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        <title>Applied Biochemistry 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 'Applied Biochemistry and Biotechnology' source.</description>
        <link><![CDATA[http://www.medworm.com/rss/search.php?qu=Applied+Biochemistry+and+Biotechnology&t=Applied+Biochemistry+and+Biotechnology&s=Search&f=source]]></link>
        <lastBuildDate>Thu, 09 Feb 2012 13:38:26 +0100</lastBuildDate>
        <item>
            <title>Surfactant-Assisted Acid Pretreatment of Sugarcane Tops for Bioethanol Production.</title>
            <link>http://www.medworm.com/index.php?rid=5671492&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22290245%26dopt%3DAbstract</link>
            <description>Authors: Sindhu R, Kuttiraja M, Binod P, Preeti VE, Sandhya SV, Vani S, Sukumaran RK, Pandey A
    Abstract
    Sugarcane tops is one of the largest biomass resources in India and in tropical countries such as Brazil in terms of surplus availability. Conversion of this feedstock to ethanol requires pretreatment to make it more accessible for the enzymes used in saccharification. Though several pretreatment regimens have been developed for addressing biomass recalcitrance, very few seem to be promising as an industrial process. A novel hybrid method involving use of mild acid and surfactant was developed which could effectively remove lignin and improve the sugar yield from sugar cane tops. Operational parameters that affect the pretreatment efficiency (measured as yield of sugars) were stu...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5671492</comments>
            <pubDate>Tue, 31 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5671492</guid>        </item>
        <item>
            <title>Enzymatic Hydrolysis of Recovered Office Printing Paper with Low Enzyme Dosages to Produce Fermentable Sugars.</title>
            <link>http://www.medworm.com/index.php?rid=5671493&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22286832%26dopt%3DAbstract</link>
            <description>Authors: Chen H, Venditti RA, Jameel H, Park S
    Abstract
    The use of recovered paper and paper manufacturing wastes are a potentially large, concentrated, and convenient raw material for ethanol production via enzyme hydrolysis and fermentation. However, many previous studies in the area have investigated impractically high enzyme charges. In this research, low dosages of enzymes on copy paper (CP) were investigated for the conditions of 5% consistency (w/v) and 50 °C for 48 h. The removal of inorganic filler (mainly calcium carbonate) by washing prior to hydrolysis led to higher sugar yields than the unwashed CP as well as CP acidified to remove the ash. Enzyme adsorption measurement showed that both acid-soluble ash and acid-insoluble ash adsorb enzymes with a greater affinity t...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5671493</comments>
            <pubDate>Sun, 29 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5671493</guid>        </item>
        <item>
            <title>Neuroprotective Effect of Phlorotannin Isolated from Ishige okamurae Against H(2)O          (2)-Induced Oxidative Stress in Murine Hippocampal Neuronal Cells, HT22.</title>
            <link>http://www.medworm.com/index.php?rid=5636644&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22281782%26dopt%3DAbstract</link>
            <description>Neuroprotective Effect of Phlorotannin Isolated from Ishige okamurae Against H(2)O     (2)-Induced Oxidative Stress in Murine Hippocampal Neuronal Cells, HT22.
    Appl Biochem Biotechnol. 2012 Jan 27;
    Authors: Heo SJ, Cha SH, Kim KN, Lee SH, Ahn G, Kang DH, Oh C, Choi YU, Affan A, Kim D, Jeon YJ
    Abstract
    The present study is designed to investigate the neuroprotective effect of a kind of phlorotannins, diphlorethohydroxycarmalol (DPHC) isolated from Ishige okamurae against hydrogen peroxide (H(2)O(2))-induced oxidative stress in murine hippocampal neuronal cells, HT22. H(2)O(2) treatment induced neurotoxicity, whereas DPHC prevented cells from H(2)O(2)-induced damage then restoring cell viability was significantly increased. DPHC slightly reduced the expression of Bax induced ...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5636644</comments>
            <pubDate>Fri, 27 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5636644</guid>        </item>
        <item>
            <title>Effects of Wort Gravity and Nitrogen Level on Fermentation Performance of Brewer's Yeast and the Formation of Flavor Volatiles.</title>
            <link>http://www.medworm.com/index.php?rid=5636643&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22281783%26dopt%3DAbstract</link>
            <description>Authors: Lei H, Zhao H, Yu Z, Zhao M
    Abstract
    Normal gravity wort and high gravity wort with different nitrogen levels were used to examine their effects on the fermentation performance of brewer's yeast and the formation of flavor volatiles. Results showed that both the wort gravity and nitrogen level had significant impacts on the growth rate, viability, flocculation, and gene expression of brewer's yeast and the levels of flavor volatiles. The sugar (glucose, maltose, and maltotriose) consumption rates and net cell growth decreased when high gravity worts were used, while these increased with increasing nitrogen level. Moreover, high gravity resulted in lower expression levels of ATF1, BAP2, BAT1, HSP12, and TDH, whereas the higher nitrogen level caused higher expression levels ...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5636643</comments>
            <pubDate>Fri, 27 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5636643</guid>        </item>
        <item>
            <title>In Vitro Gastric and Intestinal Digestions of Pulsed Light-Treated Shrimp Extracts.</title>
            <link>http://www.medworm.com/index.php?rid=5636649&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22278049%26dopt%3DAbstract</link>
            <description>In this study, PUV-treated shrimp extracts were subjected to simulated gastric fluid containing pepsin and simulated intestinal fluid containing trypsin and chymotrypsin, and then tested for changes in allergen potency. SDS-PAGE showed no major band deviation between undigested and digested PUV-treated shrimp extracts. IgE binding to tropomyosin remained markedly decreased as seen in Western blot analysis. Total shrimp allergen reactivity remained unchanged following in vitro peptic digestion and was markedly reduced following in vitro intestinal digestion as illustrated in indirect ELISA. The PUV reduced shrimp allergens remained at a low level under the in vitro simulated digestive conditions. The results inferred that PUV could be a potential method to create less allergenic shrimp prod...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5636649</comments>
            <pubDate>Thu, 26 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5636649</guid>        </item>
        <item>
            <title>Gold Nanomaterials: Preparation, Chemical Modification, Biomedical Applications and Potential Risk Assessment.</title>
            <link>http://www.medworm.com/index.php?rid=5636648&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22278050%26dopt%3DAbstract</link>
            <description>Authors: Jiang XM, Wang LM, Wang J, Chen CY
    Abstract
    Gold nanomaterials (Au NMs) have attracted increasing attention in biomedicine due to their facile preparation, multifunctional modifications, unique optical and electrical properties, and good biocompatibility. The physicochemical properties of Au NMs at nanoscale, like size, shape, surface chemistry, and near field effects, are rendering Au NMs potent candidates in biomedicine. Thus, risk assessment of negative effects of Au NMs on biological systems is becoming urgent and necessary for future applications. In this review, we summarize up-to-date progresses on the preparation and modification of Au NMs and their biomedical applications, including biosensor, bioimaging and phototherapy, gene/drug delivery. Finally, we discuss th...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5636648</comments>
            <pubDate>Thu, 26 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5636648</guid>        </item>
        <item>
            <title>Production and Characterization of Violacein by Locally Isolated Chromobacterium violaceum Grown in Agricultural Wastes.</title>
            <link>http://www.medworm.com/index.php?rid=5636647&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22278051%26dopt%3DAbstract</link>
            <description>Authors: Ahmad WA, Yusof NZ, Nordin N, Zakaria ZA, Rezali MF
    Abstract
    The present work highlighted the production of violacein by the locally isolated Chromobacterium violaceum (GenBank accession no. HM132057) in various agricultural waste materials (sugarcane bagasse, solid pineapple waste, molasses, brown sugar), as an alternative to the conventional rich medium. The highest yield for pigment production (0.82 g L(-1)) was obtained using free cells when grown in 3 g of sugarcane bagasse supplemented with 10% (v/v) of L: -tryptophan. A much lower yield (0.15 g L(-1)) was obtained when the cells were grown either in rich medium (nutrient broth) or immobilized onto sugarcane bagasse. Violacein showed similar chemical properties as other natural pigments based on the UV-Vis, Four...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5636647</comments>
            <pubDate>Thu, 26 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5636647</guid>        </item>
        <item>
            <title>Polyvinyl Alcohol-Pectin Cryogel Films for Controlled Release of Enrofloxacin.</title>
            <link>http://www.medworm.com/index.php?rid=5636646&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22278052%26dopt%3DAbstract</link>
            <description>Authors: Martinez YN, Piñuel L, Castro GR, Breccia JD
    Abstract
    The release of enrofloxacin entrapped in polyvinyl alcohol (PVA) cryogel at pH 5.5 showed a first-order kinetic, releasing 69.7% of the antibiotic after 4.5 h at 37 °C. In order to slow down the fluoroquinolone release rate, high-methoxylated pectin was added into the cryogel (PVA-P). A film containing 1.0% (w/v) HM pectin and 5.0 μg/ml enrofloxacin released only 3.7% of the antibiotic after 4.5 h. Since the FTIR spectrum showed that most of the interactions between PVA-P matrix and enrofloxacin were due to polar groups (carboxylate and amine), a two-layer film system was designed to modulate the releasing rate of the drug. The top film equilibrated with 0.75 or 1.5 M NaCl release up to 41.9% and 89.0% of the e...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5636646</comments>
            <pubDate>Thu, 26 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5636646</guid>        </item>
        <item>
            <title>Xylanase Isozymes from the Newly Isolated Bacillus sp. CKBx1D and Optimization of Its Deinking Potentiality.</title>
            <link>http://www.medworm.com/index.php?rid=5636645&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22278053%26dopt%3DAbstract</link>
            <description>In this study, the deinking effectiveness of purified xylanase from a newly isolated bacterium was evaluated for recycling of laser jet paper waste. A potent xylanases-producing bacterium from the microbial consortia of termite gut was isolated, which was further identified on the basis of 16S rRNA sequence as Bacillus sp. CKBx1D. In submerged fermentation condition, the isolate produced the highest level of xylanase (480 U/ml) at 36 h of growth. The extracellular xylanase system comprises of three distinct isozymes (est. Mw 35.28, 28.63, 18.94 kDa). The deinking of laser printed paper waste was performed using the purified enzyme mixture. Whole operational parameters were optimized using the Response Surface Methodology; it was found that at pH 6.8 with 47.2 h of continuous shaking at...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5636645</comments>
            <pubDate>Thu, 26 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5636645</guid>        </item>
        <item>
            <title>Decomposition Behavior of Hemicellulose and Lignin in the Step-Change Flow Rate Liquid Hot Water.</title>
            <link>http://www.medworm.com/index.php?rid=5636653&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22270547%26dopt%3DAbstract</link>
            <description>Authors: Zhuang X, Yu Q, Wang W, Qi W, Wang Q, Tan X, Yuan Z
    Abstract
    Hemicellulose and lignin are the main factors limiting accessibility of hydrolytic enzymes besides the crystallinity of cellulose. The decomposition behavior of hemicellulose and lignin in the step-change flow rate hot water system was investigated. Xylan removal increased from 64.53% for batch system (solid concentration 4.25% w/v, 18 min, 184°C) to 83.78% at high flow rates of 30 ml/min for 8 min, and then 10 ml/min for 10 min. Most of them (80-90%) were recovered as oligosaccharide. It was hypothesized that the flowing water could enhance the mass transfer to improve the sugars recovery. In addition, the solubilization mechanism of lignin in the liquid hot water was proposed according to the results of F...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5636653</comments>
            <pubDate>Sun, 22 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5636653</guid>        </item>
        <item>
            <title>Effect of Physicochemical Characteristics of Cellulosic Substrates on Enzymatic Hydrolysis by Means of a Multi-Stage Process for Cellobiose Production.</title>
            <link>http://www.medworm.com/index.php?rid=5636651&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22270549%26dopt%3DAbstract</link>
            <description>Authors: Vanderghem C, Jacquet N, Danthine S, Blecker C, Paquot M
    Abstract
    The effect of two types of cellulose, microcrystalline cellulose and paper pulp, on enzymatic hydrolysis for cellobiose production was investigated. The particle size, the relative crystallinity index and the water retention value were determined for both celluloses. A previously studied multistage hydrolysis process that proved to enhance the cellobiose production was studied with both types of celluloses. The cellobiose yield exhibited a significant improvement (120% for the microcrystalline cellulose and 75% for the paper pulp) with the multistage hydrolysis process compared to continuous hydrolysis. The conversion of cellulose to cellobiose was greater for the microcrystalline cellulose than for the pape...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5636651</comments>
            <pubDate>Sun, 22 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5636651</guid>        </item>
        <item>
            <title>Tannase Production by Penicillium purpurogenum PAF6 in Solid State Fermentation of Tannin-Rich Plant Residues Following OVAT and RSM.</title>
            <link>http://www.medworm.com/index.php?rid=5636650&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22270550%26dopt%3DAbstract</link>
            <description>Authors: Jana A, Maity C, Halder SK, Mondal KC, Pati BR, Mohapatra PK
    Abstract
    Tannase production by newly isolated Penicillium purpurogenum PAF6 was investigated by 'one variable at a time' (OVAT) approach followed by response surface methodology (RSM). Tannin-rich plant residues were used as supporting solid substrate and sole carbon source and, among them, tamarind seed was found to be the most favorable substrate than haritaki, pomegranate, tea leaf waste and arjun fruit. Physicochemical parameters were initially optimized using OVAT methodology and some important factors like incubation time, incubation temperature, substrate:moisture ratio as well as carbon, nitrogen and phosphate concentrations were verified with Box-Behken design of response surface methodology. Phosphate s...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5636650</comments>
            <pubDate>Sun, 22 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5636650</guid>        </item>
        <item>
            <title>Intracellular Detection and Evolution of Site-Specific Proteases Using a Genetic Selection System.</title>
            <link>http://www.medworm.com/index.php?rid=5636652&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22270548%26dopt%3DAbstract</link>
            <description>Authors: Verhoeven KD, Altstadt OC, Savinov SN
    Abstract
    Development of endoproteases, programmed to promote degradation of peptides or proteins responsible for pathogenic states, represents an attractive therapeutic strategy, since such biocatalytic agents could be directed against a potentially unlimited repertoire of extracellular proteinaceous targets. Difficulties associated with engineering enzymes with tailor-made substrate specificities have, however, hindered the discovery of proteases possessing both the efficiency and selectivity to act as therapeutics. Here, we disclose a genetic system, designed to report on site-specific proteolysis through the survival of a bacterial host, and the implementation of this method in the directed evolution of proteases with a non-native s...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5636652</comments>
            <pubDate>Sat, 21 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5636652</guid>        </item>
        <item>
            <title>Nonthermal Effect of Microwave Irradiation in Nonaqueous Enzymatic Esterification.</title>
            <link>http://www.medworm.com/index.php?rid=5618515&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22262019%26dopt%3DAbstract</link>
            <description>Authors: Wan HD, Sun SY, Hu XY, Xia YM
    Abstract
    Microwave has nonthermal effects on enzymatic reactions, mainly caused by the polarities of the solvents and substrates. In this experiment, a model reaction with caprylic acid and butanol that was catalyzed by lipase from Mucor miehei in alkanes or arenes was employed to investigate the nonthermal effect in nonaqueous enzymatic esterification. With the comparison of the esterification carried by conventional heating and consecutive microwave irradiation, the positive nonthermal effect on the initial reaction rates was found substrate concentration-dependent and could be vanished ostensibly when the substrate concentration was over 2.0 mol L(-1). The polar parameter log P well correlates the solvent polarity with the microwave effec...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5618515</comments>
            <pubDate>Fri, 20 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5618515</guid>        </item>
        <item>
            <title>Induction of Apoptosis by Ribosome Inactivating Proteins : Importance of N-glycosidase Activity.</title>
            <link>http://www.medworm.com/index.php?rid=5618514&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22262020%26dopt%3DAbstract</link>
            <description>This article reviews various experimental outcomes on the importance of N-glycosidase activity of RIPs in the induction of apoptosis.
    PMID: 22262020 [PubMed - as supplied by publisher] (Source: Applied Biochemistry and Biotechnology)</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5618514</comments>
            <pubDate>Fri, 20 Jan 2012 05:00:00 +0100</pubDate>
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        <item>
            <title>A Novel endo-1,4-β-Mannanase from Bispora antennata with Good Adaptation and Stability over a Broad pH Range.</title>
            <link>http://www.medworm.com/index.php?rid=5618518&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22258646%26dopt%3DAbstract</link>
            <description>Authors: Liu Q, Yang P, Luo H, Shi P, Huang H, Meng K, Yao B
    Abstract
    An endo-β-1,4-mannanase encoding gene, man5, was cloned from Bispora antennata CBS 126.38, which was isolated from a beech stump. The cDNA of man5 consists of 1,299 base pairs and encodes a 432-amino-acid protein with a theoretical molecular mass of 46.6 kDa. Deduced MAN5 exhibited the highest amino acid sequence identity of 58% to a β-mannanase of glycoside hydrolase family 5 from Aspergillus aculeatus. Recombinant MAN5 was expressed in Pichia pastoris and purified to electrophoretic homogeneity. The specific activity of the final preparation towards locust bean gum was 289 U mg(-1). MAN5 showed optimal activity at pH 6.0 and 70 °C and had good adaptation and stability over a broad range of pH values. The e...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5618518</comments>
            <pubDate>Thu, 19 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5618518</guid>        </item>
        <item>
            <title>Proteomic Analysis of Plasma Proteins in Diabetic Rats by 2D Electrophoresis and MALDI-TOF-MS.</title>
            <link>http://www.medworm.com/index.php?rid=5618517&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22258647%26dopt%3DAbstract</link>
            <description>Authors: Karthik D, Ilavenil S, Kaleeswaran B, Sunil S, Ravikumar S
    Abstract
    Despite tremendous advances in our understanding of the molecular basis of diabetes mellitus, substantial gaps still remain in our understanding of disease pathogenesis and in the development of effective strategies for early diagnosis and treatment. The proteomic approach has offered many opportunities and challenges in identifying new marker proteins and therapeutic targets, i.e., using 2D-polyacrylamide gel electrophoresis and matrix-assisted laser desorption/ionisation-time of flight mass spectrometry. The differential protein expressions were analyzed in alloxan-induced diabetic rats treated with Cynodon dactylon leaf extract. The plant extract was administered for 15 days that resulted in a signific...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5618517</comments>
            <pubDate>Thu, 19 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5618517</guid>        </item>
        <item>
            <title>Synthesis, Characterization and Antiproliferative Activity of 1,2-Naphthoquinone and Its Derivatives.</title>
            <link>http://www.medworm.com/index.php?rid=5618516&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22258648%26dopt%3DAbstract</link>
            <description>Authors: Shukla S, Srivastava RS, Shrivastava SK, Sodhi A, Kumar P
    Abstract
    In the present study substituted 1,2-naphthoquinones were synthesized, purified and characterized by spectroscopic studies (UV, FT-IR, (1)H NMR, (13) C NMR and elemental analysis). These compounds were evaluated for cytotoxicity against a panel of human cancer cell lines (Hep-G(2) for liver sarcoma(,) MG-63 for osteosarcoma and MCF-7 for human breast cancer). The cells were dosed with these ortho-naphthoquinone derivatives at varying concentrations, and cell viability was measured by a 3-(4,5-dimethylthiazol-2-yl)-2, 5-diphenyltetrazolium bromide (MTT) assay with doxorubicin as positive control. Significant anticancer activities were observed in vitro for some members of the series, and compounds 1,2-naph...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5618516</comments>
            <pubDate>Thu, 19 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5618516</guid>        </item>
        <item>
            <title>Isolation of Hemoglobin from Bovine Erythrocytes by Controlled Hemolysis in the Membrane Bioreactor.</title>
            <link>http://www.medworm.com/index.php?rid=5618519&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22252906%26dopt%3DAbstract</link>
            <description>Authors: Stojanović R, Ilić V, Manojlović V, Bugarski D, Dević M, Bugarski B
    Abstract
    In this work, we describe an optimized procedure based on gradual hemolysis for the isolation of hemoglobin derived from bovine slaughterhouse erythrocytes in a membrane bioreactor. The membrane bioreactor system that provided high yields of hemoglobin (mainly oxyhemoglobin derivate) and its separation from the empty erythrocyte membranes (ghosts) was designed at a pilot scale. Ten different concentrations of hypotonic media were assessed from the aspect of the extent of hemolysis, hematocrit values of the erythrocyte suspensions, cell swelling, and membrane deformations induced by decreased salt concentration. Effective gradual osmotic hemolysis with an extent of hemolysis of 88% was performe...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5618519</comments>
            <pubDate>Wed, 18 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5618519</guid>        </item>
        <item>
            <title>Substitution of the Catalytic Metal and Protein PEGylation Enhances Activity and Stability of Bacterial Phosphotriesterase.</title>
            <link>http://www.medworm.com/index.php?rid=5618522&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22249853%26dopt%3DAbstract</link>
            <description>Authors: Perezgasga L, Sánchez-Sánchez L, Aguila S, Vazquez-Duhalt R
    Abstract
    Phosphotriesterase, a pesticide-degrading enzyme, from Flavobacterium sp. was cloned and expressed in Escherichia coli. The catalytic zinc ions were replaced by cobalt atoms increasing the catalytic activity of phosphotriesterase on different pesticides. This metal substitution increased the catalytic activity from 1.4 times to 4 times according to the pesticide. In order to explain this catalytic increase, QM/MM calculations were performed. Accordingly, the HOMO energy of the substrate is closer to the LUMO energy of the cobalt-substituted enzyme. The chemical modification of the enzyme surface with poly(ethylene glycol) increased the thermostability and stability against metal chelating agents of both...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5618522</comments>
            <pubDate>Tue, 17 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5618522</guid>        </item>
        <item>
            <title>One-Step Expression and Tyrosine O-Sulfonation of Ax21 in Escherichia coli.</title>
            <link>http://www.medworm.com/index.php?rid=5618521&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22249854%26dopt%3DAbstract</link>
            <description>Authors: Shuguo H, Wei Z, Chao Z, Daoji W
    Abstract
    Ax21 (activator of Xa21-mediated immunity), a pathogen-associated molecular pattern secreted by Xanthomonas oryzae pv. oryzae, can be perceived by a membrane-located pattern recognition receptor Xa21 and triggered immune responses in rice. An Ax21-derived peptide (17-amino acid) containing a sulfated tyrosine-22 (axY(S)22) is sufficient for Ax21 activity. Here, we expressed Ax21 and O-sulfated its tyrosine-22 through coexpressing a putative tyrosine sulfotransferase, raxST, and two other genes involved in the synthesis of 3'-phosphoadenosine 5'-phosphosulfate in Escherichia coli BL21 (DE3). The sulfated Ax21 fused with a histidine tag in its N-terminus was extracted and bound onto a Ni-NTA agarose and then cleaved with Factor Xa an...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5618521</comments>
            <pubDate>Tue, 17 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5618521</guid>        </item>
        <item>
            <title>Covalent Immobilization of Cellulases onto a Water-Soluble-Insoluble Reversible Polymer.</title>
            <link>http://www.medworm.com/index.php?rid=5618520&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22249855%26dopt%3DAbstract</link>
            <description>Authors: Yu Y, Yuan J, Wang Q, Fan X, Wang P
    Abstract
    The covalent immobilization of a commercial preparation of cellulase on a reversibly soluble-insoluble enteric polymer Eudragit S-100 by carbodiimide coupling was carried out. The characteristics of covalent Eudragit cellulase were evaluated using Fourier transform infrared (FTIR) spectra, circular dichroism (CD) spectra, and fluorescence spectra. FTIR, CD, and fluorescence measurements also revealed that the cellulases were covalently bonded to the supports. Covalent Eudragit cellulase had binding efficiency of 81.08% which was higher than the noncovalent Eudragit cellulase 56.83%. The relative activity of the native cellulase and covalent Eudragit cellulase increased and reached the maximum (at pH 5.0, 50°C) and then decreas...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5618520</comments>
            <pubDate>Tue, 17 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5618520</guid>        </item>
        <item>
            <title>Selenium Enrichment on Cordyceps militaris Link and Analysis on Its Main Active Components.</title>
            <link>http://www.medworm.com/index.php?rid=5618531&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22246726%26dopt%3DAbstract</link>
            <description>Authors: Dong JZ, Lei C, Ai XR, Wang Y
    Abstract
    To investigate the effects of selenium on the main active components of Cordyceps militaris fruit bodies, selenium-enriched cultivation of C. militaris and the main active components of the fruit bodies were studied. Superoxide dismutase (SOD) activity and contents of cordycepin, cordycepic acid, and organic selenium of fruit bodies were sodium selenite concentration dependent; contents of adenosine and cordycep polysaccharides were significantly enhanced by adding sodium selenite in the substrates, but not proportional to sodium selenite concentrations. In the cultivation of wheat substrate added with 18.0 ppm sodium selenite, SOD activity and contents of cordycepin, cordycepic acid, adenosine, cordycep polysaccharides, and total am...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5618531</comments>
            <pubDate>Sat, 14 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5618531</guid>        </item>
        <item>
            <title>Constitutive Expression of Yarrowia lipolytica Lipase LIP2 in Pichia pastoris Using GAP as Promoter.</title>
            <link>http://www.medworm.com/index.php?rid=5618530&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22246727%26dopt%3DAbstract</link>
            <description>Authors: Wang X, Sun Y, Ke F, Zhao H, Liu T, Xu L, Liu Y, Yan Y
    Abstract
    A gene encoding Yarrowia lipolytica lipase LIP2 (YlLIP2) was cloned into a constitutive expression vector pGAPZαA and electrotransformed into the Pichia pastoris X-33 strain. The high-yield clones obtained by high copy and enzyme activity screening were chosen as the host strains for shaking flask and fermentor culture. The results showed that glucose was the optimum carbon source for YlLIP2 production, and the maximum hydrolytic activity of recombinant YlLIP2 reached 1,315 U/ml under the flask culture at 28 °C, pH 7.0, for 48 h. The fed-batch fermentation was carried out in 3- and 10-l bioreactors by continuously feeding glucose into the growing medium for achieving high cell density and YlLIP2 yields. ...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5618530</comments>
            <pubDate>Sat, 14 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5618530</guid>        </item>
        <item>
            <title>Keratinase Production and Biodegradation of Whole Chicken Feather Keratin by a Newly Isolated Bacterium Under Submerged Fermentation.</title>
            <link>http://www.medworm.com/index.php?rid=5618529&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22246728%26dopt%3DAbstract</link>
            <description>Authors: Sahoo DK, Das A, Thatoi H, Mondal KC, Mohapatra PK
    Abstract
    A new feather-degrading bacterium PKD 5 was isolated from feather dumping soil and identified as Bacillus weihenstephanensis based on morphological and physiochemical characteristics as well as 16S rRNA gene analysis. Extracellular keratinase was produced during submerged aerobic cultivation in a medium containing chicken feather as sole carbon and energy source and supplemented with salt solutions (NaCl 5.0, MgSO(4) 1.0, K(2)HPO(4) 1.0, (NH(4))(2)SO(4), 2.0 g/l). The optimal conditions for keratinase production include initial pH of 7.0, inoculum size of 2% (v/v), and cultivation at 40 °C. The maximum keratinase production and keratinolytic activity of PKD 5 was achieved after 7 days of fermentation under sha...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5618529</comments>
            <pubDate>Sat, 14 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5618529</guid>        </item>
        <item>
            <title>Modelling Growth and Bacteriocin Production by Pediococcus acidilactici PA003 as a Function of Temperature and pH Value.</title>
            <link>http://www.medworm.com/index.php?rid=5618527&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22246730%26dopt%3DAbstract</link>
            <description>Authors: Zhang J, Zhang Y, Liu SN, Han Y, Zhou ZJ
    Abstract
    To investigate the effect of pH and temperature on the cell growth and bacteriocin production of Pediococcus acidilactici PA003, a lactic acid bacterium isolated from traditionally fermented cabbage, the kinetic behaviour of P. acidilactici PA003 was simulated in vitro during laboratory fermentations by making use of MRS broth. Firstly, primary models were developed for cell growth, glucose consumption, lactic acid and bacteriocin production for a given set of environmental conditions. Based on primary models, further study was undertaken to fit secondary models to describe the influence of temperature and pH on microbial behaviour. The models were validated successfully for all components. The results from the cell yield c...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5618527</comments>
            <pubDate>Sat, 14 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5618527</guid>        </item>
        <item>
            <title>Atropa belladonna Hairy Roots: Orchestration of Concurrent Oxidation and Reduction Reactions for Biotransformation of Carbonyl Compounds.</title>
            <link>http://www.medworm.com/index.php?rid=5618525&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22246731%26dopt%3DAbstract</link>
            <description>Authors: Srivastava V, Negi AS, Ajayakumar PV, Khan SA, Banerjee S
    Abstract
    The biotransformation potential of a selected Atropa belladonna hairy root clone (AB-09) had been evaluated with regard to three different aromatic carbonyl compounds, i.e., 3,4,5-trimethoxybenzaldehyde (1), 3,4,5-trimethoxyacetophenone (2), and 3,4,5-trimethoxy benzoic acid (3). The results demonstrated for the first time the untapped potentials of the selected hairy root clone to perform simultaneous oxidation (34.49%) and reduction (32.68%) of 3,4,5-trimethoxy benzaldehyde (1) into 3,4,5-trimethoxy benzoic acid (3), and 3,4,5-trimethoxy benzyl alcohol (4), respectively, without any intermediate separation or addition of reagents. The same hairy root clone also demonstrated reduction (&amp;lt;5%) of a 3,4,5-t...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5618525</comments>
            <pubDate>Sat, 14 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5618525</guid>        </item>
        <item>
            <title>Design of Biosolvents Through Hydroxyl Functionalization of Compounds with High Dielectric Constant.</title>
            <link>http://www.medworm.com/index.php?rid=5618523&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22246733%26dopt%3DAbstract</link>
            <description>Authors: Ou G, He B, Yuan Y
    Abstract
    We proposed basic principles for biosolvent design on the viewpoint of ionization. Two classes of biosolvents, based on cyclic carbonate moiety and amide moiety, were designed through hydroxyl functionalization of highly dielectric compound. The newly designed compounds, glycerol carbonate (GC) and N-hydroxymethyl formamide (HOF), were synthesized for the development of soluble enzymatic systems and characterized by (13)C NMR and (1)H NMR. All the characterization data were consistent with the expected structures. Using conductance measurements, the pK           (a) values of trichloroacetic acid in GC and HOF were determined as 0.80 and 0.85 at 25.0 °C, which was very close to that in water (pK           (a) = 0.70), suggesting that the i...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5618523</comments>
            <pubDate>Sat, 14 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5618523</guid>        </item>
        <item>
            <title>Strategies to Overcome Oxygen Transfer Limitations During Hairy Root Cultivation of Azadiracta indica for Enhanced Azadirachtin Production.</title>
            <link>http://www.medworm.com/index.php?rid=5618528&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22246729%26dopt%3DAbstract</link>
            <description>Authors: Srivastava S, Srivastava AK
    Abstract
    The vast untapped potential of hairy root cultures as a stable source of biologically active chemicals has focused the attention of scientific community toward its commercial exploitation. However, the major bottleneck remains its successful scale-up. Due to branching, the roots form an interlocked matrix that exhibits resistance to oxygen transfer. Thus, present work was undertaken to develop cultivation strategies like optimization of inlet gas composition (in terms of % (v/v) O(2) in air), air-flow rate and addition of oxygen vectors in the medium, to curb the oxygen transfer limitations during hairy root cultivation of Azadirachta indica for in vitro azadirachtin (a biopesticide) production. It was found that increasing the oxygen f...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5618528</comments>
            <pubDate>Fri, 13 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5618528</guid>        </item>
        <item>
            <title>Genetically Engineered Epidermal Growth Factor Conjugate Crosses Cell Membrane.</title>
            <link>http://www.medworm.com/index.php?rid=5618524&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22246732%26dopt%3DAbstract</link>
            <description>Authors: Zhao B, Guo Y, Fu A
    Abstract
    Epidermal growth factor (EGF) is a well-known pleiotropic growth factor in mammal, and has been attempted to be used in many different fields. However, the application of EGF is limited because of its poor cell permeation. In order to increase membrane permeation ability of EGF, a genetically modified recombinant EGF (GST-TAT-EGF) was prepared through conjugation of EGF with two protein transduction domains, glutathione-S-transferase and TAT47-57. The results showed that the GST-TAT-EGF fusion protein exhibited higher ability in biomembrane penetration than that of the EGF alone. The results also implied that two different mechanisms (EGF receptor-mediated endocytosis and direct penetration) might be involved in GST-TAT-EGF transmembrane delive...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5618524</comments>
            <pubDate>Fri, 13 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5618524</guid>        </item>
        <item>
            <title>Sequential Anaerobic/Aerobic Treatment of Dye-Containing Wastewaters: Colour and COD Removals, and Ecotoxicity Tests.</title>
            <link>http://www.medworm.com/index.php?rid=5618544&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22238010%26dopt%3DAbstract</link>
            <description>Authors: da Silva ME, Firmino PI, de Sousa MR, Dos Santos AB
    Abstract
    Colour and COD removals of the azo dyes Congo Red (CR) and Reactive Black 5 (RB5) were individually evaluated in a sequential anaerobic/aerobic treatment system. Additionally, dye toxicity was assessed by using acute ecotoxicity tests with Daphnia magna as the indicator-organism. The anaerobic reactor was operated at approximately 27 °C and with hydraulic retention times of 12 and 24 h. The aerobic reactor was operated in batch mode with a total cycle of 24 h. During anaerobic step, high colour removals were obtained, 96.3% for CR (400 mg/L) and 75% for RB5 (200 mg/L). During the aerobic phase, COD effluent was considerably reduced, with an average removal efficiency of 52% for CR and 85% for RB5, which res...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5618544</comments>
            <pubDate>Thu, 12 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5618544</guid>        </item>
        <item>
            <title>ANCUT2, an Extracellular Cutinase from Aspergillus nidulans Induced by Olive Oil.</title>
            <link>http://www.medworm.com/index.php?rid=5618543&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22238011%26dopt%3DAbstract</link>
            <description>Authors: Castro-Ochoa D, Peña-Montes C, González-Canto A, Alva-Gasca A, Esquivel-Bautista R, Navarro-Ocaña A, Farrés A
    Abstract
    Cutinases are versatile carboxylic ester hydrolases with great potential in many biocatalytic processes, including biodiesel production. Genome sequence analysis of the model organism Aspergillus nidulans reveals four genes encoding putative cutinases. In this work, we purified and identified for the first time a cutinase (ANCUT2) produced by A. nidulans. ANCUT2 is a 29-kDa protein which consists of 255 amino acid residues. Comparison of the amino acid sequence of ANCUT2 with other microbial cutinase sequences revealed a high degree of homology with other fungal cutinases as well as new features, which include a serine-rich region and conserved cystein...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5618543</comments>
            <pubDate>Thu, 12 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5618543</guid>        </item>
        <item>
            <title>Biofouling Potential Reductions Using a Membrane Hybrid System as a Pre-treatment to Seawater Reverse Osmosis.</title>
            <link>http://www.medworm.com/index.php?rid=5618542&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22238012%26dopt%3DAbstract</link>
            <description>In this study, AOC method was modified to measure the growth of bacteria in seawater by using the Pseudomonas P.60 strain.
    PMID: 22238012 [PubMed - as supplied by publisher] (Source: Applied Biochemistry and Biotechnology)</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5618542</comments>
            <pubDate>Thu, 12 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5618542</guid>        </item>
        <item>
            <title>Cloning, Expression, and Characterization of a Wide-pH-Range Stable Phosphite Dehydrogenase from Pseudomonas sp. K in Escherichia coli.</title>
            <link>http://www.medworm.com/index.php?rid=5618541&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22238013%26dopt%3DAbstract</link>
            <description>Authors: Liu DF, Ding HT, Du YQ, Zhao YH, Jia XM
    Abstract
    A phosphite dehydrogenase gene (ptdhK) consisting of 1,011-bp nucleotides which encoding a peptide of 336 amino acid residues was cloned from Pseudomonas sp. K. gene ptdhK was expressed in Escherichia coli BL21 (DE3) and the corresponding recombinant enzyme was purified by metal affinity chromatography. The recombinant protein is a homodimer with a monomeric molecular mass of 37.2 kDa. The specific activity of PTDH-K was 3.49 U mg(-1) at 25 °C. The recombinant PTDH-K exhibited maximum activity at pH 3.0 and at 40 °C and displayed high stability within a wide range of pHs (5.0 to 10.5). PTDH-K had a high affinity to its natural substrates, with K           (m) values for sodium phosphite and NAD of 0.475 ± 0.073...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5618541</comments>
            <pubDate>Thu, 12 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5618541</guid>        </item>
        <item>
            <title>Kinetic Study of Empty Fruit Bunch Using Hot Liquid Water and Dilute Acid.</title>
            <link>http://www.medworm.com/index.php?rid=5618540&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22238014%26dopt%3DAbstract</link>
            <description>Authors: Kim JS, Choi WI, Kang M, Park JY, Lee JS
    Abstract
    Empty fruit bunch (EFB), a residual product of the palm plantation, is an attractive biomass for biorefinery. As xylan is susceptible to high temperature pretreatment, it is important to setup a proper pretreatment condition to maximize the sugar recovery from EFB. Kinetic parameters of mathematical models were obtained in order to predict the concentration of xylose, glucose, furfural, and acetic acid in the hydrolysate and to find production conditions of xylose. We investigated the kinetics of hot liquid water and dilute sulfuric acid hydrolysis over a 40-min period using a self-designed setup by measuring the concentrations of released sugars (xylose, glucose) and degradation products (acetic acid and furfural). The rea...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5618540</comments>
            <pubDate>Thu, 12 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5618540</guid>        </item>
        <item>
            <title>Novel Copper-Based Therapeutic Agent for Anti-Inflammatory: Synthesis, Characterization, and Biochemical Activities of Copper(II) Complexes of Hydroxyflavone Schiff Bases.</title>
            <link>http://www.medworm.com/index.php?rid=5618539&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22238015%26dopt%3DAbstract</link>
            <description>Authors: Joseph J, Nagashri K
    Abstract
    Four hydroxyflavone derivatives have been synthesized with the aim of obtaining a good model of superoxide dismutase. Better to mimic the natural metalloenzyme, copper complexes have been designed. The Cu(II) complexes of general formulae, [CuL] where L = 5-hydroxyflavone-o-phenylenediamine (L(1)H(2))/m-phenylenediamine (L(2)H(2)) and 3-hydroxyflavone-o-phenylenediamine (L(3)H(2))/m-phenylenediamine (L(4)H(2)) have been synthesized. The structural features have been determined from their analytical and spectral data. All the Cu(II) complexes exhibit square planar geometry. Redox behavior of copper complexes was studied and the present ligand systems stabilize the unusual oxidation state of the copper ion during electrolysis. The in vitro a...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5618539</comments>
            <pubDate>Thu, 12 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5618539</guid>        </item>
        <item>
            <title>Enhanced Ammonia Content in Compost Leachate Processed by Black Soldier Fly Larvae.</title>
            <link>http://www.medworm.com/index.php?rid=5618538&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22238016%26dopt%3DAbstract</link>
            <description>Authors: Green TR, Popa R
    Abstract
    Black soldier fly (BSF) larvae (Hermetia illucens), feeding on leachate from decaying vegetable and food scrap waste, increase ammonia (NH             (4)                  (+)           ) concentration five- to sixfold relative to leachate unprocessed by larvae. NH             (4)                  (+)            in larva-processed leachate reached levels as high as ∼100 mM. Most of this NH             (4)                  (+)            appears to have come from organic nitrogen within the frass produced by the larvae as they fed on leachate. In nitrate-enriched solutions, BSF larvae also facilitate dissimilatory nitrate reduction to ammonia. The markedly higher concentration of NH             (4)                  (+)            recovered in le...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5618538</comments>
            <pubDate>Thu, 12 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5618538</guid>        </item>
        <item>
            <title>Improved Mass Multiplication of Rhodiola crenulata Shoots Using Temporary Immersion Bioreactor with Forced Ventilation.</title>
            <link>http://www.medworm.com/index.php?rid=5618537&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22238017%26dopt%3DAbstract</link>
            <description>Authors: Zhao Y, Sun W, Wang Y, Saxena PK, Liu CZ
    Abstract
    A temporary immersion bioreactor system was found to be suitable for mass shoot proliferation of Rhodiola crenulata. The shoot multiplication ratio and hyperhydration rate reached 46.8 and 35.4%, respectively, at a temporary immersion cycle of 3-min immersion every 300 min. Forced ventilation was employed in the temporary immersion bioreactor culture in order to decrease the hyperhydration rate, improve shoot quality and enhance the multiplication ratio. The highest multiplication ratio of 55.7 was obtained under a temporary immersion cycle of 3-min immersion every 180 min with the forced ventilation at an air flow rate of 40 l/h, and the hyperhydration rate was reduced to 26.1%. Forced ventilation also improved the subs...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5618537</comments>
            <pubDate>Thu, 12 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5618537</guid>        </item>
        <item>
            <title>Biomarkers in Catfish Sciades herzbergii (Teleostei: Ariidae) from Polluted and Non-polluted Areas (São Marcos' Bay, Northeastern Brazil).</title>
            <link>http://www.medworm.com/index.php?rid=5618545&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22228406%26dopt%3DAbstract</link>
            <description>Authors: Carvalho-Neta RN, Torres AR, Abreu-Silva AL
    Abstract
    Biomarkers based on specific enzyme activities and histological alterations are useful tools for evaluating toxicological effects of xenobiotics in wild fish. In this work, an experimental system of biomarkers with enzyme glutathione S-transferase (GST) and branchial lesions in catfish (Sciades herzbergii) was mathematically modeled. The fish were collected along known pollution gradients (S1) and from areas regarded relatively free of anthropogenic input (S2) in São Marcos' Bay, Brazil. GST was measured spectrophotometrically, and branchial lesions were examined by light microscope. The databases from this analysis were compiled, and non-linear models were used to analyze the dependence of the enzyme activity on the ar...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5618545</comments>
            <pubDate>Sat, 07 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5618545</guid>        </item>
        <item>
            <title>Development of a Mathematical Model for Growth and Oxygen Transfer in In Vitro Plant Hairy Root Cultivations.</title>
            <link>http://www.medworm.com/index.php?rid=5576431&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22222429%26dopt%3DAbstract</link>
            <description>Authors: Palavalli RR, Srivastava S, Srivastava AK
    Abstract
    Genetically transformed, &quot;Hairy roots&quot; once developed can serve as a stable parent culture for in vitro production of plant secondary metabolites. However, the major bottleneck in the commercial exploitation of hairy roots remains its successful scale-up due to oxygen transfer limitation in three-dimensionally growing hairy root mass. Mass transfer resistances near the gas-liquid and liquid-solid boundary layer affect the oxygen delivery to the growing hairy roots. In addition, the diffusional mass transfer limitation due to increasing size of the root ball (matrix) with growth also plays a limiting role in the oxygen transfer rate. In the present study, a mathematical model is developed which describes the oxygen transfer...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5576431</comments>
            <pubDate>Fri, 06 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5576431</guid>        </item>
        <item>
            <title>Fed-batch Anaerobic Valorization of Slaughterhouse By-products with Mesophilic Microbial Consortia Without Methane Production.</title>
            <link>http://www.medworm.com/index.php?rid=5576430&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22222430%26dopt%3DAbstract</link>
            <description>Authors: Pessiot J, Nouaille R, Jobard M, Singhania RR, Bournilhas A, Christophe G, Fontanille P, Peyret P, Fonty G, Larroche C
    Abstract
    This work aimed at setting up a fully instrumented, laboratory-scale bioreactor enabling anaerobic valorization of solid substrates through hydrogen and/or volatile fatty acid (VFA) production using mixed microbial populations (consortia). The substrate used was made of meat-based wastes, especially from slaughterhouses, which are becoming available in large amounts as a consequence of the growing constraints for waste disposal from meat industry. A reconstituted microbial mesophilic consortium without Archaebacteria (methanogens), named PBr, was cultivated in a 5-L anaerobic bioreactor on slaughterhouse wastes. The experiments were carried out wi...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5576430</comments>
            <pubDate>Fri, 06 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5576430</guid>        </item>
        <item>
            <title>Purification and Characterisation of a 31-kDa Chitinase from the Myzus Persicae Aphid: A Target for Hemiptera Biocontrol.</title>
            <link>http://www.medworm.com/index.php?rid=5576429&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22222431%26dopt%3DAbstract</link>
            <description>Authors: Francis F, Saguez J, Cherqui A, Vandermoten S, Vincent C, Versali MF, Dommès J, De Pauw E, Giordanengo P, Haubruge E
    Abstract
    Hydrolytic enzymes involved in chitin degradation are important to allow moulting during insect development. Chitinases are interesting targets to disturb growth and develop alternative strategies to control insect pests. In this work, a chitinase from the aphid Myzus persicae was purified with a 36-fold purification rate in a three step procedure by ammonium sulphate fractionation, anion-exchange chromatography on a DEAE column and on an affinity Concanavalin A column. The purified chitinase purity assessed by 1D and 2D SDS-PAGE revealed a single band and three spots at 31 kDa, respectively. Chitinases were found to have high homologies with Conc...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5576429</comments>
            <pubDate>Fri, 06 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5576429</guid>        </item>
        <item>
            <title>Watermelon Rind: Agro-waste or Superior Biosorbent?</title>
            <link>http://www.medworm.com/index.php?rid=5576428&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22222432%26dopt%3DAbstract</link>
            <description>Authors: Liu C, Ngo HH, Guo W
    Abstract
    Biosorption of copper (Cu), zinc (Zn), and lead (Pb) on watermelon rind in a well-stirred batch system was investigated. pH showed significant influence on the biosorption process. Optimal pH for Cu, Zn, and Pb biosorption was found to be 5.0, 6.8 and 6.8, respectively. Watermelon rind was in favor of Pb and it could remove up to 99% Pb between pH ranges of 5 and 6.8 when Pb concentration is lower than 100 mg/L. The biosorptive capacity of watermelon on Cu, Zn, and Pb was 6.281, 6.845, and 98.063 mg/g, respectively. The equilibrium data fitted well to Langmuir adsorption isotherm while pseudo-second-order kinetic model exhibited more advantages for describing kinetic data than pseudo-first-order kinetic model. NaOH was found to be a suitable...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5576428</comments>
            <pubDate>Fri, 06 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5576428</guid>        </item>
        <item>
            <title>Regulation of Xylanase Biosynthesis in Bacillus cereus BSA1.</title>
            <link>http://www.medworm.com/index.php?rid=5576427&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22222433%26dopt%3DAbstract</link>
            <description>In this study, regulation of xylanase production was examined in Bacillus cereus BSA1. Xylanase production was induced by xylan. The enzyme production further increased in the presence of xylose and arabinose in very low concentration with addition of xylan (0.5% up to 6.02 U/ml). Addition of glucose (about 0.1%) to the media supplemented with xylan repressed xylanase production. Even higher concentration (&amp;gt;0.1%) of xylose and arabinose repressed xylanase biosynthesis. Glucose-mediated repression was partially relived by addition of cyclic adenosine monophosphate. Chemical like 2-4-dinitrophenol, which can inhibit adenosine triphosphate synthesis in cell, repressed xylanase synthesis and it suggested xylanase synthesis to be an energy dependent process.
    PMID: 22222433 [PubMed - as s...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5576427</comments>
            <pubDate>Fri, 06 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5576427</guid>        </item>
        <item>
            <title>The Construction of Glucose Biosensor Based on Platinum Nanoclusters-Multiwalled Carbon Nanotubes Nanocomposites.</title>
            <link>http://www.medworm.com/index.php?rid=5576438&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22215252%26dopt%3DAbstract</link>
            <description>Authors: Wang CY, Tan XR, Chen SH, Hu FX, Zhong HA, Zhang Y
    Abstract
    One-step synthesis method was proposed to obtain the nanocomposites of platinum nanoclusters and multiwalled carbon nanotubes (PtNCs-MWNTs), which were used as a novel immobilization matrix for the enzyme to fabricate glucose biosensor. The fabrication process of the biosensor was characterized by cyclic voltammetry, electrochemical impedance spectroscopy, atomic force microscopy and scanning electron microscope. Due to the favorable characteristic of PtNCs-MWNTs nanocomposites, the biosensor exhibited good characteristics, such as wide linear range (3.0 μM-12.1 mM), low detection limit (1.0 μM), high sensitivity (12.8 μA mM(-1)), rapid response time (within 6 s). The apparent Michaelis-Menten constant ([...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5576438</comments>
            <pubDate>Wed, 04 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5576438</guid>        </item>
        <item>
            <title>Characterization of Xyn10J, a Novel Family 10 Xylanase from a Compost Metagenomic Library.</title>
            <link>http://www.medworm.com/index.php?rid=5576432&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22215253%26dopt%3DAbstract</link>
            <description>Authors: Jeong YS, Na HB, Kim SK, Kim YH, Kwon EJ, Kim J, Yun HD, Lee JK, Kim H
    Abstract
    A gene encoding an extracellular xylanase was cloned from a compost metagenomic library. The xylanase gene, xyn10J, was 1,137 bp in length and was predicted to encode a protein of 378 amino acid residues with a putative signal peptide of 27 amino acid residues. The molecular mass of the mature Xyn10J was calculated to be 39,882 Da with a pI of 6.09. Xyn10J had a motif GVKVHFTEMDI characteristic of most members of glycosyl hydrolase family 10. The amino acid sequence of Xyn10J showed 60.0% identity to that of XynH, a xylanase from an uncultured soil bacterium and 55% identity to XylC of Cellvibrio mixtus. Site-directed mutagenesis of the expected active site based on the sequence analysis indi...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5576432</comments>
            <pubDate>Wed, 04 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5576432</guid>        </item>
        <item>
            <title>Bioactive Electroconductive Hydrogels: The Effects of Electropolymerization Charge Density on the Storage Stability of an Enzyme-Based Biosensor.</title>
            <link>http://www.medworm.com/index.php?rid=5576464&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22212391%26dopt%3DAbstract</link>
            <description>Authors: Kotanen CN, Tlili C, Guiseppi-Elie A
    Abstract
    Electrode-supported hydrogels were conferred with the biospecificity of enzymes during the process of electropolymerization to give rise to a class of bioactive, stimuli-responsive co-joined interpenetrating networks of inherently conductive polymers and highly hydrated hydrogels. Glucose responsive biotransducers were prepared by potentiostatic electropolymerization [750 mV vs. Ag/AgCl (3 M KCl)] of pyrrole at Poly(hydoxyethyl methacrylate)-based hydrogel-coated Pt micro-electrodes (Φ = 100 μm) from aqueous solutions of pyrrole and glucose oxidase (GOx; 0.4 M pyrrole, 1.0 mg/ml GOx) to 1.0 and 10.0 mC/cm(2). Polypyrrole was them over-oxidized by cyclic voltammetry (0-1.2 V vs. Ag/AgCl, 40 cycles in PBKCl, pH =...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5576464</comments>
            <pubDate>Tue, 03 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5576464</guid>        </item>
        <item>
            <title>Erratum to: Proteomic Analysis of Differential Protein Expression of Achilles Tendon in a Rabbit Model by Two-Dimensional Polyacrylamide Gel Electrophoresis at 21 Days Postoperation.</title>
            <link>http://www.medworm.com/index.php?rid=5576459&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22212392%26dopt%3DAbstract</link>
            <description>Authors: Jielile J, Jialili A, Sabirhazi G, Shawutali N, Redati D, Chen J, Tang B, Bai J, Aldyarhan K
    PMID: 22212392 [PubMed - as supplied by publisher] (Source: Applied Biochemistry and Biotechnology)</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5576459</comments>
            <pubDate>Tue, 03 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5576459</guid>        </item>
        <item>
            <title>Effect of Substrate Concentration on Dark Fermentation Hydrogen Production Using an Anaerobic Fluidized Bed Reactor.</title>
            <link>http://www.medworm.com/index.php?rid=5576457&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22212393%26dopt%3DAbstract</link>
            <description>Authors: de Amorim EL, Sader LT, Silva EL
    Abstract
    The effect of substrate (glucose) concentration on the stability and yield of a continuous fermentative process that produces hydrogen was studied. Four anaerobic fluidized bed reactors (AFBRs) were operated with a hydraulic retention time (HRT) from 1 to 8 h and an influent glucose concentration from 2 to 25 g L(-1). The reactors were inoculated with thermally pre-treated anaerobic sludge and operated at a temperature of 30 °C with an influent pH around 5.5 and an effluent pH of about 3.5. The AFBRs with a HRT of 2 h and a feed strength of 2, 4, and 10 g L(-1) showed satisfactory H(2) production performance, but the reactor fed with 25 g L(-1) of glucose did not. The highest hydrogen yield value was obtained in the re...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5576457</comments>
            <pubDate>Tue, 03 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5576457</guid>        </item>
        <item>
            <title>High pH Solubilization and Chromatography-Based Renaturation and Purification of Recombinant Human Granulocyte Colony-Stimulating Factor from Inclusion Bodies.</title>
            <link>http://www.medworm.com/index.php?rid=5576450&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22212394%26dopt%3DAbstract</link>
            <description>In this study, rhG-CSF was solubilized from inclusion bodies by using a high-pH solution containing low concentration of urea. It was found that solubilization of the rhG-CSF inclusion bodies greatly depended on the buffer pH employed; alkalic pH significantly favored the solubilization. In addition, when small amount of urea was added to the solution at high pH, the solubilization was further enhanced. After solubilization, the rhG-CSF was renatured with simultaneous purification by using weak anion exchange, strong anion exchange, and hydrophobic interaction chromatography, separately. The results indicated that the rhG-CSF solubilized by the high-pH solution containing low concentration of urea had much higher mass recovery than the one solubilized by 8 M urea when using anyone of the ...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5576450</comments>
            <pubDate>Tue, 03 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5576450</guid>        </item>
        <item>
            <title>Investigation on Ultrasound-Assisted Extraction and Separation of Enduracidin from Streptomyces sp. NJWGY3665.</title>
            <link>http://www.medworm.com/index.php?rid=5557835&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22207586%26dopt%3DAbstract</link>
            <description>Authors: Hu Y, Yang W, Wan W, Shen F, Lei Z, Wang D
    Abstract
    Ultrasound-assisted extraction of enduracidin from Streptomyces sp. NJWGY3665 was studied. The effects of various factors on the yield of target components were investigated. The results showed that the extraction by ultrasound-assisted extraction is four times faster than those by conventional solvent extraction. The results also indicated that fast extraction rate was obtained in the first 30 min, and the maximum yield was obtained at the power of 150 W. The effects of other factors such as different solvents, solvent concentration, solvent to solid ratio, and extraction batches on the field were also discussed. The optimum conditions were found at solvent of methanol, time of 30 min, power of 150 W, pH of 7.0, solv...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5557835</comments>
            <pubDate>Fri, 30 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5557835</guid>        </item>
        <item>
            <title>Exhausted Jackknife Validation Exemplified by Prediction of Temperature Optimum in Enzymatic Reaction of Cellulases.</title>
            <link>http://www.medworm.com/index.php?rid=5557834&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22207587%26dopt%3DAbstract</link>
            <description>In this study, two aims were defined (a) which amino acid property works better to predict the temperature optimum and (b) with which deletion the jackknife validation works. The results showed that the amino acid distribution probability works better in predicting the optimum temperature of catalytic reaction by cellulase, and the delete-4, more precisely one-fifth deletion, jackknife validation works better.
    PMID: 22207587 [PubMed - as supplied by publisher] (Source: Applied Biochemistry and Biotechnology)</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5557834</comments>
            <pubDate>Fri, 30 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5557834</guid>        </item>
        <item>
            <title>Kinetics of Alloxan-Induced Inhibition on δ-Aminolevulinate Dehydratase Activity in Mouse Liver Homogenates.</title>
            <link>http://www.medworm.com/index.php?rid=5557833&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22207588%26dopt%3DAbstract</link>
            <description>This study evaluated the effects of alloxan on the kinetics properties of the δ-aminolevulinate dehydratase (δ-ALA-D) using mouse liver homogenates. δ-ALA-D is an important sulfhydryl enzyme that catalyses the second step in heme biosynthesis and is commonly diminished in experimental and human diabetes. Despite the known effects of alloxan in models of experimental diabetes, there are no data in the literature demonstrating the effects of alloxan on the kinetics properties of the δ-ALA-D. The results showed that alloxan (1.25-20 μM) caused a concentration-dependent inhibition of hepatic δ-ALA-D activity. The inhibition constant (K           (             i           )) for alloxan-induced inhibition on δ-ALA-D was 3.64 μM. The alloxan (5 μM) caused a decrease in V           (m...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5557833</comments>
            <pubDate>Fri, 30 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5557833</guid>        </item>
        <item>
            <title>Isolation of Thermo-stable and Solvent-Tolerant Bacillus sp. Lipase for the Production of Biodiesel.</title>
            <link>http://www.medworm.com/index.php?rid=5557839&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22205320%26dopt%3DAbstract</link>
            <description>This study presents the production of biodiesel from algae oil by transesterification using thermophilic microorganism. The microorganism used in this study was isolated from the soil sample obtained near the furnace. The organism was identified as Bacillus sp., and the lipase obtained was purified by ammonium sulfate precipitation and ion exchange chromatography leading to 8.6-fold purification and 13% recovery. Molecular weight of the enzyme was determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and it was found to be 45 kDa. The effect of pH, temperature, and solvent addition on lipase activity was investigated. The enzyme showed maximum activity at 55 °C and at pH 7 and was also found to be highly active in the presence of organic solvents such as hexane and t...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5557839</comments>
            <pubDate>Thu, 29 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5557839</guid>        </item>
        <item>
            <title>Amentoflavone Inhibits UVB-Induced Matrix Metalloproteinase-1 Expression Through the Modulation of AP-1 Components in Normal Human Fibroblasts.</title>
            <link>http://www.medworm.com/index.php?rid=5557838&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22205321%26dopt%3DAbstract</link>
            <description>Authors: Lee CW, Na Y, Park NH, Kim HS, Ahn SM, Kim JW, Kim HK, Jang YP
    Abstract
    Amentoflavone is a well-known biflavonoid that has diverse biological effects. Previously, we reported that amentoflavone suppressed UVB-induced matrix metalloproteinase-1 (MMP-1) expression in normal human fibroblasts (NHF). We investigated the effects of amentoflavone on UVB-induced MMP-1 expression in order to elucidate its mode of action. NHF were treated with amentoflavone for indicated times and doses with UVB irradiation. The expressions of MMP-1 gene and protein were determined by RT-PCR and ELISA, respectively. MAP kinase phosphorylation and the expression of c-Fos protein were determined by Western blot. The treatment of amentoflavone completely blocked the upregulation of MMP-1 which is indu...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5557838</comments>
            <pubDate>Thu, 29 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5557838</guid>        </item>
        <item>
            <title>Biogas Production Potential and Kinetics of Microwave and Conventional Thermal Pretreatment of Grass.</title>
            <link>http://www.medworm.com/index.php?rid=5557837&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22205322%26dopt%3DAbstract</link>
            <description>In this study, conventional thermal and microwave methods were performed on raw material, namely, Pennisetum hybrid, to analyze the effect of pretreatment on anaerobic digestion by the calculation of performance parameters using Logistic function, modified Gompertz equation, and transference function. Results indicated that thermal pretreatment improved the biogas production of Pennisetum hybrid, whereas microwave method had an adverse effect on the performance. All the models fit the experimental data with R           (2) &amp;gt; 0.980, and the Reaction Curve presented the best agreement in the fitting process. Conventional thermal pretreatment showed an increasing effect on maximum production rate and total methane produced, with an improvement of around 7% and 8%, respectively. With re...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5557837</comments>
            <pubDate>Thu, 29 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5557837</guid>        </item>
        <item>
            <title>Rapid Establishment of p-Nitrophenol Biodegradation in Acetate-Fed Aerobic Granular Sludge.</title>
            <link>http://www.medworm.com/index.php?rid=5557836&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22205323%26dopt%3DAbstract</link>
            <description>Authors: Yarlagadda VN, Kadali R, Sharma N, Sekar R, Vayalam Purath V
    Abstract
    The aim of the study was to investigate the acclimation of precultivated acetate-fed aerobic granular sludge to a toxic xenobiotic biodegradation. Establishment of p-nitrophenol (PNP) biodegradation in acetate-fed aerobic granular sludge and concomitant changes in the microstructure and bacterial community were determined. Rapid establishment of PNP utilization was observed in the granular sludge when fed with PNP as the sole carbon source. The specific PNP removal was 36-mg h(-1) g(-1) granular biomass at an initial PNP concentration of 50 mg L(-1). The presence of PNP resulted in significant membrane damage in a subpopulation of the bacterial consortium, as shown by BacLight viability staining. Thi...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5557836</comments>
            <pubDate>Thu, 29 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5557836</guid>        </item>
        <item>
            <title>Effects of Different Substrate Composition on Biosynthesis of Polyhydroxybutyrate-co-hydroxyvalerate by Recombinant Escherichia coli.</title>
            <link>http://www.medworm.com/index.php?rid=5557845&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22203393%26dopt%3DAbstract</link>
            <description>Authors: Chien CC, Li HH, Soo PC, Chen SY, Wei YH, Chen WM
    Abstract
    Cupriavidus necator is well known for its ability to accumulate polyhydroxybutyrate (PHB). When supplemented with propionic acid (or sodium propionate) in the growth medium, the bacterium is also able to synthesize polyhydroxybutyrate-co-hydroxyvalerate (PHBV). In order to increase the fraction of 3-hydroxyvalerate (3HV) in PHBV, we cloned the propionate permease gene prpP from C. necator and the propionyl-CoA synthase gene prpE from Cupriavidus taiwanensis and transformed into an Escherichia coli containing phaCAB operon of C. necator. The effects on PHBV accumulation in cells co-expressed with phaCAB and prpE or prpP in the media contained mixed carbon sources (glucose and sodium propionate) were evaluated. The H...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5557845</comments>
            <pubDate>Wed, 28 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5557845</guid>        </item>
        <item>
            <title>Production of D: -tagatose, a Functional Sweetener, Utilizing Alginate Immobilized Lactobacillus fermentum CGMCC2921 Cells.</title>
            <link>http://www.medworm.com/index.php?rid=5557844&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22203394%26dopt%3DAbstract</link>
            <description>This study was aimed at developing a high-yielding D: -tagatose production process using alginate immobilized Lactobacillus fermentum CGMCC2921 cells. For the isomerization from D: -galactose into D: -tagatose, the immobilized cells showed optimum temperature and pH at 65 °C and 6.5, respectively. The alginate beads exhibited a good stability after glutaraldehyde treatment and retained 90% of the enzyme activity after eight cycles (192 h at 65 °C) of batch conversion. The addition of borate with a molar ratio of 1.0 to D: -galactose led to a significant enhancement in the D: -tagatose yield. Using commercial β-galactosidase and immobilized L. fermentum cells, D: -tagatose was successfully obtained from lactose after a two-step biotransformation. The relatively high conversion rate an...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5557844</comments>
            <pubDate>Wed, 28 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5557844</guid>        </item>
        <item>
            <title>Extraction of Soluble Fiber from Distillers' Grains.</title>
            <link>http://www.medworm.com/index.php?rid=5557843&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22203395%26dopt%3DAbstract</link>
            <description>Authors: Flodman HR, Boyer EJ, Muthukumarappan A, Noureddini H
    Abstract
    The feasibility of using coproducts from dry grind corn ethanol production as a substrate for the production of soluble fiber was examined. Acid- and base-catalyzed hydrolysis experiments were performed using sulfuric acid and sodium hydroxide to partially hydrolyze hemicellulose content of whole stillage, a precursor to distillers' grains, to soluble fiber. The influences of temperature, reaction time, and hydrolyzing agent concentration on the formation of soluble fiber were studied. Soluble fiber was recovered by precipitation in a 95% ethanol solution. Results indicate that appreciable quantities of soluble fiber may be extracted using either acid- or base-catalyzed reactions. The highest yield of soluble f...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5557843</comments>
            <pubDate>Wed, 28 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5557843</guid>        </item>
        <item>
            <title>Laccase Production and Enzymatic Modification of Lignin by a Novel Peniophora sp.</title>
            <link>http://www.medworm.com/index.php?rid=5557842&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22203396%26dopt%3DAbstract</link>
            <description>Authors: Shankar S, Shikha 
    Abstract
    A novel laccase producing Basidiomycete Peniophora sp. (NFCCI-2131) was isolated from pulp and paper mill effluent. The optimal temperature and initial pH for laccase production by the isolate in submerged culture were found to be 30 and 4.6° C, respectively. Maltose (20 g l(-1)) and tryptone (1.0 g l(-1)) were the most suitable carbon and nitrogen sources for laccase production. Cu(2+) (1.0 mM) and veratryl alcohol induced maximum laccase production giving 6.6 and 6.07 U/ml laccase activity, respectively. Under optimised culture conditions, 7.6 U/ml activity was obtained, which was 2.4 times higher than that was achieved in basal medium. An evaluation of the delignification efficiency of the crude enzyme in the presence of redox med...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5557842</comments>
            <pubDate>Wed, 28 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5557842</guid>        </item>
        <item>
            <title>Hydrolysis of Native and Heat-Treated Starches at Sub-Gelatinization Temperature Using Granular Starch Hydrolyzing Enzyme.</title>
            <link>http://www.medworm.com/index.php?rid=5557841&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22203397%26dopt%3DAbstract</link>
            <description>Authors: Uthumporn U, Shariffa YN, Karim AA
    Abstract
    The effect of heat treatment below the gelatinization temperature on the susceptibility of corn, mung bean, sago, and potato starches towards granular starch hydrolysis (35°C) was investigated. Starches were hydrolyzed in granular state and after heat treatment (50°C for 30 min) by using granular starch hydrolyzing enzyme for 24 h. Hydrolyzed heat-treated starches showed a significant increase in the percentage of dextrose equivalent compared to native starches, respectively, with corn 53% to 56%, mung bean 36% to 47%, sago 15% to 26%, and potato 12% to 15%. Scanning electron microscopy micrographs showed the presence of more porous granules and surface erosion in heat-treated starch compared to native starch. X-ray analysis ...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5557841</comments>
            <pubDate>Wed, 28 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5557841</guid>        </item>
        <item>
            <title>Production of Oils from Acetic Acid by the Oleaginous Yeast Cryptococcus curvatus.</title>
            <link>http://www.medworm.com/index.php?rid=5557840&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22203398%26dopt%3DAbstract</link>
            <description>Authors: Christophe G, Deo JL, Kumar V, Nouaille R, Fontanille P, Larroche C
    Abstract
    The feasibility of the conversion of acetic acid, a metabolite commonly obtained during anaerobic fermentation processes, into oils using the yeast Cryptococcus curvatus was reported. This microorganism exhibited very slow growth rates on acetate as carbon source, which led to design a two-stage cultivation process. The first consisted of cell growth on glucose as carbon source until its complete exhaustion. The second step involved the use of acetate as carbon source under nitrogen limitation in order to induce lipid accumulation. A typical experiment performed in a bioreactor involved a preliminary yeast growth with a glucose initial concentration of 15 g/L glucose. Further additions of acetate...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5557840</comments>
            <pubDate>Wed, 28 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5557840</guid>        </item>
        <item>
            <title>Integrated Perspective for Effective Bioremediation.</title>
            <link>http://www.medworm.com/index.php?rid=5544472&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22198863%26dopt%3DAbstract</link>
            <description>Authors: Paliwal V, Puranik S, Purohit HJ
    Abstract
    Identification of factors which can influence the natural attenuation process with available microbial genetic capacities can support the bioremediation which has been viewed as the safest procedure to combat with anthropogenic compounds in ecosystems. With the advent of molecular techniques, assimilatory capacity of an ecosystem can be defined with changing community dynamics, and if required, the essential genetic potential can be met through bioaugmentation. At the same time, intensification of microbial processes with nutrient balancing, expressing and enhancing the degradative capacities, could reduce the time frame of restoration of the ecosystem. The new concept of ecosystems biology has added greatly to conceptualize the ne...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5544472</comments>
            <pubDate>Sat, 24 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5544472</guid>        </item>
        <item>
            <title>A Thermophilic Cellulase Complex from Phialophora sp. G5 Showing High Capacity in Cellulose Hydrolysis.</title>
            <link>http://www.medworm.com/index.php?rid=5544471&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22198864%26dopt%3DAbstract</link>
            <description>Authors: Zhao J, Shi P, Bai Y, Huang H, Luo H, Zhang H, Xu D, Wang Y, Yao B
    Abstract
    A cellulase-producing mesophilic fungal strain, named G5, was isolated from the acidic wastewater and mud of a tin mine and identified as Phialophora sp. based on the internal transcribed spacer sequence. The volumetric activities and specific activities of cellulase induced by different carbon sources (Avicel, corn cob, wheat bran and corn stover) were compared. The cellulase complex of Phialophora sp. G5 exhibited the optimal activities at 60-65 °C and pH 4.0-5.0, and had good long-term thermostability at 50 °C. Compared with the commercial cellulase (Accellerase 1500, Genencor), the enzyme under study showed 60% and 80% of the capacity to hydrolyze pure cellulose and natural cellulose, resp...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5544471</comments>
            <pubDate>Sat, 24 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5544471</guid>        </item>
        <item>
            <title>Solid-State Fermentation of Mortierella isabellina for Lipid Production from Soybean Hull.</title>
            <link>http://www.medworm.com/index.php?rid=5544470&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22198865%26dopt%3DAbstract</link>
            <description>Authors: Zhang J, Hu B
    Abstract
    Soybean hull, generated from soybean processing, is a lignocellulosic material with limited industrial applications and little market value. This research is exploring a new application of soybean hull to be converted to fungal lipids for biodiesel production through solid-state fermentation. Mortierella isabellina was selected as the oil producer because of its high lipid content at low C/N ratio. Several cultivation factors were investigated, including moisture content, inoculums size, fungal spore age, and nutrient supplements, in an attempt to enhance the lipid production of the solid-state fermentation process. The results showed that lipid production with the increase of the moisture content and the spore age, while decreased as the size of ino...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5544470</comments>
            <pubDate>Sat, 24 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5544470</guid>        </item>
        <item>
            <title>Cloning, Differential Expression, and Association Analysis with Fat Traits of Porcine IDH3γ Gene.</title>
            <link>http://www.medworm.com/index.php?rid=5544469&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22198866%26dopt%3DAbstract</link>
            <description>Authors: Ren Z, Xiong Y, Deng C, Jiang S
    Abstract
    Mitochondrial NAD(+)-dependent isocitrate dehydrogenase (IDH3) catalyzes the allosterically regulated rate-limiting step of the tricarboxylic acid cycle activated. In pigs, very little is known about this gene. Here, we cloned 1,346 bp full-length cDNA and 8,778 bp genomic sequence of porcine γ subunit of IDH3 (IDH3γ). IDH3γ contains 12 exons separated by 11 introns. Real-time PCR revealed that IDH3γ mRNA were upregulated in backfat of Large White compared with Meishan and F1 hybrids, and most abundant in small intestine via tissue distribution profile. A microsatellite (&quot;GT&quot; repeats) in second intron was found. The selected pigs were genotyped at this microsatellite. The IDH3γ genotypes showed a significant effect on backfat...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5544469</comments>
            <pubDate>Sat, 24 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5544469</guid>        </item>
        <item>
            <title>Synthesis, Characterization, and Oil Recovery Application of Biosurfactant Produced by Indigenous Pseudomonas aeruginosa WJ-1 Using Waste Vegetable Oils.</title>
            <link>http://www.medworm.com/index.php?rid=5544468&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22198867%26dopt%3DAbstract</link>
            <description>Authors: Xia WJ, Luo ZB, Dong HP, Yu L, Cui QF, Bi YQ
    Abstract
    A bacterial strain was isolated and cultured from the oil excavation areas in tropical zone in northern China. The biochemical characteristics and partial sequenced 16S rRNA gene of isolate, WJ-1, was identical to those of cultured representatives of the species Pseudomonas aeruginosa. This bacterium was able to produce a type of biosurfactant. Compositional analysis revealed that the extracted biosurfactant was composed of high percentage lipid (∼74%, w/w) and carbohydrate (∼20%, w/w) in addition to a minor fraction of protein (∼6%, w/w). The best production of 50.2 g/l was obtained when the cells were grown on minimal salt medium containing 6.0% (w/v) glucose and 0.75% (w/v) sodium nitrate supplemented with 0.1...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5544468</comments>
            <pubDate>Sat, 24 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5544468</guid>        </item>
        <item>
            <title>Apoptosis Mechanism of Human Cholangiocarcinoma Cells Induced by Bile Extract from Crocodile.</title>
            <link>http://www.medworm.com/index.php?rid=5544476&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22194052%26dopt%3DAbstract</link>
            <description>Authors: Kang JH, Zhang WQ, Song W, Shen DY, Li SS, Tian L, Shi Y, Liang G, Xiong YX, Chen QX
    Abstract
    Animal bile is popularly used as a traditional medicine in China, and bile acids are their major bioactive constituents. In the present study, effects of bile extract from crocodile gallbladder on QBC939 cell growth, cell cycle, and apoptosis were investigated by MTT assay, inverted microscopy, fluorescence microscopy, transmission electron microscopy, scanning electron microscopy, PI single- and FITC/PI double-staining flow cytometry, and western blotting. Our data have revealed that bile extract inhibited cells growth significantly, and the cell cycle was arrested in G1 phase. Bile extract induced QBC939 cell apoptosis, which was associated with collapse of the mitochondrial mem...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5544476</comments>
            <pubDate>Fri, 23 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5544476</guid>        </item>
        <item>
            <title>Microbial Production of Propionic Acid with Propionibacterium freudenreichii Using an Anion Exchanger-Based In Situ Product Recovery (ISPR) Process with Direct and Indirect Contact of Cells.</title>
            <link>http://www.medworm.com/index.php?rid=5544475&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22194053%26dopt%3DAbstract</link>
            <description>Authors: Wang P, Wang Y, Su Z
    Abstract
    The recovery of an inhibiting product from a bioreactor soon after its formation is an important issue in industrial bioprocess development. In the present study, the potential of the anion exchanger-based in situ product recovery (ISPR) technique for the biocatalytic production of propionic acid was discussed. The focus of the current work was the selection of a suitable configuration of metabolically active cells for application in propionic acid production. Accumulation of propionic acid in fermentation broth caused feedback inhibition of the growth and biotransformation activity of Propionibacterium freudenreichii CICC 10019. Relevant product inhibition kinetics was discussed, and the results showed that keeping the aqueous propionic acid ...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5544475</comments>
            <pubDate>Fri, 23 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5544475</guid>        </item>
        <item>
            <title>Role of Tyr-435 of Vibrio harveyi Chitinase A in Chitin Utilization.</title>
            <link>http://www.medworm.com/index.php?rid=5544474&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22194054%26dopt%3DAbstract</link>
            <description>This study reports the effects of Tyr-435 using site-directed mutagenesis technique. Mutation of Tyr-435 to Ala (mutant Y435A) enhanced both binding and catalytic efficiency of VhChiA, whereas substitution of Tyr-435 to Trp (mutant Y435W) lessened the ability of the enzyme to bind and hydrolyze chitin substrates. The increased activity of Y435A can be explained by partial removal of a steric clash around subsite (+2), thereby allowing a chitin chain to move beyond or to access the enzyme's active site from the aglycone side more straightforwardly.
    PMID: 22194054 [PubMed - as supplied by publisher] (Source: Applied Biochemistry and Biotechnology)</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5544474</comments>
            <pubDate>Fri, 23 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5544474</guid>        </item>
        <item>
            <title>Identification of Highly Active Flocculant Proteins in Bovine Blood.</title>
            <link>http://www.medworm.com/index.php?rid=5544473&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22194055%26dopt%3DAbstract</link>
            <description>Authors: Piazza GJ, Nuñez A, Garcia RA
    Abstract
    Synthetic polymeric flocculants are used extensively for wastewater remediation, soil stabilization, and reduction in water leakage from unlined canals. Sources of highly active, inexpensive, renewable flocculants are needed to replace synthetic flocculants. High kaolin flocculant activity was documented for bovine blood (BB) and blood plasma with several anticoagulant treatments. BB serum also had high flocculant activity. To address the hypothesis that some blood proteins have strong flocculating activity, the BB proteins were separated by SEC. Then, the major proteins of the flocculant-active fractions were separated by SDS-PAGE. Identity of the major protein components was determined by tryptic digestion and peptide analysis by M...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5544473</comments>
            <pubDate>Fri, 23 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5544473</guid>        </item>
        <item>
            <title>Soybean Hulls Pretreated Using Thermo-Mechanical Extrusion-Hydrolysis Efficiency, Fermentation Inhibitors, and Ethanol Yield.</title>
            <link>http://www.medworm.com/index.php?rid=5544478&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22187220%26dopt%3DAbstract</link>
            <description>Authors: Yoo J, Alavi S, Vadlani P, Behnke KC
    Abstract
    Soybean hulls were subjected to thermo-mechanical extrusion pretreatment at various in-barrel moisture contents and screw speeds. Extrusion degraded the lignocellulosic structure and enhanced enzymatic hydrolysis of soybean hulls, with up to 155% increase in glucose yield as compared to untreated substrate. Greater glucose yields were observed at higher in-barrel moistures (45% and 50%) and lower screw speed (280 and 350 rpm). Maximum 74% cellulose to glucose conversion resulted from using a two-enzyme cocktail consisting of cellulase and β-glucosidase. Conversion increased to 87% when a three-enzyme cocktail having a cell wall degrading enzyme complex was used for hydrolysis. Fermentation inhibitors, such as furfural, 5-(hyd...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5544478</comments>
            <pubDate>Wed, 21 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5544478</guid>        </item>
        <item>
            <title>Biochemical Characterization of a Type III Polyketide Biosynthetic Gene Cluster from Streptomyces toxytricini.</title>
            <link>http://www.medworm.com/index.php?rid=5544477&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22187221%26dopt%3DAbstract</link>
            <description>Authors: Zeng J, Decker R, Zhan J
    Abstract
    A type III polyketide biosynthetic gene cluster has been discovered in the industrially important strain Streptomyces toxytricini NRRL 15443, including four genes stp450-1, stts, stp450-2, and stmo. The stts gene encodes a putative type III polyketide synthase that is homologous to RppA, a 1,3,6,8-tetrahydroxynaphthalene (THN) synthase from Streptomyces griseus. The deduced protein product of stmo resembles the cupin-containing monooxygenase MomA from Streptomyces antibioticus that oxidizes THN into flaviolin. Two cytochrome P450s (CYPs), StP450-1 and StP450-2, are present in the gene cluster. StTS was overexpressed in Escherichia coli BL21(DE3) and identified as a THN synthase. The synthesized THN can be easily oxidized into flaviolin by ...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5544477</comments>
            <pubDate>Wed, 21 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5544477</guid>        </item>
        <item>
            <title>Biohydrogen Production from Cheese Whey Wastewater in a Two-Step Anaerobic Process.</title>
            <link>http://www.medworm.com/index.php?rid=5525368&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22183564%26dopt%3DAbstract</link>
            <description>Authors: Rai PK, Singh SP, Asthana RK
    Abstract
    Cheese whey-based biohydrogen production was seen in batch experiments via dark fermentation by free and immobilized Enterobacter aerogenes MTCC 2822 followed by photofermentation of VFAs (mainly acetic and butyric acid) in the spent medium by Rhodopseudomonas BHU 01 strain. E. aerogenes free cells grown on cheese whey diluted to 10 g lactose/L, had maximum lactose consumption (∼79%), high production of acetic acid (1,900 mg/L), butyric acid (537.2 mg/L) and H(2) yield (2.04 mol/mol lactose; rate,1.09 mmol/L/h). The immobilized cells improved lactose consumption (84%), production of acetic acid (2,100 mg/L), butyric acid (718 mg/L) and also H(2) yield (3.50 mol/mol lactose; rate, 1.91 mmol/L/h). E. aerogenes spent medium (10...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5525368</comments>
            <pubDate>Tue, 20 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5525368</guid>        </item>
        <item>
            <title>Expression of Rice Thaumatin-Like Protein Gene in Transgenic Banana Plants Enhances Resistance to Fusarium Wilt.</title>
            <link>http://www.medworm.com/index.php?rid=5525367&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22183565%26dopt%3DAbstract</link>
            <description>Authors: Mahdavi F, Sariah M, Maziah M
    Abstract
    The possibility of controlling Fusarium wilt-caused by Fusarium oxysporum sp. cubensec (race 4)-was investigated by genetic engineering of banana plants for constitutive expression of rice thaumatin-like protein (tlp) gene. Transgene was introduced to cauliflower-like bodies' cluster, induced from meristemic parts of male inflorescences, using particle bombardment with plasmid carrying a rice tlp gene driving by the CaMV 35S promoter. Hygromycin B was used as the selection reagent. The presence and integration of rice tlp gene in genomic DNA confirmed by PCR and Southern blot analyses. RT-PCR revealed the expression of transgene in leaf and root tissues in transformants. Bioassay of transgenic banana plants challenged with Fusarium wi...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5525367</comments>
            <pubDate>Tue, 20 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5525367</guid>        </item>
        <item>
            <title>Start-up of Completely Autotrophic Nitrogen Removal Over Nitrite Enhanced by Hydrophilic-Modified Carbon Fiber.</title>
            <link>http://www.medworm.com/index.php?rid=5525369&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22173783%26dopt%3DAbstract</link>
            <description>This study demonstrates the hydrophilic-modified ACFs have better biological affinity than unmodified ACFs. Maximal total nitrogen removal rate of 0.088 k g N m(-3) day(-1) was achieved for the CANON process on day 80, indicating the CANON process was successfully started up. Apart from supports, the strategies of DO supplying and controlling FA concentration were also keys in starting up the CANON process within a shorter period.
    PMID: 22173783 [PubMed - as supplied by publisher] (Source: Applied Biochemistry and Biotechnology)</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5525369</comments>
            <pubDate>Fri, 16 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5525369</guid>        </item>
        <item>
            <title>Process Evaluation of Enzymatic Hydrolysis with Filtrate Recycle for the Production of High Concentration Sugars.</title>
            <link>http://www.medworm.com/index.php?rid=5525372&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22167689%26dopt%3DAbstract</link>
            <description>Authors: Xue Y, Rusli J, Chang HM, Phillips R, Jameel H
    Abstract
    Process simulation and lab trials were carried out to demonstrate and confirm the efficiency of the concept that recycling hydrolysate at low total solid enzymatic hydrolysis is one of the options to increase the sugar concentration without mixing problems. Higher sugar concentration can reduce the capital cost for fermentation and distillation because of smaller retention volume. Meanwhile, operation cost will also decrease for less operating volume and less energy required for distillation. With the computer simulation, time and efforts can be saved to achieve the steady state of recycling process, which is the scenario for industrial production. This paper, to the best of our knowledge, is the first paper discussin...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5525372</comments>
            <pubDate>Thu, 15 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5525372</guid>        </item>
        <item>
            <title>Improving Stability and Activity of Cross-linked Enzyme Aggregates Based on Polyethylenimine in Hydrolysis of Fish Oil for Enrichment of Polyunsaturated Fatty Acids.</title>
            <link>http://www.medworm.com/index.php?rid=5525371&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22167690%26dopt%3DAbstract</link>
            <description>Authors: Yan J, Gui X, Wang G, Yan Y
    Abstract
    Cross-linking of enzyme aggregates from recombinant Geotrichum sp. lipase based on polyethylenimine (PEI) was applied to hydrolyze fish oil for enrichment of polyunsaturated fatty acids successfully. Through acetone precipitation and cross-linking of physical aggregates using glutaraldehyde in the presence of PEI, firmly cross-linked enzyme aggregates (PEI-CLEAs) were prepared. They could maintain more than 65% of relative hydrolysis degree after incubation in the range of 50-55 °C for 4 h and maintain more than 85% of relative hydrolysis degree after being treated by acetone, tert-butyl alcohol and octane for 4 h. PEI-CLEAs increased hydrolysis degree to 42% from 12% by free lipase. After five batch reactions, PEI-CLEAs still maint...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5525371</comments>
            <pubDate>Thu, 15 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5525371</guid>        </item>
        <item>
            <title>A Fungus Capable of Degrading Microcystin-LR in the Algal Culture of Microcystis aeruginosa PCC7806.</title>
            <link>http://www.medworm.com/index.php?rid=5525370&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22167691%26dopt%3DAbstract</link>
            <description>This study examines the ability of Trichaptum abietinum 1302BG, a white rot fungus, to degrade microcystin-LR in the harmful algal culture of Microcystis aeruginosa PCC7806. Results showed that microcystin-LR could not be detected by high-performance liquid chromatography after 12 h in algal culture incubated with the fungus. There were also high activities of catalase and peroxidase in algal culture incubated with the fungus. However, similar to the control, they decreased to normal levels after 72 h. Meanwhile, the micronucleus test in the toxicity studies revealed that the degraded algal culture had low toxicity.
    PMID: 22167691 [PubMed - as supplied by publisher] (Source: Applied Biochemistry and Biotechnology)</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5525370</comments>
            <pubDate>Thu, 15 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5525370</guid>        </item>
        <item>
            <title>Fermentation of Reactive-Membrane-Extracted and Ammonium-Hydroxide-Conditioned Dilute-Acid-Pretreated Corn Stover.</title>
            <link>http://www.medworm.com/index.php?rid=5525380&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22161211%26dopt%3DAbstract</link>
            <description>In this study, we treated the liquor fraction of dilute-acid-pretreated corn stover using AHC and a new reactive membrane extraction technique, both separately and in combination, and then the sugars in the treated liquors were fermented to ethanol with the glucose-xylose-fermenting bacterium, Zymomonas mobilis 8b. We performed reactive extraction with mixtures of octanol/Alamine 336 or oleyl alcohol/Alamine 336. The best ethanol yields and rates were achieved for oleyl alcohol-extracted hydrolysates followed by AHC hydrolysates, while octanol-extracted hydrolysates were unfermentable because highly toxic octanol was found in the hydrolysate. Adding olive oil significantly improved yields for octanol-extracted hydrolysate. Additional work is underway to determine if this technology is a co...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5525380</comments>
            <pubDate>Tue, 13 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5525380</guid>        </item>
        <item>
            <title>Recycling of Cellulosic Fibers by Enzymatic Process.</title>
            <link>http://www.medworm.com/index.php?rid=5525379&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22161212%26dopt%3DAbstract</link>
            <description>This study investigates to detect the optimum enzyme concentration and time of treatments for suitable changes of length and weight loss. The main purposes of this article are shortening of cellulosic fibers and evaluating of enzymatic treatment in different kind of cellulosic fibers. According to the data of experiments, with the increase of enzyme concentration and the treatment time, the length and weight loss percentage of the cellulosic fibers has been decreased. The length and weight loss percentage of treated viscose is more than that of lyocell and cotton fibers. Optimized condition, reaction time, and enzyme concentration have been determined by mean length of treated cellulosic samples. Suitable longitudinal distribution of fiber for papermaking industries is in the range of 0 to...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5525379</comments>
            <pubDate>Tue, 13 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5525379</guid>        </item>
        <item>
            <title>Improvement of Ethanol Yield from Glycerol via Conversion of Pyruvate to Ethanol in Metabolically Engineered Saccharomyces cerevisiae.</title>
            <link>http://www.medworm.com/index.php?rid=5525378&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22161213%26dopt%3DAbstract</link>
            <description>Authors: Yu KO, Jung J, Ramzi AB, Kim SW, Park C, Han SO
    Abstract
    The conversion of low-priced glycerol to higher value products has been proposed as a way to improve the economic viability of the biofuels industry. In a previous study, the conversion of glycerol to ethanol in a metabolically engineered strain of Saccharomyces cerevisiae was accomplished by minimizing the synthesis of glycerol, the main by-product in ethanol fermentation processing. To further improve ethanol production, overexpression of the native genes involved in conversion of pyruvate to ethanol in S. cerevisiae was successfully accomplished. The overexpression of an alcohol dehydrogenase (adh1) and a pyruvate decarboxylase (pdc1) caused an increase in growth rate and glycerol consumption under fermentative co...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5525378</comments>
            <pubDate>Tue, 13 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5525378</guid>        </item>
        <item>
            <title>In Vitro Reduction of Hexavalent Chromium by Cytoplasmic Fractions of Pannonibacter phragmitetus LSSE-09 under Aerobic and Anaerobic Conditions.</title>
            <link>http://www.medworm.com/index.php?rid=5525377&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22161214%26dopt%3DAbstract</link>
            <description>Authors: Xu L, Luo M, Jiang C, Wei X, Kong P, Liang X, Zhao J, Yang L, Liu H
    Abstract
    Hexavalent chromate reductase was characterized and was found to be localized in the cytoplasmic fraction of a chromium-resistant bacterium Pannonibacter phragmitetus LSSE-09. The Cr(VI) reductase activity of cell-free extract (S(12)) was significantly improved by external electron donors, such as NADH, glucose, acetate, formate, citrate, pyruvate, and lactate. The reductase activity was optimal at pH 7.0 with NADH as the electron donor. The aerobic and anaerobic Cr(VI)-reduction enhanced by 0.1 mM NADH were respectively 3.5 and 3.4 times as high as that without adding NADH. The Cr(VI) reductase activity was inhibited by Mn(2+), Cd(2+), Fe(3+), and Hg(2+), whereas Cu(2+) enhanced the chromate re...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5525377</comments>
            <pubDate>Tue, 13 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5525377</guid>        </item>
        <item>
            <title>Purification and Biochemical Characterization of a Highly Thermostable Xylanase from Actinomadura sp. Strain Cpt20 Isolated from Poultry Compost.</title>
            <link>http://www.medworm.com/index.php?rid=5525382&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22161140%26dopt%3DAbstract</link>
            <description>Authors: Taibi Z, Saoudi B, Boudelaa M, Trigui H, Belghith H, Gargouri A, Ladjama A
    Abstract
    An extracellular thermostable xylanase from a newly isolated thermophilic Actinomadura sp. strain Cpt20 was purified and characterized. Based on matrix-assisted laser desorption-ionization time-of-flight mass spectrometry analysis, the purified enzyme is a monomer with a molecular mass of 20,110.13 Da. The 19 residue N-terminal sequence of the enzyme showed 84% homology with those of actinomycete endoxylanases. The optimum pH and temperature values for xylanase activity were pH 10 and 80 °C, respectively. This xylanase was stable within a pH range of 5-10 and up to a temperature of 90 °C. It showed high thermostability at 60 °C for 5 days and half-life times at 90 °C and 100 °C...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5525382</comments>
            <pubDate>Sat, 10 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5525382</guid>        </item>
        <item>
            <title>Identification and Molecular Characterization of a Novel DyP-Type Peroxidase from Pseudomonas aeruginosa PKE117.</title>
            <link>http://www.medworm.com/index.php?rid=5525381&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22161141%26dopt%3DAbstract</link>
            <description>Authors: Li J, Liu C, Li B, Yuan H, Yang J, Zheng B
    Abstract
    A new DyP-type peroxidase from Pseudomonas aeruginosa PKE117 was identified and characterized. The dypPa was first identified via sequence analysis and then cloned in Escherichia coli. Subsequently, the recombinant protein DyPPa was expressed and purified. Its DNA sequence analysis revealed an open reading frame of 897 bp, encoding a protein monomer of 299 amino acid residues with isoelectric point 4.62. According to SDS-PAGE analysis and FPLC result, DyPPa mainly existed as homodimer (64 kDa). DyPPa displayed typical heme absorbance of Soret band, with an Rz value of 1.18. Inductively coupled plasma-atomic absorption spectrum data also indicated DyPPa contained iron. Multiple amino acid sequence alignment of DyPPa with...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5525381</comments>
            <pubDate>Sat, 10 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5525381</guid>        </item>
        <item>
            <title>Heterologous Expression of a Nelumbo nucifera Phytochelatin Synthase Gene Enhances Cadmium Tolerance in Arabidopsis thaliana.</title>
            <link>http://www.medworm.com/index.php?rid=5525374&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22161260%26dopt%3DAbstract</link>
            <description>Authors: Liu Z, Gu C, Chen F, Yang D, Wu K, Chen S, Jiang J, Zhang Z
    Abstract
    Phytochelatin synthase (PCS) is a key enzyme involved in the synthesis of phytochelatins, which are thought to play important roles in heavy metal detoxification. The sacred lotus (Nelumbo nucifera), one of the most popular ornamental species, has been shown to be a potential phytoremediator of heavy metal polluted water. However, the phytochelatin synthase gene in N. nucifera has not been identified yet. Here, we report the isolation and function characterization of a N. nucifera homologue of phytochelatin synthase. The sequence obtained shares a high degree of similarity with PCSs from other plant species and was named as Nelumbo nucifera phytochelatin synthase1 (NnPCS1). By using quantitative RT-PCR, w...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5525374</comments>
            <pubDate>Fri, 09 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5525374</guid>        </item>
        <item>
            <title>Metabolic Engineering of Nocardia sp. CS682 for Enhanced Production of Nargenicin A(1).</title>
            <link>http://www.medworm.com/index.php?rid=5525373&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22161261%26dopt%3DAbstract</link>
            <description>In this study, we applied a metabolic engineering approach based on recombinant DNA technology in order to boost the production of nargenicin A(1) from Nocardia sp. CS682. Initially, we optimized the transformation of this new strain by electroporation method. Heterologous expression of S-adenosylmethionine synthetase (MetK1-sp) in Nocardia sp. CS682 enhanced the production of nargenicin A(1) by about 2.8 times due to transcriptional activation of biosynthetic genes as revealed by reverse transcription polymerase chain reaction analysis. Similarly, expression of acetyl-CoA carboxylase genes improved nargenicin A(1) production by about 3.8 times in Nocardia sp. ACC18 compared to that in Nocardia sp. CS682 and Nocardia sp. NV18 by increasing precursor pool. Thus, enhanced production of narge...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5525373</comments>
            <pubDate>Fri, 09 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5525373</guid>        </item>
        <item>
            <title>Lactobacillus plantarum AS1 Isolated from South Indian Fermented Food Kallappam Suppress 1,2-Dimethyl Hydrazine (DMH)-Induced Colorectal Cancer in Male Wistar Rats.</title>
            <link>http://www.medworm.com/index.php?rid=5525376&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22161238%26dopt%3DAbstract</link>
            <description>In this study, an increased level of lipid peroxide (LPO) products and increased activities of antioxidant enzymes (superoxide dismutase, catalase and glutathione-S transferase) and marker enzymes (alkaline phosphatase and acid phosphatase) in colon and plasma of cancer-bearing animals have been observed. AS1 was supplemented either before initiation or during initiation and selection/promotion phases of colon carcinogenesis and was found to be effective in altering lipid peroxidation and antioxidant enzyme activities and marker enzymes to a statistically significant level measured either in the colon and in the plasma. These alterations inclined towards normal in a time-dependent manner on AS1 supplementation. The mean tumor volume diameter and total number of tumors were found to be stat...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5525376</comments>
            <pubDate>Thu, 08 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5525376</guid>        </item>
        <item>
            <title>Identification of WA-Type Three-Line Hybrid Rice with Real-Time Polymerase Chain Reaction (PCR) Method.</title>
            <link>http://www.medworm.com/index.php?rid=5525375&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22161239%26dopt%3DAbstract</link>
            <description>Authors: Cheng Y, Gao BD, Chen HY, Mao JJ, Cao AX, Zhu JG, Zhu SF
    Abstract
    A real-time fluorescent PCR (RTF-PCR) was developed to detect and quantify wild abortive (WA)-type three-line hybrid rice (Oryza sativa L.). The mitochondrial R(2-630) WA gene was reported to be closely related to male sterility in plants, and developed as a molecular maker to identify the cytoplasmic male sterility system of hybrid rice. First, we got the DNA sequence of R(2-630) WA gene in 17 rice species with traditional PCR. Then, a pair of specific primers (P(3), P(4)) and TaqMan fluorescence probe (P(3-14)) were designed based on the R(2-630) DNA sequence. The following RTF-PCR was performed on the 17 rice species finally. The results indicate that the probes used here are specific for three-line hybri...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5525375</comments>
            <pubDate>Thu, 08 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5525375</guid>        </item>
        <item>
            <title>Erratum to: Preliminary Studies for Cephamycin C Purification Technique.</title>
            <link>http://www.medworm.com/index.php?rid=5525383&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22147297%26dopt%3DAbstract</link>
            <description>Authors: de Baptista Neto A, Bustamante MC, de Oliveira JH, Granato AC, Bellão C, Badino AC, Barboza M, Hokka CO
    PMID: 22147297 [PubMed - as supplied by publisher] (Source: Applied Biochemistry and Biotechnology)</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5525383</comments>
            <pubDate>Wed, 07 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5525383</guid>        </item>
        <item>
            <title>The Effect of Intracellular Amino Acids on GSH Production by High-cell-density Cultivation of Saccharomyces cerevisiae.</title>
            <link>http://www.medworm.com/index.php?rid=5525385&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22143994%26dopt%3DAbstract</link>
            <description>Authors: Wang M, Sun J, Xue F, Shang F, Wang Z, Tan T
    Abstract
    The present paper studies the effects of precursor amino acids, i.e., L: -glutamic acid (Glu), L: -glycine (Gly), and L: -cysteine (Cys), on the glutathione (GSH) production. The three amino acids were added during the fermentations. The GSH production was analyzed by gas chromatography-mass spectrometry (GC-MS). It was observed that the cell content of Cys reduced continually, Gly maintained a fairly constant concentration, while Glu remained at a high concentration compared with Cys and Gly. The synthesis of GSH was found to significantly increase after 28 h of fermentation upon addition of 6 mmol l(-1) of each of the three amino acids. Under these conditions, the GSH yields reached 2,250 ± 50 mg l(-1) at 34...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5525385</comments>
            <pubDate>Tue, 06 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5525385</guid>        </item>
        <item>
            <title>Pretreatment of Corn Stover with Twin-Screw Extrusion Followed by Enzymatic Saccharification.</title>
            <link>http://www.medworm.com/index.php?rid=5525384&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22143995%26dopt%3DAbstract</link>
            <description>The objective of this study was to examine the effect of extrusion as a pretreatment method and the underlying factors ruling the improvement of sugar yields. The optimum glucose, xylose, and combined sugar recoveries were 48.79%, 24.98%, and 40.07%, respectively, at 27.5% moisture content and 80 rpm screw speed. These yields were 2.2, 6.6, and 2.6 times higher than those for untreated corn stover. X-ray diffraction analysis showed that the crystallinity index was not a good indicator of sugar yield. However, scanning electron microscopy showed that the cellulose network was exposed due to the destruction of the lignin sheath. The Langmuir adsorption model was shown to be an effective tool for the estimation of the SSA of corn stover. The SSA of pretreated samples was significantly amplif...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5525384</comments>
            <pubDate>Tue, 06 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5525384</guid>        </item>
        <item>
            <title>Construction of a Genetically Engineered Microorganism that Simultaneously Degrades Organochlorine and Organophosphate Pesticides.</title>
            <link>http://www.medworm.com/index.php?rid=5525389&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22139730%26dopt%3DAbstract</link>
            <description>Authors: Yang J, Liu R, Song W, Yang Y, Cui F, Qiao C
    Abstract
    Field contamination with pesticide mixtures of organophosphates (OPs) and organochlorines (OCs) is becoming global issues to be solved urgently. The strategy of utilizing engineered microorganisms that have an ability to simultaneously degrade OPs and OCs has increasingly received great interest. In this work, an OP degradation gene (mpd) and an OC degradation gene (linA) were simultaneously introduced into Escherichia coli by using two compatible plasmids, resulting in strains with both OP degradation and OC degradation capabilities. To overcome the potential substrate uptake limitation, MPH was displayed on the cell surface of Escherichia coli using the N- and C-terminal domains of ice nucleation protein (INPNC) as an...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5525389</comments>
            <pubDate>Sat, 03 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5525389</guid>        </item>
        <item>
            <title>Further Stabilization of Leu(155) Mutant Thermolysins by Mutation of an Autodegradation Site.</title>
            <link>http://www.medworm.com/index.php?rid=5525388&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22139731%26dopt%3DAbstract</link>
            <description>In this study, further stabilization of the mutant TLNs to suppress this new autodegradation was attempted by the substitution of Ile(156) to Asp and Val (L155A-I156N, L155A-I156V, L155S-I156N, and L155S-I156V). SDS-PAGE analysis showed that the autodegradation at 155-156 of all double-mutant TLNs was suppressed. Thermostability at 80 °C was enhanced in all double-mutant TLNs (half-life at 80 °C: WT, 18.3 min; L155A, 25.0 min; L155S, 24.0 min; L155A-I156N, 60.8 min; L155A-I156V, 62.4 min; L155S-I156N, 93.3 min; and L155S-I156V, 40.0 min), and k           (cat)/K           (m) values were: WT, 220; L155A, 240; L155S, 123; L155A-I156N, 62; L155A-I156V, 760; L155S-I156N, 240; and L155S-I156V, 520 min(-1) mM(-1).
    PMID: 22139731 [PubMed - as supplied by publisher] (Source: Appl...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5525388</comments>
            <pubDate>Sat, 03 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5525388</guid>        </item>
        <item>
            <title>A Hydrogen Peroxide Biosensor Based on Direct Electrochemistry of Hemoglobin in Palladium Nanoparticles/Graphene-Chitosan Nanocomposite Film.</title>
            <link>http://www.medworm.com/index.php?rid=5525387&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22139732%26dopt%3DAbstract</link>
            <description>Authors: Sun A, Sheng Q, Zheng J
    Abstract
    Thermally two-dimensional lattice graphene (GR) and biocompatibility chitosan (CS) act as a suitable support for the deposition of palladium nanoparticles (PdNPs). A novel hydrogen peroxide (H(2)O(2)) biosensor based on immobilization of hemoglobin (Hb) in thin film of CS containing GR and PdNPs was developed. The surface morphologies of a set of representative membranes were characterized by means of scanning electron microscopy and showed that the PdNPs are of a sphere shape and an average diameter of 50 nm. Under the optimal conditions, the immobilized Hb showed fast and excellent electrocatalytic activity to H(2)O(2) with a small Michaelis-Menten constant of 16 μmol L(-1), a linear range from 2.0 × 10(-6) to 1.1 × 10(-3) ...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5525387</comments>
            <pubDate>Sat, 03 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5525387</guid>        </item>
        <item>
            <title>Chemiluminescence Response of Murine Macrophages on Multilayer Microfluidic Chips.</title>
            <link>http://www.medworm.com/index.php?rid=5525386&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22139733%26dopt%3DAbstract</link>
            <description>Authors: Yu L, Li Q, Gai H, Wang Z
    Abstract
    We have demonstrated an integrated platform for microfluidics and chemiluminescence (CL) detection that is capable of parallel cell culture, convenient liquid manipulation, and sensitive chemiluminescent detection. Luminol-dependent CL responses induced by three different stimuli, phytohemagglutinin (PHA), concanavalin A (ConA), and lipopolysaccharides (LPS), which can evoke a CL response in macrophages, were evaluated on this microfluidic chip. We studied the dose-dependent effect of these three stimuli on CL response in murine macrophages. PHA produced the highest CL response compared to LPS and ConA. The CL intensity produced by PHA was 6.85 and four times higher than that by LPS and ConA, respectively, at the low concentration of 100...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5525386</comments>
            <pubDate>Sat, 03 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5525386</guid>        </item>
        <item>
            <title>Analysis of the Production Process of Optically Pure D: -Lactic Acid from Raw Glycerol Using Engineered Escherichia coli Strains.</title>
            <link>http://www.medworm.com/index.php?rid=5470857&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22127808%26dopt%3DAbstract</link>
            <description>Authors: Posada JA, Cardona CA, Gonzalez R
    Abstract
    Glycerol has become an ideal feedstock for producing fuels and chemicals. Here, five technological schemes for optically pure D: -lactic acid production from raw glycerol were designed, simulated, and economically assessed based on five fermentative scenarios using engineered Escherichia coli strains. Fermentative scenarios considered different qualities of glycerol (pure, 98 wt.%, and crude, 85 wt.%) with concentrations ranging from 20 to 60 g/l in the fermentation media, and two fermentation stages were also analyzed. Raw glycerol (60 wt.%) was considered as the feedstock feeding the production process in all cases; then a purification process of raw glycerol up to the required quality was required. Simulation processes were...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5470857</comments>
            <pubDate>Wed, 30 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5470857</guid>        </item>
        <item>
            <title>Chemometric Analysis with Near-Infrared Spectroscopy for Chemically Pretreated Erianthus toward Efficient Bioethanol Production.</title>
            <link>http://www.medworm.com/index.php?rid=5470856&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22127809%26dopt%3DAbstract</link>
            <description>Authors: Horikawa Y, Imai T, Takada R, Watanabe T, Takabe K, Kobayashi Y, Sugiyama J
    Abstract
    In this paper, we report the combination of a near-infrared (NIR) spectroscopic method with multivariate analysis in order to develop a calibration model of the saccharification ratio of chemically pretreated Erianthus. The regression models clearly depend on the NIR spectral regions, and the information of CH and aromatic framework vibrations contributed most effectively to the alkaline dataset. From interpretations of the regression coefficient, lignin and cellulose were negatively and positively correlated with the saccharification ratio, respectively, and this result was supported by the data from wet chemical analysis. A more complex dataset was obtained from varied chemical pretreatm...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5470856</comments>
            <pubDate>Wed, 30 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5470856</guid>        </item>
        <item>
            <title>Identification of Potential Markers Related to Neoadjuvant Chemotherapy Sensitivity of Breast Cancer by SELDI-TOF MS.</title>
            <link>http://www.medworm.com/index.php?rid=5470855&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22127810%26dopt%3DAbstract</link>
            <description>Authors: Zhang K, Yuan K, Wu H, Li Q, Wang Y, Chen S, Zhang L, Gu H, Fu R
    Abstract
    Neoadjuvant chemotherapy (NACT) is known to be beneficial for patients with locally advanced breast cancer. However, there is still no unified standard on the evaluation of NACT. To identify the potential markers related to NACT sensitivity of breast cancer, in the present study, we examined the protein spectrum of breast cancer tissues before and after NACT using surface-enhanced laser desorption/ionization time-of-flight mass spectrometry (SELDI-TOF MS). Totally, 87 protein samples were extracted from tissues of breast cancer, with 30 from patients before NACT, 30 from patients after NACT, and 27 from patients without any treatment. To eliminate confounding factors a couple of tissue samples from t...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5470855</comments>
            <pubDate>Wed, 30 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5470855</guid>        </item>
        <item>
            <title>Pathophysiology of Microwave Radiation: Effect on Rat Brain.</title>
            <link>http://www.medworm.com/index.php?rid=5470854&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22134878%26dopt%3DAbstract</link>
            <description>Authors: Kesari KK, Kumar S, Behari J
    Abstract
    The study aims to investigate the effect of 2.45 GHz microwave radiation on Wistar rats. Rats of 35 days old with 130 ± 10 g body weight were selected for this study. Animals were divided into two groups: sham exposed and experimental (six animals each). Animals were exposed for 2 h a day for 45 days at 2.45 GHz frequency (power density, 0.21 mW/cm(2)). The whole body specific absorption rate was estimated to be 0.14 W/kg. Exposure took place in a ventilated plexiglas cage and kept in an anechoic chamber under a horn antenna. After completion of the exposure period, rats were killed, and pineal gland and whole brain tissues were isolated for the estimation of melatonin, creatine kinase, caspase 3, and calcium ion concentra...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5470854</comments>
            <pubDate>Tue, 29 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5470854</guid>        </item>
        <item>
            <title>Effect of Extracorporeal Shockwave Treatment on the Melanogenic Activity of Cultured Melanocytes.</title>
            <link>http://www.medworm.com/index.php?rid=5452775&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22116672%26dopt%3DAbstract</link>
            <description>Authors: Huang F, Kuo HK, Hsieh CH, Wu PC, Wu YC, Wang CJ
    Abstract
    In addition to the traditional lithotripsy treatment, extracorporeal shockwaves (ESWs) have been shown to be effective in the treatment of certain musculoskeletal disorders and in enhancing skin flap neovascularization. However, relatively little is known about its effect on melanocytes. To investigate its effect on the melanogenic activity of cultured melanocytes, mouse B16F10 melanocytes were treated with defocused ESWs of different energies (15, 21, and 27 kV) and at different doses (300 and 600 impulses). Cell viability was measured 1 and 24 h after treatment. Melanin content was measured and compared against a standard curve generated with fungal melanin. Cellular tyrosinase activity was calculated with the 3...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5452775</comments>
            <pubDate>Sat, 26 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5452775</guid>        </item>
        <item>
            <title>Design and Evaluation of an Optimal Controller for Simultaneous Saccharification and Fermentation Process.</title>
            <link>http://www.medworm.com/index.php?rid=5452777&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22116670%26dopt%3DAbstract</link>
            <description>Authors: Murthy GS, Johnston DB, Rausch KD, Tumbleson ME, Singh V
    Abstract
    Ethanol from corn is produced using dry grind corn process in which simultaneous saccharification and fermentation (SSF) is one of the most critical unit operations. In this work an optimal controller based on a previously validated SSF model was developed by formulating the SSF process as a Bolza problem and using gradient descent methods. Validation experiments were performed to evaluate the performance of optimal controller under different process disturbances that are likely to occur in practice. Use of optimal control algorithm for the SSF process resulted in lower peak glucose concentration, similar ethanol yields (13.38±0.36% v/v and 13.50±0.15% v/v for optimally controlled and baseline experiments,...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5452777</comments>
            <pubDate>Fri, 25 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5452777</guid>        </item>
        <item>
            <title>Effect of Physicochemical Parameters on Enzymatic Biodecaffeination During Tea Fermentation.</title>
            <link>http://www.medworm.com/index.php?rid=5452776&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22116671%26dopt%3DAbstract</link>
            <description>We report for the first time the development of a biodecaffeination process for tea synchronised with tea fermentation process using enzymes isolated from Pseudomonas alcaligenes. Cell-free extract was used for biodecaffeination of tea during fermentation of tea and 80% of the caffeine in the tea dhool was degraded within 90 min of incubation. Several factors that tend to effect the biodecaffeination during this stage, like moisture, aeration, intermittent enzyme addition and mixing, were optimized, and inhibitory interactions of proteins with polyphenols, caffeine-polyphenol interactions, which directly influence the biodecaffeination process were prevented by the use of glycine (5% w/w) in the dhool. Tea decaffeinated through the enzymatic route retained the original flavor and aroma, a...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5452776</comments>
            <pubDate>Fri, 25 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5452776</guid>        </item>
        <item>
            <title>Expression, Purification, and Antibacterial Activity of Bovine Lactoferrampin-Lactoferricin in Pichia pastoris.</title>
            <link>http://www.medworm.com/index.php?rid=5452778&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22109740%26dopt%3DAbstract</link>
            <description>Authors: Tang XS, Tang ZR, Wang SP, Feng ZM, Zhou D, Li TJ, Yin YL
    Abstract
    Bovine lactoferrampin (LFA) and bovine lactoferricin (LFC) are two antimicrobial peptides located in the N(1) domain of bovine lactoferrin. The bactericidal activity of the fused peptide LFA-LFC is stronger than that of either LFA or LFC. The high cost of peptide production from either native digestion or chemical synthesis limits the clinical application of antimicrobial peptides. The expression of recombinant peptides in yeast may be an effective alternative. In the current study, the expression, purification, and antibacterial activity of LFA-LFC using the Pichia pastoris expression system are reported. The linearized expression vector pPICZaA-LFA-LFC was transformed into P. pastoris KM71 by electroporat...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5452778</comments>
            <pubDate>Wed, 23 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5452778</guid>        </item>
        <item>
            <title>Additional Paper Waste in Pulping Sludge for Biohydrogen Production by Heat-Shocked Sludge.</title>
            <link>http://www.medworm.com/index.php?rid=5452783&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22101444%26dopt%3DAbstract</link>
            <description>The objective of this study was to investigate the optimal proportion of pulping sludge to paper waste, the optimal initial pH, and the optimal ratio of carbon and nitrogen (C/N) for H(2) production by anaerobic seed sludge pretreated with heat. The pulping sludge was pretreated with NaOH solution at high temperature and further hydrolyzed with crude cellulase. Pretreatment of the pulping sludge with 3% NaOH solution under autoclave at 121 °C for 2 h, hydrolysis with 5 FPU crude cellulase at 50 °C, and pH 4.8 for 24 h provided the highest reducing sugar production yield (229.68 ± 2.09 mg/g(TVS)). An initial pH of 6 and a C/N ratio of 40 were optimal conditions for H(2) production. Moreover, the supplement of paper waste in the pulping sludge enhanced the cumulative H(2) produc...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5452783</comments>
            <pubDate>Sat, 19 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5452783</guid>        </item>
        <item>
            <title>Improving Phytase Enzyme Activity in a Recombinant phyA Mutant Phytase from Aspergillus niger N25 by Error-Prone PCR.</title>
            <link>http://www.medworm.com/index.php?rid=5452782&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22101445%26dopt%3DAbstract</link>
            <description>Authors: Liao Y, Zeng M, Wu ZF, Chen H, Wang HN, Wu Q, Shan Z, Han XY
    Abstract
    The mutant acid phytase (phyA           (             m           )) gene was modified by random mutagenesis to improve enzymatic activity by using an error-prone PCR (ep-PCR) strategy. The mutated gene was linearized and inserted into plasmid vector pPIC9K and transformed by electroporation into Pichia pastoris GS115. A single transformant, PP-NP(ep)-6A, showing the strongest phytase activity from among the 5,500 transformants, was selected for detailed analyses. Southern blot analysis of the mutant yeast transformant showed that phyA           (             ep           ) gene was integrated into the chromosome genome through single crossover with one copy of phyA. The kinetic parameters indicated that...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5452782</comments>
            <pubDate>Sat, 19 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5452782</guid>        </item>
        <item>
            <title>Tandem Multimer Expression and Preparation of Hypoglycemic Peptide MC6 from Momordica charantia in Escherichia coli.</title>
            <link>http://www.medworm.com/index.php?rid=5452781&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22101446%26dopt%3DAbstract</link>
            <description>Authors: Wang FJ, Song HL, Wang XM, Zhang WJ, Wang BL, Zhao J, Hu ZB
    Abstract
    Tandem repeat multimers of Momordica charantia (MC) peptide MC6 were designed and the recombinant plasmid containing 10 copies of MC6 gene was constructed to improve the expression level of MC6 in Escherichia coli. Under the selected conditions of cultivation and induction, the expression level of recombinant TrxA-MC6(10) protein was above 25% of total bacteria protein. This fusion protein was purified and cleaved with HCl (13%, w/v). Either the un-cleaved or cleaved recombinant proteins was analyzed pharmacological activity by alloxan-induced diabetic mice and only the cleaved products of the recombinant protein showed significant hypoglycemic effects. The study provides a convenient and economical metho...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5452781</comments>
            <pubDate>Sat, 19 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5452781</guid>        </item>
        <item>
            <title>Cloning of Thermostable Cellulase Genes of Clostridium thermocellum and Their Secretive Expression in Bacillus subtilis.</title>
            <link>http://www.medworm.com/index.php?rid=5452780&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22101447%26dopt%3DAbstract</link>
            <description>In this study, five cellobiohydrolase genes and one endoglucanase gene sourced from Clostridium thermocellum DSM 1237, cbhA, celK, celO, cel48Y, cel48S, and celA were cloned into a newly established tool vector pP43JM2 and expressed in two Bacillus subtilis strains, B. subtilis WB600 and B. subtilis WB800, respectively. Most of the cellulases produced in the B. subtilis recombinants were efficiently secreted into the culture medium. These secreted soluble proteins showed distinct cellulase activities using phosphoric acid swollen cellulose (PASC) as the substrate and they also demonstrated strong synergistic effects for PASC, Avicel cellulose, and the dilute acid pretreated corn stover. The current work provided a quick secretive cloning method for screening cellulase genes and may provide...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5452780</comments>
            <pubDate>Sat, 19 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5452780</guid>        </item>
        <item>
            <title>Interspecies Interaction of Signal Peptide PapR Secreted by Bacillus cereus and Its Effect on Production of Antimicrobial Peptide.</title>
            <link>http://www.medworm.com/index.php?rid=5452779&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22101448%26dopt%3DAbstract</link>
            <description>This study was carried out to investigate the interspecies interaction of PapR peptide secreted by Bacillus cereus on production of BSAP-254, an antimicrobial peptide produced by Bacillus subtilis SC-8 isolated from the Korean fermented soybean paste and exhibited narrow antagonistic activity against the B. cereus group, but not against other foodborne pathogens. PapR is a signal peptide that activates PlcR, which is a pleiotropic regulator controlling the expression of various virulence factors in B. cereus. When B. subtilis SC-8 was co-cultured with B. cereus, it completely inhibited the growth of B. cereus within 12 h, and the rate of BSAP-254 production was increased 34.2% at 12 h. Furthermore, 5 μM of synthetic PapR peptide added to the culture of B. subtilis SC-8 increased the ra...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5452779</comments>
            <pubDate>Sat, 19 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5452779</guid>        </item>
        <item>
            <title>Maximum Saccharification of Cellulose Complex by an Enzyme Cocktail Supplemented with Cellulase from Newly Isolated Aspergillus fumigatus ECU0811.</title>
            <link>http://www.medworm.com/index.php?rid=5452786&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22086563%26dopt%3DAbstract</link>
            <description>Authors: Wang D, Sun J, Yu HL, Li CX, Bao J, Xu JH
    Abstract
    Either the natural biodegradation process or the industrial hydrolytic process requires synergistic interactions between various cellulases. However, it is sometimes impeded by low hydrolytic rate of existing cellulases and the lack of accessory enzymes. Herein, the ability of a commercial cellulase (Spezyme CP, from Genencor) to degrade steam explosion-pretreated corn stover was significantly improved. Firstly, a fungal cellulase producer, Aspergillus fumigatus ECU0811, was isolated from hundreds of soil samples. A 96-deep-well microscale-based platform was developed here to reduce the labor-intensive screening work and proved to be consistent with macroscale screening work. After optimization of fermentation, 3% corn cob...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5452786</comments>
            <pubDate>Wed, 16 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5452786</guid>        </item>
        <item>
            <title>Characterization of a Thermostable Family 1 Glycosyl Hydrolase Enzyme from Putranjiva roxburghii Seeds.</title>
            <link>http://www.medworm.com/index.php?rid=5452785&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22086564%26dopt%3DAbstract</link>
            <description>Authors: Patel GK, Kar B, Sharma AK
    Abstract
    A 66-kDa thermostable family 1 Glycosyl Hydrolase (GH1) enzyme with β-glucosidase and β-galactosidase activities was purified to homogeneity from the seeds of Putranjiva roxburghii belonging to Euphorbiaceae family. N-terminal and partial internal amino acid sequences showed significant resemblance to plant GH1 enzymes. Kinetic studies showed that enzyme hydrolyzed p-nitrophenyl β-D: -glucopyranoside (pNP-Glc) with higher efficiency (K           (cat)/K           (m) = 2.27 × 10(4) M(-1) s(-1)) as compared to p-nitrophenyl β-D: -galactopyranoside (pNP-Gal; K           (cat)/K           (m) = 1.15 × 10(4) M(-1) s(-1)). The optimum pH for β-galactosidase activity was 4.8 and 4.4 in citrate phosphate and acetate b...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5452785</comments>
            <pubDate>Wed, 16 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5452785</guid>        </item>
        <item>
            <title>Enhanced β-Galactosidase Production from Whey Powder by a Mutant of the Psychrotolerant Yeast Guehomyces pullulans 17-1 for Hydrolysis of Lactose.</title>
            <link>http://www.medworm.com/index.php?rid=5452784&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22086565%26dopt%3DAbstract</link>
            <description>Authors: Xu JL, Zhao J, Wang LF, Sun HY, Song CL, Chi ZM
    Abstract
    In order to isolate β-galactosidase overproducers of the psychrotolerant yeast Guehomyces pullulans 17-1, its cells were mutated by using nitrosoguanidine (NTG). One mutant (NTG-133) with enhanced β-galactosidase production was obtained. The mutant grown in the production medium with 30.0 g/l lactose and 2.0 g/l glucose could produce more β-galactosidase than the same mutant grown in the production medium with only 30.0 g/l lactose while β-galactosidase production by its wild type was sensitive to the presence of glucose in the medium. It was found that 40.0 g/l of the whey powder was the most suitable for β-galactosidase production by the mutant. After optimization of the medium and cultivation conditions, ...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5452784</comments>
            <pubDate>Wed, 16 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5452784</guid>        </item>
        <item>
            <title>In Vitro Azadirachtin Production by Hairy Root Cultivation of Azadirachta indica in Nutrient Mist Bioreactor.</title>
            <link>http://www.medworm.com/index.php?rid=5411435&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22083394%26dopt%3DAbstract</link>
            <description>Authors: Srivastava S, Srivastava AK
    Abstract
    Azadirachtin, a well-known biopesticide is a secondary metabolite conventionally extracted from the seeds of Azadirachta indica. The present study involved in vitro azadirachtin production by developing hairy roots of A. indica via Agrobacterium rhizogenes-mediated transformation of A. indica explants. Liquid culture of hairy roots was established in shake flask to study the kinetics of growth and azadirachtin production. A biomass production of 13.3 g/L dry weight (specific growth rate of 0.7 day(-1)) was obtained after 25 days of cultivation period with an azadirachtin yield of 3.3 mg/g root biomass. To overcome the mass transfer limitation in conventionally used liquid-phase reactors, batch cultivation of hairy roots was carried ...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5411435</comments>
            <pubDate>Tue, 15 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5411435</guid>        </item>
        <item>
            <title>Genome Shuffling Enhanced ε-Poly-L: -Lysine Production by Improving Glucose Tolerance of Streptomyces graminearus.</title>
            <link>http://www.medworm.com/index.php?rid=5411434&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22083395%26dopt%3DAbstract</link>
            <description>Authors: Li S, Li F, Chen XS, Wang L, Xu J, Tang L, Mao ZG
    Abstract
    The productivity of ε-poly-L: -lysine (ε-PL) in currently reported wild-type strains is low. Here we improved glucose tolerance of a Streptomyces graminearus strain LS-B1 by genome shuffling while simultaneously enhancing the ε-PL productivity. The starting population was generated by ultraviolet irradiation and nitrosoguanidine mutagenesis and then subjected for recursive protoplast fusion. The positive colonies from library, created by fusing the inactivated protoplasts were screened on agar plates containing different concentrations of glucose. Characterization of all recombinants and wild-type strain in shake-flask fermentation indicated the compatibility of two phenotypes of glucose tolerance and ε-PL yiel...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5411434</comments>
            <pubDate>Tue, 15 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5411434</guid>        </item>
        <item>
            <title>Decarboxylation of Ferulic Acid to 4-Vinyl Guaiacol by Streptomyces setonii.</title>
            <link>http://www.medworm.com/index.php?rid=5411443&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22081324%26dopt%3DAbstract</link>
            <description>Authors: Max B, Carballo J, Cortés S, Domínguez JM
    Abstract
    4-Vinyl guaiacol (3-methoxy 4-hydroxystyrene) can be obtained by decarboxylation of ferulic acid by the strain Streptomyces setonii ATCC 39116. The formation of this metabolite was favoured by microaerobic conditions and the culture medium employed, increasing progressively the product concentration from 543.3 up to 885.1 mg/l when aeration level was diminished, reaching a highest volumetric productivity of 70.4 mg/l h and a product yield of 1.11 mol/mol. The identity of the metabolite was confirmed by gas chromatography-mass spectrometry. A metabolic study of ferulic acid and the main degradation products (ferulic acid, 4-vinyl guaiacol, protocatechuic acid, vanillyl alcohol, vanillic acid and vanillin) suggested th...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5411443</comments>
            <pubDate>Sat, 12 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5411443</guid>        </item>
        <item>
            <title>Adding Value to the Oil Cake as a Waste from Oil Processing Industry: Production of Lipase and Protease by Candida utilis in Solid State Fermentation.</title>
            <link>http://www.medworm.com/index.php?rid=5411442&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22081325%26dopt%3DAbstract</link>
            <description>Authors: Moftah OA, Grbavčić S, Zuža M, Luković N, Bezbradica D, Knežević-Jugović Z
    Abstract
    Olive oil cake is a by-product from the olive oil processing industry and can be used for the lipase and protease production by Candida utilis in solid state fermentation. Different carbon and nitrogen sources were evaluated, and the results showed that the supplementation of the substrate with maltose and starch as carbon sources and yeast extract as a nitrogen source significantly increased the lipase production. The best results were obtained with maltose, whereas rather low lipase and protease activities were found with glucose and oleic acid. Response surface methodology and a five-level-three-factor central composite rotatable design were used to evaluate the effects of the ini...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5411442</comments>
            <pubDate>Sat, 12 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5411442</guid>        </item>
        <item>
            <title>Development of Saccharomyces cerevisiae Producing Higher Levels of Sulfur Dioxide and Glutathione to Improve Beer Flavor Stability.</title>
            <link>http://www.medworm.com/index.php?rid=5411441&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22081326%26dopt%3DAbstract</link>
            <description>Authors: Chen Y, Yang X, Zhang S, Wang X, Guo C, Guo X, Xiao D
    Abstract
    Sulfur compounds, such as sulfite (SO(2)), hydrogen sulfide (H(2)S), and glutathione (GSH), play different roles in beer flavor stability. SO(2) and GSH have antiaging effects which are helpful to improve the flavor stability of beer, whereas H(2)S is undesirable to beer flavor because of its unpleasant aroma. Here, we report the development of Saccharomyces cerevisiae which produces higher levels of SO(2) and GSH but lower level of H(2)S to improve beer flavor stability by nongenetic engineering approaches. After two rounds of UV mutagenesis coupled with specific plate screening methods, one promising mutant named MV16 was obtained. Compared with the original strain, the SO(2) and GSH production of MV16 in fer...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5411441</comments>
            <pubDate>Sat, 12 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5411441</guid>        </item>
        <item>
            <title>Purification and Characterization of a Mannose Recognition Lectin from Oreochromis niloticus (Tilapia Fish): Cytokine Production in Mice Splenocytes.</title>
            <link>http://www.medworm.com/index.php?rid=5411440&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22081327%26dopt%3DAbstract</link>
            <description>In conclusion, OniL lectin was successfully purified and showed a preferential Th1 response in mice splenocytes.
    PMID: 22081327 [PubMed - as supplied by publisher] (Source: Applied Biochemistry and Biotechnology)</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5411440</comments>
            <pubDate>Sat, 12 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5411440</guid>        </item>
        <item>
            <title>Determination of Dimethyl Phthalate in Environment Water Samples by a Highly Sensitive Indirect Competitive ELISA.</title>
            <link>http://www.medworm.com/index.php?rid=5411439&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22081328%26dopt%3DAbstract</link>
            <description>Authors: Zhang M, Liu S, Zhuang H, Hu Y
    Abstract
    Recent controversy over the discovery of clouding agents containing the banned chemical di(2-ethylhexyl) phthalate in beverages in 2011 in Taiwan has caused public concerns. For the detection of dimethyl phthalate (DMP) in environment water samples, an indirect competitive enzyme-linked immunosorbent assay (ic-ELISA) was developed in this paper. Dimethyl 4-aminophthalate (4-DMAP) was covalently attached to bovine serum albumin as immunogen by a diazotization method. The conjugation of DMAP and ovalbumin as coating antigen was obtained in the same way. Polyclonal antibody was obtained from New Zealand white rabbits. Under the optimized conditions, DMP was detected in the concentration range of 0.02-419 ng/mL with a detection limit of...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5411439</comments>
            <pubDate>Sat, 12 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5411439</guid>        </item>
        <item>
            <title>An Optimum Fermentation Model Established by Genetic Algorithm for Biotransformation from Crude Polydatin to Resveratrol.</title>
            <link>http://www.medworm.com/index.php?rid=5411438&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22081329%26dopt%3DAbstract</link>
            <description>Authors: Chong Y, Yan A, Yang X, Cai Y, Chen J
    Abstract
    Natural resveratrol is widely used in medicine, food, and cosmetic because of its pharmacological properties. Due to its low content in plants, this study was conducted to increase the yield of resveratrol by microorganism transformation. Fungi Aspergillus niger AN-2436 was employed in biotransformation to produce resveratrol from polydatin, and genetic algorithm (GA) was used to optimize the fermentation conditions. A transformation ratio of higher than 95% was achieved in the following conditions: culture temperature of 30.3 °C, inoculum size of 20% (v/v), rotating speed of 147 rpm, and cultivation time of 36 h. Compared with the polydatin absorbance under the experimental conditions obtained by single-factor, orthogonal...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5411438</comments>
            <pubDate>Sat, 12 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5411438</guid>        </item>
        <item>
            <title>Production and Characteristics of the Whole-Cell Lipase from Organic Solvent Tolerant Burkholderia sp. ZYB002.</title>
            <link>http://www.medworm.com/index.php?rid=5411437&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22081330%26dopt%3DAbstract</link>
            <description>Authors: Shu ZY, Wu JG, Cheng LX, Chen D, Jiang YM, Li X, Huang JZ
    Abstract
    The thermostable and organic solvent tolerant whole-cell lipase (WCL) was produced by Burkholderia sp. ZYB002 with broad spectrum organic solvent tolerance. The production medium of the WCL was primarily optimized, which resulted in the maximum activity of 22.8 U/mL and the 5.1-fold increase of the WCL yield. The optimized culture medium was as follows (% w/v or v/v): soybean meal 2, soybean oil 0.5, manganese sulfate 0.1, K(2)HPO(4) 0.1, olive oil 0.5, initial pH 6.0, inoculum density 2, liquid volume 35 mL in 250-mL Erlenmeyer flask, and incubation time 24 h. The biochemical characterization of the WCL from Burkholderia sp. ZYB002 was determined, and the results showed that the optimal pH and temperat...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5411437</comments>
            <pubDate>Sat, 12 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5411437</guid>        </item>
        <item>
            <title>A Laccase of Fomes durissimus MTCC-1173 and Its Role in the Conversion of Methylbenzene to Benzaldehyde.</title>
            <link>http://www.medworm.com/index.php?rid=5411436&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22081331%26dopt%3DAbstract</link>
            <description>Authors: Sahay R, Yadav RS, Yadava S, Yadav KD
    Abstract
    A laccase has been purified from the liquid culture growth medium containing bagasse particles of Fomes durissimus. The method involved concentration of the culture filtrate by ultrafiltration and anion exchange chromatography on diethyl aminoethyl cellulose. The sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) and native polyacrylamide gel electrophoresis both gave single protein band indicating that the enzyme preparation was pure. The molecular mass of the purified laccase determined from SDS-PAGE analysis was 75 kDa. Using 2,6-dimethoxyphenol as the substrate, the determined K           (m) and k           (cat) values of the laccase are 182 μM and 0.35 s(-1), respectively, giving a k           (ca...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5411436</comments>
            <pubDate>Sat, 12 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5411436</guid>        </item>
        <item>
            <title>Photoprotective Effects of a Formulation Containing Tannase-Converted Green Tea Extract Against UVB-Induced Oxidative Stress in Hairless Mice.</title>
            <link>http://www.medworm.com/index.php?rid=5411453&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22068688%26dopt%3DAbstract</link>
            <description>Authors: Hong YH, Jung EY, Shin KS, Kim TY, Yu KW, Chang UJ, Suh HJ
    Abstract
    Ultraviolet B (UVB) irradiation may induce the acceleration of skin aging. The purpose of this study was to develop an effective formulation containing tannase-converted green tea extract (FTGE) to inhibit UVB-induced oxidative damage. Significant (p &amp;lt; 0.05) prevention of the reduced form of glutathione (GSH) depletion was observed in mice treated with FTGE. The hydrogen peroxide levels of mice treated with FTGE were similar to those of UVB non-irradiated mice. No significant difference was observed between No UVB control and FTGE mice. Also, mice treated with FTGE had significant (p &amp;lt; 0.05) decreases in thiobarbituric acid-reactive substance levels by lipid peroxidation compared with No UVB ...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5411453</comments>
            <pubDate>Thu, 10 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5411453</guid>        </item>
        <item>
            <title>Discrimination of A1555G and C1494T Point Mutations in the Mitochondrial 12S rRNA Gene by On/Off Switch.</title>
            <link>http://www.medworm.com/index.php?rid=5411452&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22068689%26dopt%3DAbstract</link>
            <description>The objective of this study was to apply the &quot;on/off&quot; switch consisting of 3' phosphorothioate-modified allele specific primers and exo(+) polymerase in single base discrimination of A1555G and C1494T mutations in the highly conserved sites of the mitochondrial 12S rRNA. The two point mutations are the hotspot mutations associated with either aminoglycoside antibiotics induced deafness or inherited nonsyndromic hearing loss. The PCR products of mitochondrial DNA (mtDNA) 12S rRNA gene were inserted into the pMD19-T vector for transformation into Escherichia coli JM109 competent cells for preparing wild-type pMD19-T/mt vector. Inverse PCR was carried out for mtDNA 12S rRNA gene C1494T and A1555G mutagenesis and DpnI endonuclease degradating methylated pMD19-T/mt vector existing in the invers...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5411452</comments>
            <pubDate>Thu, 10 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5411452</guid>        </item>
        <item>
            <title>Kinetics of Ergothioneine Inhibition of Mushroom Tyrosinase.</title>
            <link>http://www.medworm.com/index.php?rid=5411451&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22068690%26dopt%3DAbstract</link>
            <description>Authors: Liao WC, Wu WH, Tsai PC, Wang HF, Liu YH, Chan CF
    Abstract
    The native amino acid ergothioneine, a thiourea derivative of histidine, inhibits mushroom tyrosinase activity in a dose-dependent manner, with an IC(50) value of 1.025 mg/ml (4.47 mM). By contrast, histidine exhibited no inhibitory effect on mushroom tyrosinase activity. We characterized ergothioneine as a noncompetitive tyrosinase inhibitor using a Lineweaver-Burk plot of experimental kinetic data. The IC(50) value for ergothioneine scavenging of 2,2-diphenyl-1-picrylhydrazyl was 6.110 ± 0.305 mg/ml, much higher than the IC(50) for inhibition of tyrosinase activity which indicating ergothioneine on tyrosinase shows a weak correlation to its antioxidative activity. The results demonstrated that ergothionei...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5411451</comments>
            <pubDate>Thu, 10 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5411451</guid>        </item>
        <item>
            <title>Chemiluminescent Detection of Carbohydrates in the Tumoral Breast Diseases.</title>
            <link>http://www.medworm.com/index.php?rid=5411450&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22068691%26dopt%3DAbstract</link>
            <description>Authors: Brustein VP, Cavalcanti CL, de Melo-Junior MR, Correia MT, Beltrão EI, Carvalho LB
    Abstract
    Nowadays, there is an increase of investigations into the fibroadenoma, mainly because some studies have shown that the occurrence of fibroadenoma is linked to an increased risk of developing breast carcinoma. Currently, the chemiluminescence biomarkers are applied for validation methods and screening. Here, a lectin chemiluminescence is proposed as new histochemistry method to identify carbohydrates in mammary tumoral tissues. The lectins concanavalin A (Con A) and peanut agglutinin (PNA) conjugated to acridinium ester were used to characterize the glycocode of breast tissues: normal, fibroadenoma, and invasive duct carcinoma (IDC). The lectin chemiluminescence expressed in relati...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5411450</comments>
            <pubDate>Thu, 10 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5411450</guid>        </item>
        <item>
            <title>Optimization of Culture Conditions for 1,3-Propanediol Production from Glycerol Using a Mutant Strain of Klebsiella pneumoniae.</title>
            <link>http://www.medworm.com/index.php?rid=5411449&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22072138%26dopt%3DAbstract</link>
            <description>Authors: Oh BR, Seo JW, Heo SY, Hong WK, Luo LH, Kim S, Park DH, Kim CH
    Abstract
    In the present work, mutant strains of Klebsiella pneumoniae with deletions of the als gene encoding acetolactate synthase involved in synthesis of 2,3-butanediol, the ldhA gene encoding lactate dehydrogenase required for lactate synthesis, or both genes, were prepared. Production of 1,3-propanediol (1,3-PD) from glycerol was enhanced in the ldhA mutant strain (ΔldhA), but lower in Δals or Δals ΔldhA mutant strains compared to the parent strain, concomitant with a reduction in the glycerol consumption rate, indicating that deletion of ldhA alone was useful to improve 1,3-PD production. Fed-batch fermentation analysis revealed that, in the ΔldhA mutant strain, 1,3-PD production was higher at low pH...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5411449</comments>
            <pubDate>Thu, 10 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5411449</guid>        </item>
        <item>
            <title>Characterization and Enhanced Production of Prodigiosin from the Spoiled Coconut.</title>
            <link>http://www.medworm.com/index.php?rid=5411448&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22072139%26dopt%3DAbstract</link>
            <description>Authors: Siva R, Subha K, Bhakta D, Ghosh AR, Babu S
    Abstract
    Many bacterial secondary products are bioactive substances that play an important role in biotechnology and pharmacology (e.g., as antibiotics or antitumor agents). Over the past few years interest in prodigiosin has been increased due to its promising anti-cancer activity. Prodigiosin is also of potential clinical interest because it is reported to have anti-fungal, anti-bacterial, anti-protozoal/anti-malarial, and immunosuppressive activity. Thus there is a need to develop a high-throughput and cost-effective bioprocess for the production of prodigiosin. In the present study, Serratia rubidaea was isolated from colored portion of a spoiled coconut and further it was authenticated by MTCC, India. The various parameters ...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5411448</comments>
            <pubDate>Thu, 10 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5411448</guid>        </item>
        <item>
            <title>In Silico Characterization of Alkaline Proteases from Different Species of Aspergillus.</title>
            <link>http://www.medworm.com/index.php?rid=5411447&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22072140%26dopt%3DAbstract</link>
            <description>Authors: Morya VK, Yadav S, Kim EK, Yadav D
    Abstract
    A total of 49 protein sequences of alkaline proteases retrieved from GenBank representing different species of Aspergillus have been characterized for various physiochemical properties, homology search, multiple sequence alignment, motif, and super family search and phylogenetic tree construction. The sequence level homology was obtained among different groups of alkaline protease enzymes, viz alkaline serine protease, oryzin, calpain-like protease, serine protease, subtilisin-like alkaline proteases. Multiple sequence alignment of alkaline protease protein sequence of different Aspergillus species revealed a stretch of conserved region for amino acid residues from 69 to 110 and 130-204. The phylogenetic tree constructed indicate...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5411447</comments>
            <pubDate>Thu, 10 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5411447</guid>        </item>
        <item>
            <title>Xylanase and β-Xylosidase Production by Aspergillus ochraceus: New Perspectives for the Application of Wheat Straw Autohydrolysis Liquor.</title>
            <link>http://www.medworm.com/index.php?rid=5411446&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22072141%26dopt%3DAbstract</link>
            <description>Authors: Michelin M, Polizeli MD, Ruzene DS, Silva DP, Vicente AA, Jorge JA, Terenzi HF, Teixeira JA
    Abstract
    The xylanase biosynthesis is induced by its substrate-xylan. The high xylan content in some wastes such as wheat residues (wheat bran and wheat straw) makes them accessible and cheap sources of inducers to be mainly applied in great volumes of fermentation, such as those of industrial bioreactors. Thus, in this work, the main proposal was incorporated in the nutrient medium wheat straw particles decomposed to soluble compounds (liquor) through treatment of lignocellulosic materials in autohydrolysis process, as a strategy to increase and undervalue xylanase production by Aspergillus ochraceus. The wheat straw autohydrolysis liquor produced in several conditions was used as ...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5411446</comments>
            <pubDate>Thu, 10 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5411446</guid>        </item>
        <item>
            <title>Isolation and Characterization of a Novel Plasma Membrane Intrinsic Protein Gene, LcPIP1, in Leymus chinensis that Enhances Salt Stress Tolerance in Saccharomyces cerevisiae.</title>
            <link>http://www.medworm.com/index.php?rid=5411445&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22072142%26dopt%3DAbstract</link>
            <description>Authors: Ma P, Liu J
    Abstract
    A novel plasma membrane intrinsic, LcPIP1, was isolated from Leymus chinensis using RACE method. The LcPIP1 has 288 amino acids with an estimated molecular mass of 30.6 kDa. Semi RT-PCR analysis indicated that the expression level of LcPIP1 was obviously higher in leaf than root. The LcPIP1 was also found to be induced by salt stress. In addition, transformed with the LcPIP1, Saccharomyces cerevisiae could increase tolerance to salt stress. These results indicate that the LcPIP1 gene seems to play a role in resistance against salt stress.
    PMID: 22072142 [PubMed - as supplied by publisher] (Source: Applied Biochemistry and Biotechnology)</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5411445</comments>
            <pubDate>Thu, 10 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5411445</guid>        </item>
        <item>
            <title>Overview of Fungal Lipase: A Review.</title>
            <link>http://www.medworm.com/index.php?rid=5411444&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22072143%26dopt%3DAbstract</link>
            <description>Authors: Singh AK, Mukhopadhyay M
    Abstract
    Lipases (triacylglycerolacyl hydrolases, EC3.1.1.3) are class of enzymes which catalyze the hydrolysis of long-chain triglycerides. In this review paper, an overview regarding the fungal lipase production, purification, and application is discussed. The review describes various industrial applications of lipase in pulp and paper, food, detergent, and textile industries. Some important lipase-producing fungal genera include Aspergillus, Penicillium, Rhizopus, Candida, etc. Current fermentation process techniques such as batch, fed-batch, and continuous mode of lipase production in submerged and solid-state fermentations are discussed in details. The purification of lipase by hydrophobic interaction chromatography is also discussed. The deve...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5411444</comments>
            <pubDate>Thu, 10 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5411444</guid>        </item>
        <item>
            <title>On-line Characterization of Metabolic State in Batch Cultivation of Clostridium diolis for 1,3-Propanediol Production Using NADH+H(+) Fluorescence.</title>
            <link>http://www.medworm.com/index.php?rid=5411484&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22057935%26dopt%3DAbstract</link>
            <description>Authors: Kaur G, Sharma R, Srivastava AK, Chand S
    Abstract
    NADH is a coenzyme which plays a central role in cellular growth and metabolism. It is an intracellular fluorophore which fluoresces at 460 nm when cells are irradiated by 340 nm wavelength of light. The application of NADH+H(+) fluorescence measurement for characterization of biomass and its metabolic activity during batch fermentation of 1,3-propanediol (1,3-PD) using Clostridium diolis was investigated in this study. A linear correlation between net fluorescence and biomass concentration was observed during both the initial and final phases of 1,3-PD fermentation. This could be used as an on-line indicator of biomass concentration inside the bioreactor thereby eliminating the need for sampling and off-line analysis for...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5411484</comments>
            <pubDate>Sun, 06 Nov 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5411484</guid>        </item>
        <item>
            <title>Molecular Analysis of OsLEA4 and Its Contributions to Improve E. coli Viability.</title>
            <link>http://www.medworm.com/index.php?rid=5411483&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22057936%26dopt%3DAbstract</link>
            <description>Authors: Hu T, Zeng H, He S, Wu Y, Wang G, Huang X
    Abstract
    OsLEA4, a late embryogenesis abundant (LEA) protein gene from rice (Oryza sativa L.), contains a 312-bp open reading frame encoding a putative polypeptide of 103 amino acids with a calculated molecular mass of 11.19 kDa and a theoretical pI of 10.04. OsLEA4 polypeptide is rich in Ala (22%), Lys (15%), Glu (9%), His (8%), Thr (8%), and Arg (7%) and lacking in Trp, Cys, Asn, and Phe residues. OsLEA4 protein contains a Pfam:LEA_1 domain architecture at positions 1-73 with three α-helical domains and without β-sheet domain. In silico predictions showed that OsLEA4 protein was strongly hydrophilic with the grand average of hydropathy value of -0.816 and instability index of 27.31. The hydrophilic regions were found in the co...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5411483</comments>
            <pubDate>Sun, 06 Nov 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5411483</guid>        </item>
        <item>
            <title>Trifluoroethanol-Induced Changes in Activity and Conformation of Manganese-Containing Superoxide Dismutase.</title>
            <link>http://www.medworm.com/index.php?rid=5411482&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22057937%26dopt%3DAbstract</link>
            <description>Authors: Yin SJ, Lü ZR, Park D, Chung HY, Yang JM, Zhou HM, Qian GY, Park YD
    Abstract
    Superoxide dismutase (SOD, EC 1.15.1.1) plays an important role in antioxidant defense in organisms exposed to oxygen. However, there is a lack of research into the regulation of SOD activity and structural changes during folding, especially for SOD originating from extremophiles. We studied the inhibitory effects of trifluoroethanol (TFE) on the activity and conformation of manganese-containing SOD (Mn-SOD) from Thermus thermophilus. TFE decreased the degree of secondary structure of Mn-SOD, which directly resulted in enzyme inactivation and disrupted the tertiary structure of Mn-SOD. The kinetic studies showed that TFE-induced inactivation of Mn-SOD is a first-order reaction and that the region...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5411482</comments>
            <pubDate>Sun, 06 Nov 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5411482</guid>        </item>
        <item>
            <title>Selection of a New Whole Cell Biocatalyst for the Synthesis of 2-Deoxyribose 5-Phosphate.</title>
            <link>http://www.medworm.com/index.php?rid=5411481&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22057938%26dopt%3DAbstract</link>
            <description>Authors: Valino AL, Palazzolo MA, Iribarren AM, Lewkowicz E
    Abstract
    2-Deoxyribose 5-phosphate (DR5P) is a key intermediate in the biocatalyzed preparation of deoxyribonucleosides. Therefore, DR5P production by means of simpler, cleaner, and economic pathways becomes highly interesting. One strategy involves the use of bacterial whole cells containing DR5P aldolase as biocatalyst for the aldol addition between acetaldehyde and D: -glyceraldehyde 3-phosphate or glycolytic intermediates that in situ generate the acceptor substrate. In this work, diverse microorganisms capable of synthesizing DR5P were selected by screening several bacteria genera. In particular, Erwinia carotovora ATCC 33260 was identified as a new biocatalyst that afforded 14.1-mM DR5P starting from a cheap raw mate...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5411481</comments>
            <pubDate>Sun, 06 Nov 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5411481</guid>        </item>
        <item>
            <title>Molecular Cloning and Characterization of a Putative cDNA Encoding Endoglucanase IV from Trichoderma Viride and its Expression in Bombyx Mori.</title>
            <link>http://www.medworm.com/index.php?rid=5411480&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22057939%26dopt%3DAbstract</link>
            <description>In this study, a putative endoglucanase IV (EG IV) complementary DNA was cloned from the mycelium of a strain of the filamentous fungus Trichoderma viride using a PCR-based exon-splicing method and expressed in both a silkworm BmN cell line and in silkworm larvae. Western blot analysis detected a band of 42 kDa in BmN cells after infection with a recombinant mBacmid/BmNPV/EG IV baculovirus. Sequence alignment analysis of the T. viride EG IV gene showed two domains that were highly conserved with glycosyl hydrolases and a funga-type cellulose-binding domain. Analysis of variance showed that silkworms infected with recombinant baculoviruses exhibited significantly higher enzyme activity that was 48.84% higher than silkworms infected with blank baculoviruses and 46.61% higher than normal sil...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5411480</comments>
            <pubDate>Sun, 06 Nov 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5411480</guid>        </item>
        <item>
            <title>Production, Partial Characterization, and Use of a Red Biochrome Produced by Serratia sakuensis subsp. nov Strain KRED for Dyeing Natural Fibers.</title>
            <link>http://www.medworm.com/index.php?rid=5411479&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22057940%26dopt%3DAbstract</link>
            <description>Authors: Vaidyanathan J, Bhathena-Langdana Z, Adivarekar RV, Nerurkar M
    Abstract
    We have described a novel red biochrome, 514 Da in size, produced by solid-state cultivation of a bacterial isolate obtained from garden soil. The growth requirements of the isolate, the chemical characteristics of the biochrome produced, and the application of the biochrome in dying of silk, wool, and cotton fabrics have been studied. The biochrome obtained after 52 h of incubation and having a λ           (max) of 535 nm was used for dyeing the fabrics. We found that silk, wool, and cotton fabrics dyed with this new natural red compound have high color strength values and dye uptake along with good color fastness as well as antibacterial activity.
    PMID: 22057940 [PubMed - as supplied by publi...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5411479</comments>
            <pubDate>Sun, 06 Nov 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5411479</guid>        </item>
        <item>
            <title>Lipids Containing Polyunsaturated Fatty Acids Synthesized by Zygomycetes Grown on Glycerol.</title>
            <link>http://www.medworm.com/index.php?rid=5411505&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22057906%26dopt%3DAbstract</link>
            <description>Authors: Bellou S, Moustogianni A, Makri A, Aggelis G
    Abstract
    Several strains of Zygomycetes cultivated on glycerol produced mycelia rich in lipids containing higher amounts of neutral lipids (NL) than glycolipids plus sphingolipids and phospholipids (P), while biosynthesis of P in Mortierella ramanniana, Mucor sp., and Cunninghamella echinulata occurred though NL accumulation process was in progress. Polyunsaturated fatty acids (PUFA) concentration gradually decreased in all lipid fractions of M. ramanniana during growth. In contrast, in C. echinulata concentration of both linoleic and γ-linolenic acids increased with time, especially in P. Taking for granted that the main function of PUFA is associated to their participation in mycelial membranes, we could suppose that biosynth...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5411505</comments>
            <pubDate>Sat, 05 Nov 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5411505</guid>        </item>
        <item>
            <title>Decolorization of Remazol Brilliant Blue R by a Purified Laccase of Polyporus brumalis.</title>
            <link>http://www.medworm.com/index.php?rid=5411503&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22057907%26dopt%3DAbstract</link>
            <description>Authors: Kim H, Lee S, Ryu S, Choi HT
    Abstract
    A white rot basidiomycete Polyporus brumalis has been reported to induce two laccase genes under degradation conditions of dibutylphthalate. When this fungus was grown in a minimal medium, one laccase enzyme was detected by the native polyacrylamide gel electrophoresis. A laccase was purified through ammonium sulfate precipitation and ion exchange chromatography, and the estimated molecular weight was 70 kDa. The optimum pH and temperature of the purified laccase was pH 4.0 and 20 °C, respectively. The K           (m) value of the enzyme was 685.0 μM, and the V           (max) was 0.147 ODmin(-1) unit(-1) for o-tolidine. Purified laccase showed effective decolorization of a dye, Remazol Brilliant Blue R (RBBR), without any lacca...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5411503</comments>
            <pubDate>Sat, 05 Nov 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5411503</guid>        </item>
        <item>
            <title>A Galactomannan-Driven Enhancement of the In Vitro Multiplication Rate for the Marubakaido Apple Rootstock (Malus prunifolia (Willd.) Borkh) is Not Related to the Degradation of the Exogenous Galactomannan.</title>
            <link>http://www.medworm.com/index.php?rid=5411496&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22057908%26dopt%3DAbstract</link>
            <description>Authors: Pereira-Netto AB, Meneguin RG, Biz A, Silveira JL
    Abstract
    Agar is a complex mixture of gel-forming polysaccharides. Gelling agents are very often used to provide proper support for plants grown in semisolid culture media. And agar is the most frequently used gelling agent in plant tissue culture media. Galactomannans, another group of gel-forming polysaccharides, consists of a (1 → 4)-linked β-D: -mannopyranosyl backbone partially substituted at O-6 with D: -galactopyranosyl side groups. In this work, we demonstrate that a statistically significant 2.7-fold increase on the multiplication rate (MR) for in vitro-grown Marubakaido (Malus prunifolia) shoots was associated with a 12.5% replacement of agar in the semi-solid culture media for a galactomannan obtained from...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5411496</comments>
            <pubDate>Sat, 05 Nov 2011 04:00:00 +0100</pubDate>
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        <item>
            <title>Preliminary Studies for Cephamycin C Purification Technique.</title>
            <link>http://www.medworm.com/index.php?rid=5411489&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22057909%26dopt%3DAbstract</link>
            <description>Authors: de Baptista Neto A, Bustamante MC, de Oliveira JH, Granato AC, Bellão C, Junior AC, Barboza M, Hokka CO
    Abstract
    A study was made for purification of cephamycin C from fermentation of Streptomyces clavuligerus. Initially, the culture broth was clarified by microfiltration and ultrafiltration, after which the resulting permeates were subjected to nonspecific adsorption and ion-exchange chromatography on resin columns. The antibiotic activity was measured by the biological method at each stage by assaying its activity against the Escherichia coli ESS, super sensitive to β-lactam antibiotic. The purification processes were assessed in relation to the variables affecting each step. The purification efficiency by nonspecific adsorption was monitored by UV spectrophotometry, w...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5411489</comments>
            <pubDate>Sat, 05 Nov 2011 04:00:00 +0100</pubDate>
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        <item>
            <title>Sox9 Is Upstream of MicroRNA-140 in Cartilage.</title>
            <link>http://www.medworm.com/index.php?rid=5411507&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22052544%26dopt%3DAbstract</link>
            <description>Authors: Nakamura Y, He X, Kato H, Wakitani S, Kobayashi T, Watanabe S, Iida A, Tahara H, Warman ML, Watanapokasin R, Postlethwait JH
    Abstract
    MicroRNA-140 (miR-140) is specifically expressed in developing cartilage tissues. We have previously reported that miR-140 plays an important role during palatal cartilage development by modulating platelet-derived growth factor receptor alpha (pdgfra) in zebrafish. However, the regulatory mechanism of miR-140 in cartilage is still unknown. Using developing zebrafish, sox9a mutant (sox9a-/-) and sox9b mutant (sox9b-/-) zebrafish and SOX9 small interfering RNA in human chondrocytes, T/C-28 cells, we found that miR-140 is regulated by the cartilage master transcription regulator Sox9 in zebrafish and mammalian cells.
    PMID: 22052544 [PubMed...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5411507</comments>
            <pubDate>Fri, 04 Nov 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5411507</guid>        </item>
        <item>
            <title>The Effect of Ni(2+) and Cu          (2+) on the Photocatalytic Degradation of Dyes by the Chitosan-TiO(2) Complex.</title>
            <link>http://www.medworm.com/index.php?rid=5411506&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22052545%26dopt%3DAbstract</link>
            <description>The Effect of Ni(2+) and Cu     (2+) on the Photocatalytic Degradation of Dyes by the Chitosan-TiO(2) Complex.
    Appl Biochem Biotechnol. 2011 Oct 22;
    Authors: Zhao X, Xiao G, Zhang X, Su H, Tan T
    Abstract
    The present research combines biosorption and photocatalysis in a functional TiO(2)-immobilized chitosan adsorbent (CTA). CTA can degrade organic pollutants and adsorb metal ions simultaneously. Target pollutants were dyes of cationic (rhodamine B, Rh.B) and anionic (methyl orange, MO) nature, with Ni(2+) and Cu(2+) selected as heavy metals. The presence of Ni(2+) or Cu(2+) improved the degradation ability of CTA for MO, but inhibited the degradation of Rh.B, with Cu(2+) exhibiting stronger effects than Ni(2+). There was no significant difference in CTA activity when the me...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5411506</comments>
            <pubDate>Sat, 22 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5411506</guid>        </item>
        <item>
            <title>Cloning and Characterization of Two β-Glucosidase/Xylosidase Enzymes from Yak Rumen Metagenome.</title>
            <link>http://www.medworm.com/index.php?rid=5358244&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22020745%26dopt%3DAbstract</link>
            <description>Authors: Bao L, Huang Q, Chang L, Sun Q, Zhou J, Lu H
    Abstract
    Two β-glucosidase/xylosidase genes, Rubg3A and Rubg3B, were cloned from yak rumen uncultured microorganisms by metagenome method and function-based screening. Recombinant RuBG3A and RuBG3B purified from Escherichia coli were characterized for enzymatic properties, and they exhibited activity against 4-nitrophenyl-β-D: -glucopyranoside and 4-nitrophenyl-β-D: -xylopyranoside, suggesting bifunctional β-glucosidase/xylosidase activity. Chromatography analysis showed that they could effectively hydrolyze cellooligosaccharide substrates, indicating the facilitation in saccharification of cellulose. RuBG3A and RuBG3B can also increase the reducing sugar released in xylan hydrolysis to 218% and 169%, respectively, through s...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5358244</comments>
            <pubDate>Sat, 22 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5358244</guid>        </item>
        <item>
            <title>Thermostable Bacterial Endoglucanases Mined from Swiss-Prot Database.</title>
            <link>http://www.medworm.com/index.php?rid=5323960&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21989797%26dopt%3DAbstract</link>
            <description>Authors: Qiu LH, Li CX, Sun J, Wang Z, Ye Q, Xu JH
    Abstract
    As one critical enzyme in deconstructing complicated cellulose matrix, endoglucanase (EG) is needed to exhibit high activity and thermostability under severe industrial conditions. Driven by this purpose, EGtf1 (Q08166) and EGtf2 (Q7X2N2), with relatively high specific activities, were selected out of 43 putative EG genes from SWISS-PROT database. These distinguished EGs were successfully overexpressed in Escherichia coli and purified by one-step affinity chromatography. The maximal activity was shown at approximate pH 5.0 and 50 °C. It is worth noting that EGtf1 and EGtf2 displayed outstanding thermostability with a half-life of up to 1,386 h at 50 °C, which is almost 100-fold higher than other reported EGs. Further...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5323960</comments>
            <pubDate>Wed, 12 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5323960</guid>        </item>
        <item>
            <title>Immobilized Laccase on a New Cryogel Carrier and Kinetics of Two Anthraquinone Derivatives Oxidation.</title>
            <link>http://www.medworm.com/index.php?rid=5323959&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21989798%26dopt%3DAbstract</link>
            <description>Authors: Stanescu MD, Sanislav A, Ivanov RV, Hirtopeanu A, Lozinsky VI
    Abstract
    A coordinatively immobilized laccase was prepared using a new cryogel type carrier. The support has a wide-pore texture facilitating diffusion of different substrates to the enzyme reaction center. The biocatalyst proved to be efficient in decolorization of two anthraquinone derivatives, namely Acid Blue 62 and bromaminic acid. After 24 h over 80% of the two substrates have been oxidated. The kinetic data (K           (m) and V           (max)) for the oxidation of the two anthraquinone derivatives, with the free and immobilized enzyme, have been determined and compared. Other parameters, like k           (cat) and the specificity constant have been calculated and analyzed. The influence of substrate p...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5323959</comments>
            <pubDate>Wed, 12 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5323959</guid>        </item>
        <item>
            <title>Cellulase Hydrolysis of Unsorted MSW.</title>
            <link>http://www.medworm.com/index.php?rid=5323958&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21989799%26dopt%3DAbstract</link>
            <description>Authors: Jensen JW, Felby C, Jørgensen H
    Abstract
    A recent development in waste management and engineering has shown that the cellulase can be used for the liquefaction of organic fractions in household waste. The focus of this study was to optimize the enzyme hydrolysis of thermally treated municipal solid waste (MSW) by the addition of surfactant. Concurrently, the enzyme performance was analysed on pure cellulose in a solution of MSW wastewater. Results showed no effect of surfactant addition to the hydrolysis media as measured by viscosity and particle size distribution. MSW treatment wastewater was found to contain a high amount of calcium, potassium, sodium, chloride and others that may affect cellulolytic enzymes. Cellulase performance showed no effect of adding the metal i...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5323958</comments>
            <pubDate>Wed, 12 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5323958</guid>        </item>
        <item>
            <title>Conversion of Isoeugenol to Vanillin by Psychrobacter sp. Strain CSW4.</title>
            <link>http://www.medworm.com/index.php?rid=5323957&amp;cid=s_36928_60_f&amp;fid=36928&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21989800%26dopt%3DAbstract</link>
            <description>Authors: Ashengroph M, Nahvi I, Zarkesh-Esfahani H, Momenbeik F
    Abstract
    To screen strains of halotolerant or halophile bacteria which are able to convert isoeugenol to vanillin, 36 different strains of bacteria isolated from the salty environments in Iran were investigated. During growth on isoeugenol, a moderately halotolerant Gram-negative coccobacil showed capability of converting isoeugenol to vanillin. Based on morphological, physiological, and phylogenetic studies, strain CSW4 was classified as a bacterium belonging to the genus Psychrobacter. The bioconversion products were confirmed by thin-layer chromatography, high-performance liquid chromatography, and spectral data obtained from UV/Vis spectroscopy, FTIR, and mass-spectroscopy. Using growing cells, vanillin reached its...</description>
            <author>Applied Biochemistry and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5323957</comments>
            <pubDate>Wed, 12 Oct 2011 04:00:00 +0100</pubDate>
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