arabino-heptulosonate-7-phosphate synthase, transketolase, the chorismate mutase domain from chorismate mutase-prephenate dehydratase from E. c...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4804504</comments>
            <pubDate>Thu, 21 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4804504</guid>        </item>
        <item>
            <title>Extracellular production of beta-amylase by a halophilic isolate, Halobacillus sp. LY9.</title>
            <link>http://www.medworm.com/index.php?rid=4804506&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21505914%26dopt%3DAbstract</link>
            <description>Authors: Li X, Yu HY
    A moderately halophilic strain LY9 with high amylolytic activity was isolated from soil sample obtained from Yuncheng, China. Biochemical and physiological characterization along with 16S rRNA sequence analysis placed the isolate in the genus Halobacillus. Amylase production started from the post-exponential phase of bacterial growth and reached a maximum level during the early-stationary phase. The isolate LY9 was found to secrete the amylase, the production of which depended on the salinity of the growth medium. Maximum amylase production was observed in the presence of 10% KCl or 10% NaCl. Maltose was the main product of soluble starch hydrolysis, indicating a β-amylase activity. The enzyme showed optimal activity at 60°C, pH 8.0, and 10-12.5% of NaCl. It was ...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4804506</comments>
            <pubDate>Tue, 19 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4804506</guid>        </item>
        <item>
            <title>Influence of cultivation procedure for Saccharomyces cerevisiae used as pitching agent in industrial spent sulphite liquor fermentations.</title>
            <link>http://www.medworm.com/index.php?rid=4804505&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21505915%26dopt%3DAbstract</link>
            <description>This study therefore suggests that exposure to SSL in combination with nutrients, prior to the fermentation step, is crucial for the performance of the yeast. Supplying 0.5 g/l fresh yeast cultivated under appropriate cultivation conditions may increase ethanol concentration more than 200%.
    PMID: 21505915 [PubMed - as supplied by publisher] (Source: Journal of Industrial Microbiology and Biotechnology)</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4804505</comments>
            <pubDate>Tue, 19 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4804505</guid>        </item>
        <item>
            <title>Simultaneous production and partitioning of heterologous polyketide and isoprenoid natural products in an Escherichia coli two-phase bioprocess.</title>
            <link>http://www.medworm.com/index.php?rid=4804507&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21487833%26dopt%3DAbstract</link>
            <description>In this study, we have developed a platform E. coli strain capable of simultaneous production of both product precursors at titers greater than 15 mg l(-1). The utilization of a two-phase batch bioreactor allowed for very strong in situ separation (having a partitioning coefficient of greater than 5,000), which would facilitate downstream purification processes. The system developed here could also be used in metagenomic studies to screen environmental DNA for natural product discovery and preliminary production experiments.
    PMID: 21487833 [PubMed - as supplied by publisher] (Source: Journal of Industrial Microbiology and Biotechnology)</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4804507</comments>
            <pubDate>Tue, 12 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4804507</guid>        </item>
        <item>
            <title>Alkaliphilic bacteria: applications in industrial biotechnology.</title>
            <link>http://www.medworm.com/index.php?rid=4697594&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21479938%26dopt%3DAbstract</link>
            <description>Authors: Sarethy IP, Saxena Y, Kapoor A, Sharma M, Sharma SK, Gupta V, Gupta S
    Alkaliphiles are interesting groups of extremophilic organisms that thrive at pH of 9.0 and above. Many of their products, in particular enzymes, have found widespread applications in industry, primarily in the detergent and laundry industries. While the enzymes have been a runaway success from the industrial point of view, many more products have been reported from alkaliphiles such as antibiotics and carotenoids. Less known are their potential for degradation of xenobiotics. They also play a key role in biogeocycling of important inorganic compounds. This review provides an insight into the huge diversity of alkaliphilic bacteria, the varied products obtained from them, and the need for further investigati...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4697594</comments>
            <pubDate>Sun, 10 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4697594</guid>        </item>
        <item>
            <title>Interactions of fungi from fermented sausage with regenerated cellulose casings.</title>
            <link>http://www.medworm.com/index.php?rid=4697595&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21465179%26dopt%3DAbstract</link>
            <description>Authors: Sreenath HK, Jeffries TW
    This research examined cellulolytic effects of fungi and other microbes present in cured sausages on the strength and stability of regenerated cellulose casings (RCC) used in the sausage industry. Occasionally during the curing process, RCC would split or fail, thereby leading to loss of product. The fungus Penicillium sp. BT-F-1, which was isolated from fermented sausages, and other fungi, which were introduced to enable the curing process, produced small amounts of cellulases on RCC in both liquid and solid cultivations. During continued incubation for 15-60 days in solid substrate cultivation (SSC) on RCC support, the fungus Penicillium sp isolate BT-F-1 degraded the casings' dry weights by 15-50% and decreased their tensile strengths by ~75%. Simi...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4697595</comments>
            <pubDate>Mon, 04 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4697595</guid>        </item>
        <item>
            <title>Characterization of wines produced by mixed culture of autochthonous yeasts and Oenococcus oeni from the northwest region of Argentina.</title>
            <link>http://www.medworm.com/index.php?rid=4697598&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21461745%26dopt%3DAbstract</link>
            <description>Authors: Mendoza LM, Merín MG, Morata VI, Farías ME
    Two autochthonous yeasts from the northwest region of Argentina, Kloeckera apiculata mc1 and Saccharomyces cerevisiae mc2, were used as pure or mixed starter cultures in microvinification trials conducted in Malbec red must. Also, the effect of Oenococcus oeni X(2)L was evaluated. S. cerevisiae mc2 showed adequate growth and fermentative activity in single and composite fermentations, producing standard concentration of ethanol. The amount of esters was higher in fermentations conducted using mixed yeast starters. Independent of the timing of inoculation of O. oeni, this malolactic bacterium completely depleted malic acid. Sensory evaluation indicated that young wines fermented with mixed yeast cultures and sequential inoculation of...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4697598</comments>
            <pubDate>Fri, 01 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4697598</guid>        </item>
        <item>
            <title>Effects of polarization in the presence and absence of biocides on biofilms in a simulated paper machine water.</title>
            <link>http://www.medworm.com/index.php?rid=4697597&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21461746%26dopt%3DAbstract</link>
            <description>Authors: Peltola M, Kuosmanen T, Sinkko H, Vesalainen N, Pulliainen M, Korhonen P, Partti-Pellinen K, Räsänen JP, Rintala J, Kolari M, Rita H, Salkinoja-Salonen M
    The antifouling potential of electric polarization combined and not combined with biocides was studied in nonsaline warm water with high organic content. Deinococcus geothermalis is a bacterium known for forming colored biofilms in paper machines and for its persistence against cleaning and chemical treatments. When D. geothermalis biofilms grown for 24 h in simulated paper machine water were exposed to cathodic or cathodically weighted pulsed polarization at least 60% (P &amp;lt; 0.05) of the biofilms were removed from stainless steel (AISI 316L). Biofilm removal by 25 ppm (effective substances 5-25 ppm) of oxidizing bioc...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4697597</comments>
            <pubDate>Fri, 01 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4697597</guid>        </item>
        <item>
            <title>Introducing process analytical technology (PAT) in filamentous cultivation process development: comparison of advanced online sensors for biomass measurement.</title>
            <link>http://www.medworm.com/index.php?rid=4697596&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21461747%26dopt%3DAbstract</link>
            <description>Authors: Rønnest NP, Stocks SM, Eliasson Lantz A, Gernaey KV
    The recent process analytical technology (PAT) initiative has put an increased focus on online sensors to generate process-relevant information in real time. Specifically for fermentation, however, introduction of online sensors is often far from straightforward, and online measurement of biomass is one of the best examples. The purpose of this study was therefore to compare the performance of various online biomass sensors, and secondly to demonstrate their use in early development of a filamentous cultivation process. Eight Streptomyces coelicolor fed-batch cultivations were run as part of process development in which the pH, the feeding strategy, and the medium composition were varied. The cultivations were monitored in s...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4697596</comments>
            <pubDate>Fri, 01 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4697596</guid>        </item>
        <item>
            <title>Identification of a xylulokinase catalyzing xylulose phosphorylation in the xylose metabolic pathway of Kluyveromyces marxianus NBRC1777.</title>
            <link>http://www.medworm.com/index.php?rid=4697600&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21451977%26dopt%3DAbstract</link>
            <description>Authors: Wang R, Zhang L, Wang D, Gao X, Hong J
    Xylulokinase is one of the key enzymes in xylose metabolism and fermentation, and fine-tuned expression of xylulokinase can improve xylose fermentation in yeast. To improve the efficiency of xylose fermentation in Kluyveromyces marxianus, the gene KmXYL3, which encodes a D: -xylulokinase (E.C. 2.7.1.17), was isolated from K. marxianus NBRC1777. KmXYL3 was expressed in Escherichia coli BL21 (DE3) cells, and the specific activity of the resulting recombinant purified xylulokinase was 23.5 mU/mg. Disruption of KmXYL3 resulted in both loss of xylitol utilization and marked decrease in xylose utilization, proving that KmXYL3 encodes a xylulokinase that catalyzes the reaction from xylulose to xylulose 5-phosphate in the xylose metabolic pathw...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4697600</comments>
            <pubDate>Wed, 30 Mar 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4697600</guid>        </item>
        <item>
            <title>Effects of Orange II and Sudan III azo dyes and their metabolites on Staphylococcus aureus.</title>
            <link>http://www.medworm.com/index.php?rid=4697599&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21451978%26dopt%3DAbstract</link>
            <description>Authors: Pan H, Feng J, Cerniglia CE, Chen H
    Azo dyes are widely used in the plastic, paper, cosmetics, food, and pharmaceutical industries. Some metabolites of these dyes are potentially genotoxic. The toxic effects of azo dyes and their potential reduction metabolites on Staphylococcus aureus ATCC BAA 1556 were studied. When the cultures were incubated with 6, 18, and 36 μg/ml of Orange II and Sudan III for 48 h, 76.3, 68.5, and 61.7% of Orange II and 97.8, 93.9, and 75.8% of Sudan III were reduced by the bacterium, respectively. In the presence of 36 μg/ml Sudan III, the cell viability of the bacterium decreased to 61.9% after 48 h of incubation, whereas the cell viability of the control culture without the dye was 71.5%. Moreover, the optical density of the bacterial cultures...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4697599</comments>
            <pubDate>Wed, 30 Mar 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4697599</guid>        </item>
        <item>
            <title>Encapsulation of Pannonibacter phragmitetus LSSE-09 in alginate-carboxymethyl cellulose capsules for reduction of hexavalent chromium under alkaline conditions.</title>
            <link>http://www.medworm.com/index.php?rid=4697601&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21442414%26dopt%3DAbstract</link>
            <description>Authors: Xu L, Luo M, Yang L, Wei X, Lin X, Liu H
    Cr(VI) was efficiently reduced to Cr(III) by Pannonibacter phragmitetus LSSE-09 encapsulated in liquid-core alginate-carboxymethyl cellulose capsules under alkaline conditions. Taking into account the physical properties of the capsules, the activity of encapsulated cells, and total Cr(III) concentration in the supernatant, optimal conditions (0.5% w/v sodium alginate; 2% w/v sodium carboxymethyl cellulose; 0.1 M CaCl(2); 30-min gelation time) for LSSE-09 encapsulation were determined. At optimal conditions, a relatively high reduction rate of 4.20 mg g ((dry weight)) (-1)  min(-1) was obtained. Total Cr(III) concentration in the supernatant was significantly decreased after reduction, because 63.7% of the formed soluble organo-Cr(I...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4697601</comments>
            <pubDate>Sun, 27 Mar 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4697601</guid>        </item>
        <item>
            <title>Isolation and characterization of tetrachloroethylene- and cis-1,2-dichloroethylene-dechlorinating propionibacteria.</title>
            <link>http://www.medworm.com/index.php?rid=4639654&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21437617%26dopt%3DAbstract</link>
            <description>Authors: Chang YC, Ikeutsu K, Toyama T, Choi D, Kikuchi S
    Two rapidly growing propionibacteria that could reductively dechlorinate tetrachloroethylene (PCE) and cis-1,2-dichloroethylene (cis-DCE) to ethylene were isolated from environmental sediments. Metabolic characterization and partial sequence analysis of their 16S rRNA genes showed that the new isolates, designated as strains Propionibacterium sp. HK-1 and Propionibacterium sp. HK-3, did not match any known PCE- or cis-DCE-degrading bacteria. Both strains dechlorinated relatively high concentrations of PCE (0.3 mM) and cis-DCE (0.52 mM) under anaerobic conditions without accumulating toxic intermediates during incubation. Cell-free extracts of both strains catalyzed PCE and cis-DCE dechlorination; degradation was accelerated by...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4639654</comments>
            <pubDate>Fri, 25 Mar 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4639654</guid>        </item>
        <item>
            <title>The effect of cyclodextrins on the ethanol tolerance of microorganisms suggests potential application.</title>
            <link>http://www.medworm.com/index.php?rid=4639655&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21431889%26dopt%3DAbstract</link>
            <description>Authors: Liang Q, Wang Q, Gao C, Wang Z, Qi Q
    Cyclodextrins (CDs) are used in food, pharmaceutical, and chemical industries, as well as agriculture and environmental engineering. Cyclodextrin glucanotransferase (CGTase) is an important industrial extracellular enzyme which is used to produce CDs and oligosaccharides. We previously developed a novel yeast-surface CGTase expression system which was used for the production of CDs from starch. In the present study, we showed that the presence of CDs may increase the ethanol tolerance of microorganisms. The cell numbers of Saccharomyces cerevisiae and Escherichia coli in the presence of β-cyclodextrin and ethanol were 1,000-fold and 10-fold higher than that without CDs. The yeast strain with the immobilized CGTase produced 13 g CDs/l and ...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4639655</comments>
            <pubDate>Thu, 24 Mar 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4639655</guid>        </item>
        <item>
            <title>Cinnamic acid production using Streptomyces lividans expressing phenylalanine ammonia lyase.</title>
            <link>http://www.medworm.com/index.php?rid=4639657&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21424686%26dopt%3DAbstract</link>
            <description>Authors: Noda S, Miyazaki T, Miyoshi T, Miyake M, Okai N, Tanaka T, Ogino C, Kondo A
    Cinnamic acid production was demonstrated using Streptomyces as a host. A gene encoding phenylalanine ammonia lyase (PAL) from Streptomyces maritimus was introduced into Streptomyces lividans, and its expression was confirmed by Western blot analysis. After 4 days cultivation using glucose as carbon source, the maximal level of cinnamic acid reached 210 mg/L. When glycerol (30 g/L) was used as carbon source, the maximal level of produced cinnamic acid reached 450 mg/L. In addition, using raw starch, xylose or xylan as carbon source, the maximal level of cinnamic acid reached 460, 300, and 130 mg/L, respectively. We demonstrated that S. lividans has great potential to produce cinnamic acid as well...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4639657</comments>
            <pubDate>Tue, 22 Mar 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4639657</guid>        </item>
        <item>
            <title>Xylitol production from DEO hydrolysate of corn stover by Pichia stipitis YS-30.</title>
            <link>http://www.medworm.com/index.php?rid=4639656&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21424687%26dopt%3DAbstract</link>
            <description>Authors: Rodrigues RC, Kenealy WR, Jeffries TW
    Corn stover that had been treated with vapor-phase diethyl oxalate released a mixture of mono- and oligosaccharides consisting mainly of xylose and glucose. Following overliming and neutralization, a D: -xylulokinase mutant of Pichia stipitis, FPL-YS30 (xyl3-∆1), converted the stover hydrolysate into xylitol. This research examined the effects of phosphoric or gluconic acids used for neutralization and urea or ammonium sulfate used as nitrogen sources. Phosphoric acid improved color and removal of phenolic compounds. D: -Gluconic acid enhanced cell growth. Ammonium sulfate increased cell yield and maximum specific cell growth rate independently of the acid used for neutralization. The highest xylitol yield (0.61 g(xylitol)/g(xylose)) an...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4639656</comments>
            <pubDate>Tue, 22 Mar 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4639656</guid>        </item>
        <item>
            <title>Biosynthesis of plant-specific phenylpropanoids by construction of an artificial biosynthetic pathway in Escherichia coli.</title>
            <link>http://www.medworm.com/index.php?rid=4639658&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21424580%26dopt%3DAbstract</link>
            <description>In this study, engineered Escherichia coli containing artificial phenylpropanoid biosynthetic pathways utilizing tyrosine as the initial precursor were established for production of plant-specific metabolites such as ferulic acid, naringenin, and resveratrol. The construction of the artificial pathway utilized tyrosine ammonia lyase and 4-coumarate 3-hydroxylase from Saccharothrix espanaensis, cinnamate/4-coumarate:coenzyme A ligase from Streptomyces coelicolor, caffeic acid O-methyltransferase and chalcone synthase from Arabidopsis thaliana, and stilbene synthase from Arachis hypogaea.
    PMID: 21424580 [PubMed - as supplied by publisher] (Source: Journal of Industrial Microbiology and Biotechnology)</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4639658</comments>
            <pubDate>Sun, 20 Mar 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4639658</guid>        </item>
        <item>
            <title>Optimization of culture conditions in CO(2) fixation for succinic acid production using Actinobacillus succinogenes.</title>
            <link>http://www.medworm.com/index.php?rid=4639659&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21416273%26dopt%3DAbstract</link>
            <description>Authors: Xi YL, Chen KQ, Li J, Fang XJ, Zheng XY, Sui SS, Jiang M, Wei P
    The culture conditions in CO(2) fixation by Actinobacillus succinogenes for succinic acid production were investigated by a model of available CO(2) in a 3-l fermentor. The results from the model analysis showed that the available CO(2) for succinic acid production in the fermentation broth is the sum of HCO(3) (-), CO(3) (2-), and CO(2) influenced by external culture conditions such as medium components, CO(2) partial pressures, and temperature. The optimized conditions for CO(2) supply in a 3-l fermentor were determined as follows: CO(2) partial pressure and stirring speed were maintained at 0.1 MPa and 200 r min(-1), respectively, with a pH of 6.8 and a temperature of 37°C; 0.15 mol l(-1) NaHCO(3) was add...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4639659</comments>
            <pubDate>Thu, 17 Mar 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4639659</guid>        </item>
        <item>
            <title>Preliminary report on a catalyst derived from induced cells of Rhodococcus rhodochrous strain DAP 96253 that delays the ripening of selected climacteric fruit: bananas, avocados, and peaches.</title>
            <link>http://www.medworm.com/index.php?rid=4639663&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21409422%26dopt%3DAbstract</link>
            <description>Authors: Pierce GE, Drago GK, Ganguly S, Tucker TA, Hooker JW, Jones S, Crow SA
    Despite the use of refrigeration, improved packaging, adsorbents, and ethylene receptor blockers, on average, nearly 40% of all fruits and vegetables harvested in the US are not consumed. Many plant products, especially fruit, continue to ripen after harvesting, and as they do so, become increasingly susceptible to mechanical injury, resulting in increased rot. Other plant products during transportation and storage are susceptible to chill injury (CI). There is a real need for products that can delay ripening or mitigate the effects of CI, yet still permit full ripeness and quality to be achieved. Preliminary results are discussed where catalyst derived from cells of Rhodococcus rhodochrous DAP 96253, grown...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4639663</comments>
            <pubDate>Wed, 16 Mar 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4639663</guid>        </item>
        <item>
            <title>Process challenges relating to hematopoietic stem cell cultivation in bioreactors.</title>
            <link>http://www.medworm.com/index.php?rid=4580335&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21387081%26dopt%3DAbstract</link>
            <description>Authors: Kowalczyk M, Waldron K, Kresnowati P, Danquah MK
    Hematopoietic stem cells (HSCs) are extremely useful in treating a wide range of diseases and have a variety of useful research applications. However, the routinely generated low in vitro concentrations of HSCs from current bioreactor manufacturing systems has been a hindrance to the full-scale application of these essential cellular materials. This has made the search for novel bioreactor systems for high-concentration HSC production a major research endeavour. This review addresses process challenges in relation to bioreactor development and optimisation for high-density HSC production under effective monitoring of essential culture parameters, such as pH, dissolved oxygen and nutrient uptake. It discusses different process st...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4580335</comments>
            <pubDate>Wed, 09 Mar 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4580335</guid>        </item>
        <item>
            <title>Optimization of lipase production by Staphylococcus warneri EX17 using the polydimethylsiloxanes artificial oxygen carriers.</title>
            <link>http://www.medworm.com/index.php?rid=4525708&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21340482%26dopt%3DAbstract</link>
            <description>Authors: Rech FR, Volpato G, Ayub MA
    In this research, the combined effects of polydimethylsiloxane (PDMS) and different conditions of oxygen volumetric mass transfer coefficient (k(L)a) on lipase production by Staphylococcus warneri EX17 were studied and optimized in bioreactor cultures. Raw glycerol from biodiesel synthesis was used as the sole carbon source. Full-factorial central composite design and the response surface methodology were employed for the experimental design and analysis of the results. The optimal polydimethylsiloxane concentration and mass coefficient transfer (k(L)a) were found to be 13.5% (v/v) and 181 h(-1), respectively. Under these conditions, the maximal cell production obtained was 10.0 g/l, and the volumetric lipase activities of approximately 490 U/l, a...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4525708</comments>
            <pubDate>Tue, 22 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4525708</guid>        </item>
        <item>
            <title>An effective extracellular protein secretion by an ABC transporter system in Escherichia coli: statistical modeling and optimization of cyclodextrin glucanotransferase secretory production.</title>
            <link>http://www.medworm.com/index.php?rid=4525709&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21336875%26dopt%3DAbstract</link>
            <description>Authors: Low KO, Muhammad Mahadi N, Abdul Rahim R, Rabu A, Abu Bakar FD, Murad AM, Md Illias R
    Direct transport of recombinant protein from cytosol to extracellular medium offers great advantages, such as high specific activity and a simple purification step. This work presents an investigation on the potential of an ABC (ATP-binding cassette) transporter system, the hemolysin transport system, for efficient protein secretion in Escherichia coli (E. coli). A higher secretory production of recombinant cyclodextrin glucanotransferase (CGTase) was achieved by a new plasmid design and subsequently by optimization of culture conditions via central composite design. An improvement of at least fourfold extracellular recombinant CGTase was obtained using the new plasmid design. The optimizatio...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4525709</comments>
            <pubDate>Sat, 19 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4525709</guid>        </item>
        <item>
            <title>Analysis of experimental errors in bioprocesses. 1. Production of lactobionic acid and sorbitol using the GFOR (glucose-fructose oxidoreductase) enzyme from permeabilized cells of Zymomonas mobilis.</title>
            <link>http://www.medworm.com/index.php?rid=4525710&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21328074%26dopt%3DAbstract</link>
            <description>Authors: Júnior JB, Pinto JC, Ferraz HC, Alves TL
    The proper determination of experimental errors in bioprocesses can be very important because experimental errors can exert a major impact on the analysis of experimental results. Despite this, the effect of experimental errors on the analysis of bioprocess data has been largely overlooked in the literature. For this reason, we performed detailed statistical analyses of experimental errors obtained during the production of lactobionic acid and sorbitol in a system utilizing as catalyst the GFOR (glucose-fructose oxidoreductase) enzyme from permeabilized cells of the bacteria Zymomonas mobilis. The magnitude of the experimental errors thus obtained were then correlated with the process operation conditions and with the composition of th...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4525710</comments>
            <pubDate>Thu, 17 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4525710</guid>        </item>
        <item>
            <title>Synthesis of trimethylolpropane esters of oleic acid by Lipoprime 50T.</title>
            <link>http://www.medworm.com/index.php?rid=4525712&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21327448%26dopt%3DAbstract</link>
            <description>Authors: Kiriliauskaitė V, Bendikienė V, Juodka B
    The ability of the commercial lipolytic enzyme Lipoprime 50T to catalyze the biotechnologically important synthesis of the biodegradable and environmentally acceptable trimethylolpropane (2-ethyl-2-(hydroxymethyl)-1,3-propanediol) ester of oleic acid was investigated. Simple and accurate thin-layer chromatography and computer analysis methods were used that enable one to follow changes of all reaction mixture components simultaneously. The processes of transesterification and esterification were compared. The effects of the molar ratio of the substrates, reaction temperature, time, and medium on the composition of the reaction mixture were analyzed. Esterification was determined to be more preferable than transesterification in both s...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4525712</comments>
            <pubDate>Wed, 16 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4525712</guid>        </item>
        <item>
            <title>Hydrolytic and phosphorolytic metabolism of cellobiose by the marine aerobic bacterium Saccharophagus degradans 2-40(T).</title>
            <link>http://www.medworm.com/index.php?rid=4525711&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21327449%26dopt%3DAbstract</link>
            <description>Authors: Zhang H, Moon YH, Watson BJ, Suvorov M, Santos E, Sinnott CA, Hutcheson SW
    Saccharophagus degradans 2-40 is a marine gamma proteobacterium that can produce polyhydroxyalkanoates from lignocellulosic biomass using a complex cellulolytic system. This bacterium has been annotated to express three surface-associated β-glucosidases (Bgl3C, Ced3A, and Ced3B), two cytoplasmic β-glucosidases (Bgl1A and Bgl1B), and unusual for an aerobic bacterium, two cytoplasmic cellobiose/cellodextrin phosphorylases (Cep94A and Cep94B). Expression of the genes for each of the above enzymes was induced when cells were transferred into a medium containing Avicel as the major carbon source except for Bgl1B. Both hydrolytic and phosphorolytic degradation of cellobiose by crude cell lysates obtained fr...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4525711</comments>
            <pubDate>Sun, 13 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4525711</guid>        </item>
        <item>
            <title>Proteomic approach to enhance doxorubicin production in panK-integrated Streptomyces peucetius ATCC 27952.</title>
            <link>http://www.medworm.com/index.php?rid=4471140&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21308395%26dopt%3DAbstract</link>
            <description>Authors: Song E, Malla S, Yang YH, Lee K, Kim EJ, Lee HC, Sohng JK, Oh MK, Kim BG
    Biosynthesis of polyketide compounds depends upon the starter and extender units of coenzyme A derivatives of carboxylic acids present in the host organism. To increase the coenzyme A (CoA) pool, pantothenate kinase (panK) gene from Escherichia coli was integrated into S. peucetius ATCC 27952 (panK-integrated strain, BG200), which resulted in increase in aglycone polyketide ε-rhodomycinone (RHO), but decrease in the desired product, i.e., doxorubicin (DXR). To reduce RHO accumulation by synthesizing daunorubicin (DNR) from RHO more efficiently, glycosyltransferase (dnrQS) was overexpressed (pIBR25::dnrQS in panK-integrated strain, BG201). However, DnrQS overexpression still resulted in less production...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4471140</comments>
            <pubDate>Thu, 10 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4471140</guid>        </item>
        <item>
            <title>Expression of metallocarboxypeptidase inhibitors in Escherichia coli: effect of cysteine content and protein size in the secretory production of disulfide-bridged proteins.</title>
            <link>http://www.medworm.com/index.php?rid=4471141&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21301927%26dopt%3DAbstract</link>
            <description>Authors: Puertas JM, Caminal G, González G
    Metallocarboxypeptidase inhibitors are proteins with possible applications in biomedicine given their properties as anticoagulant and antitumoral factors. They are small, eukaryotic polypeptides comprising several disulfide bridges, which makes them hard to express in inexpensive bacterial hosts. In this work, three of them were produced in high-cell-density cultures of Escherichia coli: PCI (39 residues and three bridges), LCI (66 residues and four bridges) and TCI (75 residues and six bridges). The genes coding for the mentioned inhibitors were cloned in an arabinose-inducible plasmid fused to the signal peptide of DsbA in order to have them secreted and grant the formation of the bridges. The trigger-factor defective strain KTD101 was used...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4471141</comments>
            <pubDate>Tue, 08 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4471141</guid>        </item>
        <item>
            <title>Enhanced secreting expression and improved properties of a recombinant alkaline endoglucanase cloned in Escherichia coli.</title>
            <link>http://www.medworm.com/index.php?rid=4471142&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21298463%26dopt%3DAbstract</link>
            <description>Authors: Liu SL, Chen WZ, Liu G, Xing M
    An alkaline endoglucanase from Bacillus akibai III-3A was successfully expressed in Escherichia coli in active form, and secretion was greatly enhanced by addition of 5 g/l ethylenediamine tetraacetic acid (EDTA) to the culture medium at the induction time of 12 h. Under the optimal culture conditions, extracellular and total endoglucanase activities were 18.5 and 31.2 U/ml, respectively. Both the recombinant and native enzymes exhibited similar properties with respect to broad pH stability, good thermostability, and resistibility to various metal ions and reagents examined. However, unlike the native endoglucanase that was partly inhibited by sodium dodecyl sulfate (SDS), the recombinant enzyme had good resistibility to SDS, being very stable...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4471142</comments>
            <pubDate>Sun, 06 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4471142</guid>        </item>
        <item>
            <title>Modeling the inactivation of Bacillus subtilis spores by ethylene oxide processing.</title>
            <link>http://www.medworm.com/index.php?rid=4471145&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21298318%26dopt%3DAbstract</link>
            <description>Authors: Mendes GC, Brandão TR, Silva CL
    Ethylene oxide is currently a dominant agent in medical device sterilization. This work intends to study the main effects and interactions of temperature, ethylene oxide concentration, and relative humidity on commercial spore strips of Bacillus subtilis, var. niger (ATCC 9372) inactivation, the most common microorganism used in controlling the efficacy of the process. Experiments were carried out using a full factorial experimental design at two levels (2(3) factorial design). Limit target exposure conditions for ethylene oxide concentration, temperature, and relative humidity were 250-1,000 mg EO/l, 40-60°C, and 50-90%, respectively. Adopting a different approach from the first-order kinetics, a Gompertz model was successfully applied in da...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4471145</comments>
            <pubDate>Sat, 05 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4471145</guid>        </item>
        <item>
            <title>Gene expression profiling of a pressure-tolerant Listeria monocytogenes Scott A ctsR deletion mutant.</title>
            <link>http://www.medworm.com/index.php?rid=4471144&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21298319%26dopt%3DAbstract</link>
            <description>This study enhances our understanding of how Listeria monocytogenes survives under HHP and may contribute to the design of effective and economically feasible HHP treatment in food processing.
    PMID: 21298319 [PubMed - as supplied by publisher] (Source: Journal of Industrial Microbiology and Biotechnology)</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4471144</comments>
            <pubDate>Sat, 05 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4471144</guid>        </item>
        <item>
            <title>Application of an acid proteinase from Monascus purpureus to reduce antigenicity of bovine milk whey protein.</title>
            <link>http://www.medworm.com/index.php?rid=4471143&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21298320%26dopt%3DAbstract</link>
            <description>In this study, we investigated MpuAP's comprehensive substrate specificity, storage stability, and prospects for reducing antigenicity of whey proteins for application in the food industry. MpuAP hydrolyzed primarily five peptide bonds, Gln(4)-His(5), His(10)-Leu(11), Ala(14)-Leu(15), Gly(23)-Phe(24) and Phe(24)-Phe(25) in the oxidized insulin B-chain. The lyophilized form of the enzyme was well preserved at 30-40°C for 7 days without stabilizers. To investigate the possibility of reducing the antigenicity of the milk whey protein, enzymatic hydrolysates of the whey protein were evaluated by inhibition ELISA. Out of the three main components of whey protein, casein and α-lactalbumin were efficiently degraded by MpuAP. The sequential reaction of MpuAP and trypsin against the whey protein...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4471143</comments>
            <pubDate>Sat, 05 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4471143</guid>        </item>
        <item>
            <title>Trehalose accumulation from cassava starch and release by a highly thermosensitive and permeable mutant of Saccharomycopsis fibuligera.</title>
            <link>http://www.medworm.com/index.php?rid=4471146&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21290165%26dopt%3DAbstract</link>
            <description>Authors: Wang DS, Zhao SF, Zhao MX, Li J, Chi ZM
    Highly thermosensitive and permeable mutants are the mutants from which intracellular contents can be released when they are incubated both in low osmolarity water and at non-permissive temperature (usually 37°C). After mutagenesis by using nitrosoguanidine, a highly thermosensitive and permeable mutant named A11-b was obtained from Saccharomycopsis fibuligera A11-12, a trehalose overproducer in which the acid protease gene has been disrupted. Of the total trehalose, 73.8% was released from the mutant cells suspended in distilled water after they had been treated at 37°C overnight. However, only 10.0% of the total trehalose was released from the cells of S. fibuligera A11-12 treated under the same conditions. The cell volume of the mut...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4471146</comments>
            <pubDate>Thu, 03 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4471146</guid>        </item>
        <item>
            <title>Analysis and functional expression of NPP pathway-specific regulatory genes in Pseudonocardia autotrophica.</title>
            <link>http://www.medworm.com/index.php?rid=4402196&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21259033%26dopt%3DAbstract</link>
            <description>Authors: Jeon HG, Seo J, Lee MJ, Han K, Kim ES
    Using the genomics-guided polyene screening method, a rare actinomycetes called Pseudonocardia autotrophica was previously identified to contain functionally clustered nystatin-like biosynthetic genes and to produce a presumably novel polyene compound named nystatin-like Pseudonocardia polyene (NPP) (Kim et al., J Ind Microbiol Biotechnol 36:1425-1434, 2009). Since very low NPP productivity was observed in most P. autotrophica culture conditions, its biosynthetic pathway was proposed to be tightly regulated. Herein we report in silico analysis of six putative NPP pathway-specific regulatory genes present in its biosynthetic gene cluster, followed by functional overexpression of these regulatory genes in P. autotrophica. Three pathway-s...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4402196</comments>
            <pubDate>Sun, 23 Jan 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4402196</guid>        </item>
        <item>
            <title>Strain improvement in actinomycetes in the postgenomic era.</title>
            <link>http://www.medworm.com/index.php?rid=4402197&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21253811%26dopt%3DAbstract</link>
            <description>Authors: Baltz RH
    With the recent advances in DNA sequencing technologies, it is now feasible to sequence multiple actinomycete genomes rapidly and inexpensively. An important observation that emerged from early Streptomyces genome sequencing projects was that each strain contains genes that encode 20 or more potential secondary metabolites, only a fraction of which are expressed during fermentation. More recently, this observation has been extended to many other actinomycetes with large genomes. The discovery of a wealth of orphan or cryptic secondary metabolite biosynthetic gene clusters has suggested that sequencing large numbers of actinomycete genomes may provide the starting materials for a productive new approach to discover novel secondary metabolites. The key issue for this ap...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4402197</comments>
            <pubDate>Fri, 21 Jan 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4402197</guid>        </item>
        <item>
            <title>Cloning and knockout of phytoene desaturase gene in Sphingomonas elodea ATCC 31461 for economic recovery of gellan gum.</title>
            <link>http://www.medworm.com/index.php?rid=4402200&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21229377%26dopt%3DAbstract</link>
            <description>Authors: Zhu L, Wu X, Li O, Chen Y, Qian C, Teng Y, Tao X, Gao H
    A gene encoding phytoene desaturase (crtI) in the carotenoid biosynthetic pathway of Sphingomonas elodea ATCC 31461, an industrial gellan gum-producing strain, was cloned and identified. This gene is predicted to encode a 492-amino acid protein with significant homology to the phytoene desaturase of other carotenogenic organisms. Knockout of crtI gene blocked yellow carotenoid pigment synthesis and resulted in the accumulation of colorless phytoene, confirming that it encodes phytoene desaturase. Further research indicates that the yield of gellan gum production by crtI gene knockout mutants is almost the same as that by the wild-type strain. In addition, a recovery method based on the colorless fermentation broth of the ...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4402200</comments>
            <pubDate>Thu, 13 Jan 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4402200</guid>        </item>
        <item>
            <title>A novel dextransucrase is produced by Leuconostoc citreum strain B/110-1-2: an isolate used for the industrial production of dextran and dextran derivatives.</title>
            <link>http://www.medworm.com/index.php?rid=4402199&amp;cid=s_37320_77_f&amp;fid=37320&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21229378%26dopt%3DAbstract</link>
            <description>Authors: Fraga Vidal R, Martínez A, Moulis C, Escalier P, Morel S, Remaud-Simeon M, Monsan P
    The industrial Leuconostoc strain B/110-1-2 producing dextran and dextran derivatives was taxonomically identified by 16S rRNA as L. citreum. Its dextransucrase enzymes were characterized according to their cellular location and reaction specificity. In the presence of sucrose, the strain B/110-1-2 produced two cell-associated dextransucrases (31.54% of the total glucosyltransferase activity) with molecular weights of 160 and 240 kDa and a soluble dextransucrase (68.46%) at 160-180 kDa. Two open reading frames (ORF) coding for L. citreum strain B/110-1-2 dextransucrases were identified. One of them shared a 52% identity with the alternansucrase ASR of L. citreum NRRL B-1355 and with a putati...</description>
            <author>Journal of Industrial Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4402199</comments>
            <pubDate>Thu, 13 Jan 2011 00:00:00 +0100</pubDate>
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