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        <title>Applied Microbiology and Biotechnology via MedWorm.com</title>
        <description>MedWorm.com provides a medical RSS filtering service. Over 6000 RSS medical sources are combined and output via different filters. This feed contains the latest items from the 'Applied Microbiology and Biotechnology' source.</description>
        <link><![CDATA[http://www.medworm.com/rss/search.php?qu=Applied+Microbiology+and+Biotechnology&t=Applied+Microbiology+and+Biotechnology&s=Search&f=source]]></link>
        <lastBuildDate>Thu, 09 Feb 2012 21:34:54 +0100</lastBuildDate>
        <item>
            <title>Depolymerization of alginate into a monomeric sugar acid using Alg17C, an exo-oligoalginate lyase cloned from Saccharophagus degradans 2-40.</title>
            <link>http://www.medworm.com/index.php?rid=5637840&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22281843%26dopt%3DAbstract</link>
            <description>Authors: Kim HT, Chung JH, Wang D, Lee J, Woo HC, Choi IG, Kim KH
    Abstract
    Macroalgae are considered to be promising biomass for fuels and chemicals production. To utilize brown macroalgae as biomass, the degradation of alginate, which is the main carbohydrate of brown macroalgae, into monomeric units is a critical prerequisite step. Saccharophagus degradans 2-40 is capable of degrading more than ten different polysaccharides including alginate, and its genome sequence demonstrated that this bacterium contains several putative alginate lyase genes including alg17C. The gene for Alg17C, which is classified into the PL-17 family, was cloned and overexpressed in Escherichia coli. The recombinant Alg17C was found to preferentially act on oligoalginates with degrees of polymerization hi...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5637840</comments>
            <pubDate>Fri, 27 Jan 2012 05:00:00 +0100</pubDate>
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        <item>
            <title>Developing symbiotic consortia for lignocellulosic biofuel production.</title>
            <link>http://www.medworm.com/index.php?rid=5637842&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22278256%26dopt%3DAbstract</link>
            <description>Authors: Zuroff TR, Curtis WR
    Abstract
    The search for petroleum alternatives has motivated intense research into biological breakdown of lignocellulose to produce liquid fuels such as ethanol. Degradation of lignocellulose for biofuel production is a difficult process which is limited by, among other factors, the recalcitrance of lignocellulose and biological toxicity of the products. Consolidated bioprocessing has been suggested as an efficient and economical method of producing low value products from lignocellulose; however, it is not clear whether this would be accomplished more efficiently with a single organism or community of organisms. This review highlights examples of mixtures of microbes in the context of conceptual models for developing symbiotic consortia for biofuel p...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5637842</comments>
            <pubDate>Thu, 26 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5637842</guid>        </item>
        <item>
            <title>Improved detection of Rhodococcus coprophilus with a new quantitative PCR assay.</title>
            <link>http://www.medworm.com/index.php?rid=5637841&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22278257%26dopt%3DAbstract</link>
            <description>Authors: Wicki M, Auckenthaler A, Felleisen R, Liniger M, Loutre C, Niederhauser I, Tanner M, Baumgartner A
    Abstract
    Agricultural practices, such as spreading liquid manure or the utilisation of land as animal pastures, can result in faecal contamination of water resources. Rhodococcus coprophilus is used in microbial source tracking to indicate animal faecal contamination in water. Methods previously described for detecting of R. coprophilus in water were neither sensitive nor specific. Therefore, the aim of this study was to design and validate a new quantitative polymerase chain reaction (qPCR) to improve the detection of R. coprophilus in water. The new PCR assay was based on the R. coprophilus 16S rRNA gene. The validation showed that the new approach was specific and sensitiv...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5637841</comments>
            <pubDate>Thu, 26 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5637841</guid>        </item>
        <item>
            <title>Inhibition of anthrax lethal factor: lability of hydroxamate as a chelating group.</title>
            <link>http://www.medworm.com/index.php?rid=5637844&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22270239%26dopt%3DAbstract</link>
            <description>Authors: Li F, Chvyrkova I, Terzyan S, Wakeham N, Turner R, Ghosh AK, Zhang XC, Tang J
    Abstract
    The metalloprotease activity of lethal factor (LF) from Bacillus anthracis (B. anthracis) is a main source of toxicity in the lethality of anthrax infection. Thus, the understanding of the enzymatic activity and inhibition of B. anthracis LF is of scientific and clinical interests. We have designed, synthesized, and studied a peptide inhibitor of LF, R9LF-1, with the structure NH(2)-(D: -Arg)(9)-Val-Leu-Arg-CO-NHOH in which the C-terminal hydroxamic acid is commonly used in the inhibitors of metalloproteases to chelate the active-site zinc. This inhibitor was shown to be very stable in solution and effectively inhibited LF in kinetic assays. However, its protection on murine macrophages ...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5637844</comments>
            <pubDate>Wed, 25 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5637844</guid>        </item>
        <item>
            <title>Indole-3-acetaldehyde from Rhodococcus sp. BFI 332 inhibits Escherichia coli O157:H7 biofilm formation.</title>
            <link>http://www.medworm.com/index.php?rid=5637843&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22274708%26dopt%3DAbstract</link>
            <description>Authors: Lee JH, Kim YG, Kim CJ, Lee JC, Cho MH, Lee J
    Abstract
    Pathogenic biofilms have been associated with persistent infections due to their high resistance to antimicrobial agents. To identify nontoxic biofilm inhibitors for enterohemorrhagic Escherichia coli O157:H7, the spent media of a 4,104 Actinomycetes library was screened. The culture spent medium (1%, v/v) of plant pathogen Rhodococcus sp. BFI 332 markedly inhibited E. coli O157:H7 biofilm formation without affecting the growth of planktonic E. coli O157:H7 cells. Rhodococcus sp. BFI 332 produced significant amounts of indole-3-acetaldehyde and indole-3-acetic acid, and the former of which reduced E. coli O157:H7 biofilm formation. Global transcriptome analyses showed that indole-3-acetaldehyde most repressed two curli...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5637843</comments>
            <pubDate>Wed, 25 Jan 2012 05:00:00 +0100</pubDate>
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        <item>
            <title>Expression and purification of recombinant tung tree diacylglycerol acyltransferase 2.</title>
            <link>http://www.medworm.com/index.php?rid=5637847&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22270236%26dopt%3DAbstract</link>
            <description>Authors: Cao H, Chapital DC, Howard OD, Deterding LJ, Mason CB, Shockey JM, Klasson KT
    Abstract
    Diacylglycerol acyltransferases (DGATs) esterify sn-1,2-diacylglycerol with a long-chain fatty acyl-CoA, the last and rate-limiting step of triacylglycerol (TAG) biosynthesis in eukaryotic organisms. At least 74 DGAT2 sequences from 61 organisms have been identified, but the expression of any DGAT2 as a partial or full-length protein in Escherichia coli had not been reported. The main objective of this study was to express and purify recombinant DGAT2 (rDGAT2) from E. coli for antigen production with a minor objective to compare rDGAT2 expression in yeast. A plasmid was engineered to express tung tree DGAT2 fused to maltose binding protein and poly-histidine (His) affinity tags. Immunobl...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5637847</comments>
            <pubDate>Sun, 22 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5637847</guid>        </item>
        <item>
            <title>Effect of pretreatment of hydrothermally processed rice straw with laccase-displaying yeast on ethanol fermentation.</title>
            <link>http://www.medworm.com/index.php?rid=5637845&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22270238%26dopt%3DAbstract</link>
            <description>Authors: Nakanishi A, Bae JG, Fukai K, Tokumoto N, Kuroda K, Ogawa J, Nakatani M, Shimizu S, Ueda M
    Abstract
    A gene encoding laccase I was identified and cloned from the white-rot fungus Trametes sp. Ha1. Laccase I contained 10 introns and an original secretion signal sequence. After laccase I without introns was prepared by overlapping polymerase chain reaction, it was inserted into expression vector pULD1 for yeast cell surface display. The oxidation activity of a laccase-I-displaying yeast as a whole-cell biocatalyst was examined with 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulphonic acid) (ABTS), and the constructed yeast showed a high oxidation activity. After the pretreatment of hydrothermally processed rice straw (HPRS) with laccase-I-displaying yeast with ABTS, fermentation ...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5637845</comments>
            <pubDate>Sun, 22 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5637845</guid>        </item>
        <item>
            <title>BMP2 promotes migration and invasion of breast cancer cells via cytoskeletal reorganization and adhesion decrease: an AFM investigation.</title>
            <link>http://www.medworm.com/index.php?rid=5637848&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22270235%26dopt%3DAbstract</link>
            <description>Authors: Jin H, Pi J, Huang X, Huang F, Shao W, Li S, Chen Y, Cai J
    Abstract
    Bone morphogenetic protein 2 (BMP2) has been shown to modulate the proliferation and differentiation of breast cancer cells. However, the biochemical effects and mechanisms remain unknown. In this paper, the effects of recombinant human BMP2 on the migration of MCF-7 cells-one breast cancer cell line, using transwell and wound healing experiments, as well as on the cellular morphology, cytoskeleton, cell surface adhesion, and stiffness detected at subcellular level by an atomic force microscope, were investigated. After BMP2 treatment, the untreated round-shaped MCF-7 cells transformed to a spindle-like shape with lots of specialized structures, such as lamellipodia, filopodia, membrane protrusions, and ot...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5637848</comments>
            <pubDate>Sat, 21 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5637848</guid>        </item>
        <item>
            <title>Expression and characterization of a novel metagenome-derived cellulase Exo2b and its application to improve cellulase activity in Trichoderma reesei.</title>
            <link>http://www.medworm.com/index.php?rid=5637846&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22270237%26dopt%3DAbstract</link>
            <description>Authors: Geng A, Zou G, Yan X, Wang Q, Zhang J, Liu F, Zhu B, Zhou Z
    Abstract
    A metagenomic fosmid library containing 1 × 10(5) clones was constructed from a biogas digester fed with pig ordure and rice straw. In total, 121 clones with activity of 4-methylumbelliferyl-cellobiosidase were screened from the metagenomic library. A novel GH5 cellulase gene exo2b was identified from a sequenced clone EXO02C10 and expressed in Escherichia coli BL21. The corresponding recombinant Exo2b protein showed high specific activity toward both carboxymethylcellulose (CMC; 260 U/mg protein) and β-D: -glucan from barley (849 U/mg), with an optimal pH and temperature of 7.5 and 58 °C, respectively. Exo2b showed stable activity at a wide pH range from 5.5 to 9.0 and was highly thermostable a...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5637846</comments>
            <pubDate>Sat, 21 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5637846</guid>        </item>
        <item>
            <title>Rapid detection methods for Bacillus anthracis in environmental samples: a review.</title>
            <link>http://www.medworm.com/index.php?rid=5619719&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22262227%26dopt%3DAbstract</link>
            <description>Authors: Irenge LM, Gala JL
    Abstract
    Bacillus anthracis is a Gram-positive, spore-forming bacterium, which causes anthrax, an often lethal disease of animals and humans. Although the disease has been well studied since the nineteenth century, it has witnessed a renewed interest during the past decade, due to its use as a bioterrorist agent in the fall of 2001 in the USA. A number of techniques aimed at rapidly detecting B. anthracis, in environmental samples as well as in point-of-care settings for humans suspected of exposure to the pathogen, are now available. These technologies range from culture-based methods to portable DNA amplification devices. Despite recent developments, specific identification of B. anthracis still remains difficult because of its phenotypic and genotypic...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5619719</comments>
            <pubDate>Fri, 20 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5619719</guid>        </item>
        <item>
            <title>A genetically engineered protein domain binding to bacterial murein, archaeal pseudomurein, and fungal chitin cell wall material.</title>
            <link>http://www.medworm.com/index.php?rid=5619718&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22262228%26dopt%3DAbstract</link>
            <description>Authors: Visweswaran GR, Dijkstra BW, Kok J
    Abstract
    The major murein and pseudomurein cell wall-binding domains, i.e., the Lysin Motif (LysM) (Pfam PF01476) and pseudomurein cell wall-binding (PMB) (Pfam PF09373) motif, respectively, were genetically fused. The fusion protein is capable of binding to both murein- and pseudomurein-containing cell walls. In addition, it also binds to chitin, the major polymer of fungal cell walls. Binding is influenced by pH and occurs at a pH close to the pI of the binding protein. Functional studies on truncated versions of the fusion protein revealed that murein and chitin binding is provided by the LysM domain, while binding to pseudomurein is achieved through the PMB domain.
    PMID: 22262228 [PubMed - as supplied by publisher] (Source: Applie...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5619718</comments>
            <pubDate>Fri, 20 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5619718</guid>        </item>
        <item>
            <title>Molecular cloning and functional analysis of a recombinant ribosome-inactivating protein (alpha-momorcharin) from Momordica charantia.</title>
            <link>http://www.medworm.com/index.php?rid=5619717&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22262229%26dopt%3DAbstract</link>
            <description>In this study, we expressed the protein in Escherichia coli Rosetta (DE3) pLysS strain and purified it by nickel-nitrilotriacetic acid affinity chromatography. A total of 85 mg of homogeneous protein was obtained from 1 l culture supernatant of Rosetta (DE3) pLysS, showing a high recovery rate of 73.9%. Protein activity assay indicated that α-MC had both N-glycosidase activity and DNA-nuclease activity, the former releasing RIP diagnostic RNA fragment (Endo's fragment) from rice rRNAs and the latter converting supercoiled circular DNA of plasmid pET-32a(+) into linear conformations in a concentration-dependent manner. Specially, we found that α-MC could inhibit the mycelial growth of Fusarium solani and Fusarium oxysporum with IC(50) values of 6.23 and 4.15 μM, respectively. Results ...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5619717</comments>
            <pubDate>Fri, 20 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5619717</guid>        </item>
        <item>
            <title>Backwash intensity and frequency impact the microbial community structure and function in a fixed-bed biofilm reactor.</title>
            <link>http://www.medworm.com/index.php?rid=5619723&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22258640%26dopt%3DAbstract</link>
            <description>Authors: Li X, Yuen W, Morgenroth E, Raskin L
    Abstract
    Linkages among bioreactor operation and performance and microbial community structure were investigated for a fixed-bed biofilm system designed to remove perchlorate from drinking water. Perchlorate removal was monitored to evaluate reactor performance during and after the frequency and intensity of the backwash procedure were changed, while the microbial community structure was studied using clone libraries and quantitative PCR targeting the 16S rRNA gene. When backwash frequency was increased from once per month to once per day, perchlorate removal initially deteriorated and then recovered, and the relative abundance of perchlorate-reducing bacteria (PRB) initially increased and then decreased. This apparent discrepancy sugge...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5619723</comments>
            <pubDate>Thu, 19 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5619723</guid>        </item>
        <item>
            <title>Expression and characterization of styrene monooxygenases of Rhodococcus sp. ST-5 and ST-10 for synthesizing enantiopure (S)-epoxides.</title>
            <link>http://www.medworm.com/index.php?rid=5619722&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22258641%26dopt%3DAbstract</link>
            <description>Authors: Toda H, Imae R, Komio T, Itoh N
    Abstract
    Styrene monooxygenase (StyA, SMOA)- and flavin oxidoreductase (StyB, SMOB)-coding genes of styrene-assimilating bacteria Rhodococcus sp. ST-5 and ST-10 were successfully expressed in Escherichia coli. Determined amino acid sequences of StyAs and StyBs of ST-5 and ST-10 showed more similarity with those of Pseudomonas than with self-sufficient styrene monooxygenase (StyA2B) of Rhodococcus. Recombinant enzymes were purified from E. coli cells as functional proteins, and their properties were characterized in detail. StyBs (flavin oxidoreductase) of strains ST-5 and ST-10 have similar enzymatic properties to those of Pseudomonas, but StyB of strain ST-10 exhibited higher temperature stability than that of strain ST-5. StyAs of strains ...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5619722</comments>
            <pubDate>Thu, 19 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5619722</guid>        </item>
        <item>
            <title>Enzyme-based glucose delivery as a high content screening tool in yeast-based whole-cell biocatalysis.</title>
            <link>http://www.medworm.com/index.php?rid=5619721&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22258642%26dopt%3DAbstract</link>
            <description>Authors: Grimm T, Grimm M, Klat R, Neubauer A, Palela M, Neubauer P
    Abstract
    The influence of glucose release on growth and biotransformation of yeasts was examined by using the medium EnBase(®) Flo in shake flasks. The medium contains a polysaccharide acting as substrate, which is degraded to glucose by the addition of an enzyme. In the present paper, this medium was adapted for the cultivation of yeasts by increasing the complex components (booster) and the enzyme concentrations to guarantee a higher glucose release rate. Important changes were an increase of the complex component booster to 10-15% and an increased glucose release by increasing the enzyme content to 15 U L(-1). The 20 yeasts investigated in the present work showed an improvement of growth and biomass production ...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5619721</comments>
            <pubDate>Thu, 19 Jan 2012 05:00:00 +0100</pubDate>
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        <item>
            <title>Production, purification, and characterization of the cecropin from Plutella xylostella, pxCECA1, using an intein-induced self-cleavable system in Escherichia coli.</title>
            <link>http://www.medworm.com/index.php?rid=5619720&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22258643%26dopt%3DAbstract</link>
            <description>In this study, we expressed and characterized the cecropin from Plutella xylostella (pxCECA1) using an intein-dependent expression system in Escherichia coli. We cloned the pxCECA1 gene from larva by RT-PCR and fused the encoding sequence of mature pxCECA1 with an intein gene and a chitin-binding domain gene (CBD) in pTWIN1 plasmid. The fusion protein CBD-intein-pxCECA1 was expressed in E. coli BL21 (DE3) and separated by flowing cell extracts through a chitin column. Subsequently, self-cleavage of the intein at its C-terminus was induced in a temperature- and pH-dependent manner, resulting in the release of mature pxCECA1. The optimal conditions for self-cleavage were determined to be pH 6.0 for 48 h at 4°C, under which 12.3 mg of recombinant pxCECA1 could be recovered from 1 l of E. ...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5619720</comments>
            <pubDate>Thu, 19 Jan 2012 05:00:00 +0100</pubDate>
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        <item>
            <title>Biodiscovery of new Australian thraustochytrids for production of biodiesel and long-chain omega-3 oils.</title>
            <link>http://www.medworm.com/index.php?rid=5619726&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22252264%26dopt%3DAbstract</link>
            <description>Authors: Lee Chang KJ, Dunstan GA, Abell GC, Clementson LA, Blackburn SI, Nichols PD, Koutoulis A
    Abstract
    Heterotrophic growth of thraustochytrids has potential in co-producing a feedstock for biodiesel and long-chain (LC, ≥C(20)) omega-3 oils. Biodiscovery of thraustochytrids from Tasmania (temperate) and Queensland (tropical), Australia, covered a biogeographic range of habitats including fresh, brackish, and marine waters. A total of 36 thraustochytrid strains were isolated and separated into eight chemotaxonomic groups (A-H) based on fatty acid (FA) and sterol composition which clustered closely with four different genera obtained by 18S rDNA molecular identification. Differences in the relative proportions (%FA) of long-chain C(20), C(22), omega-3, and omega-6 polyunsaturat...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5619726</comments>
            <pubDate>Wed, 18 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5619726</guid>        </item>
        <item>
            <title>Comparison and characterization of α-amylase inducers in Aspergillus nidulans based on nuclear localization of AmyR.</title>
            <link>http://www.medworm.com/index.php?rid=5619725&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22252265%26dopt%3DAbstract</link>
            <description>Authors: Murakoshi Y, Makita T, Kato M, Kobayashi T
    Abstract
    AmyR, a fungal transcriptional activator responsible for induction of amylolytic genes in Aspergillus nidulans, localizes to the nucleus in response to the physiological inducer isomaltose. Maltose, kojibiose, and D: -glucose were also found to trigger the nuclear localization of GFP-AmyR. Isomaltose- and kojibiose-triggered nuclear localization was not inhibited by the glucosidase inhibitor, castanospermine, while maltose-triggered localization was inhibited. Thus, maltose itself does not appear to be an direct inducer, but its degraded or transglycosylated product does. Non-metabolizable D: -glucose analogues were also able to trigger the nuclear localization, implying that these sugars, except maltose, directly functio...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5619725</comments>
            <pubDate>Wed, 18 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5619725</guid>        </item>
        <item>
            <title>Controlled synthesis of Mn(2)O          (3) nanowires by hydrothermal method and their bactericidal and cytotoxic impact: a promising future material.</title>
            <link>http://www.medworm.com/index.php?rid=5619724&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22252266%26dopt%3DAbstract</link>
            <description>Controlled synthesis of Mn(2)O     (3) nanowires by hydrothermal method and their bactericidal and cytotoxic impact: a promising future material.
    Appl Microbiol Biotechnol. 2012 Jan 18;
    Authors: Hassan MS, Amna T, Pandeya DR, Hamza AM, Bing YY, Kim HC, Khil MS
    Abstract
    Mn(2)O(3) nanowires with diameter ~70 nm were synthesized by a simple hydrothermal method using Mn(II) nitrate as precursor. X-ray diffraction, field emission scanning electron microscopy, transmission electron microscopy (TEM), and energy dispersive X-ray spectroscopy techniques were employed to study structural features and chemical composition of the synthesized nanowires. A biological evaluation of the antimicrobial activity and cytotoxicity of Mn(2)O(3) nanowires was carried out using Escherichia coli a...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5619724</comments>
            <pubDate>Wed, 18 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5619724</guid>        </item>
        <item>
            <title>Enzymatic decolorization of spent textile dyeing baths composed by mixtures of synthetic dyes and additives.</title>
            <link>http://www.medworm.com/index.php?rid=5619737&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22249715%26dopt%3DAbstract</link>
            <description>Authors: Ciullini I, Gullotto A, Tilli S, Sannia G, Basosi R, Scozzafava A, Briganti F
    Abstract
    The effects of different components of real dyeing bath formulations, such as the equalizing and fixing additives-acids, salts, and surfactants-on the decolorization catalyzed by Funalia trogii enzymatic extracts, were investigated to understand their influence on the recalcitrance to biodegradation of this type of wastewater. The decolorization of selected dyes and dye mixtures after tissue dyeing was performed in the presence/absence of auxiliary compounds. All spent dyeing baths were enzymatically decolorized to different extents, by the addition of extracts containing laccase only or laccase plus cellobiose dehydrogenase. Whereas surfactant auxiliaries, in some instances, inhibit the...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5619737</comments>
            <pubDate>Tue, 17 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5619737</guid>        </item>
        <item>
            <title>Analysis of alkane-dependent methanogenic community derived from production water of a high-temperature petroleum reservoir.</title>
            <link>http://www.medworm.com/index.php?rid=5619736&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22249716%26dopt%3DAbstract</link>
            <description>Authors: Mbadinga SM, Li KP, Zhou L, Wang LY, Yang SZ, Liu JF, Gu JD, Mu BZ
    Abstract
    Microbial assemblage in an n-alkanes-dependent thermophilic methanogenic enrichment cultures derived from production waters of a high-temperature petroleum reservoir was investigated in this study. Substantially higher amounts of methane were generated from the enrichment cultures incubated at 55 °C for 528 days with a mixture of long-chain n-alkanes (C(15)-C(20)). Stoichiometric estimation showed that alkanes-dependent methanogenesis accounted for about 19.8% of the total amount of methane expected. Hydrogen was occasionally detected together with methane in the gas phase of the cultures. Chemical analysis of the liquid cultures resulted only in low concentrations of acetate and formate. Phylog...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5619736</comments>
            <pubDate>Tue, 17 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5619736</guid>        </item>
        <item>
            <title>Fungal aryl-alcohol oxidase: a peroxide-producing flavoenzyme involved in lignin degradation.</title>
            <link>http://www.medworm.com/index.php?rid=5619735&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22249717%26dopt%3DAbstract</link>
            <description>Authors: Hernández-Ortega A, Ferreira P, Martínez AT
    Abstract
    Aryl-alcohol oxidase (AAO) is an extracellular flavoprotein providing the H(2)O(2) required by ligninolytic peroxidases for fungal degradation of lignin, the key step for carbon recycling in land ecosystems. O(2) activation by Pleurotus eryngii AAO takes place during the redox-cycling of p-methoxylated benzylic metabolites secreted by the fungus. Only Pleurotus AAO sequences were available for years, but the number strongly increased recently due to sequencing of different basidiomycete genomes, and a comparison of 112 GMC (glucose-methanol-choline oxidase) superfamily sequences including 40 AAOs is presented. As shown by kinetic isotope effects, alcohol oxidation by AAO is produced by hydride transfer to the flavin, a...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5619735</comments>
            <pubDate>Tue, 17 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5619735</guid>        </item>
        <item>
            <title>In vitro synthesis of polyhydroxyalkanoate (PHA) incorporating lactate (LA) with a block sequence by using a newly engineered thermostable PHA synthase from Pseudomonas sp. SG4502 with acquired LA-polymerizing activity.</title>
            <link>http://www.medworm.com/index.php?rid=5619734&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22249718%26dopt%3DAbstract</link>
            <description>In this study, we cloned a pha locus from the bacterium and identified two genes encoding PHA synthases (PhaC1(SG) and PhaC2(SG)). Two mutations, Ser324Thr and Gln480Lys, corresponding to those of a lactate (LA)-polymerizing enzyme (LPE) from mesophilic Pseudomonas sp. 61-3 were introduced into PhaC1(SG) to evaluate the potential of the resulting protein as a &quot;thermostable LPE&quot;. The mutated PhaC1(SG) [PhaC1(SG)(STQK)] showed high thermal stability in synthesizing P(LA-co-3HB) in an in vitro reaction system under a range of high temperatures. Requirement of 3HBCoA as a priming unit for LA polymerization by the LPE has been suggested in both of the in vitro and in vivo experiments. Based on the finding, the PhaC1(SG)(STQK)-mediated synthesis of a LA-based copolymer with a block sequence was ...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5619734</comments>
            <pubDate>Tue, 17 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5619734</guid>        </item>
        <item>
            <title>Intestinal microbiota associated with differential feed conversion efficiency in chickens.</title>
            <link>http://www.medworm.com/index.php?rid=5619733&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22249719%26dopt%3DAbstract</link>
            <description>In this study, differences in cecal and jejunal microbiota between broiler chickens with extreme feed conversion capabilities were analysed in order to identify candidate bacteria that may influence growth performance. The jejunal microbiota was largely dominated by lactobacilli (over 99% of jejunal sequences) and showed no difference between the birds with high and low feed conversion ratios. The cecal microbial community displayed higher diversity, and 24 unclassified bacterial species were found to be significantly (&amp;lt;0.05) differentially abundant between high and low performing birds. Such differentially abundant bacteria represent target populations that could potentially be modified with prebiotics and probiotics in order to improve animal growth performance.
    PMID: 22249719 [Pu...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5619733</comments>
            <pubDate>Tue, 17 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5619733</guid>        </item>
        <item>
            <title>Disruption of the acetate kinase (ack) gene of Clostridium acetobutylicum results in delayed acetate production.</title>
            <link>http://www.medworm.com/index.php?rid=5619732&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22249720%26dopt%3DAbstract</link>
            <description>Authors: Kuit W, Minton NP, López-Contreras AM, Eggink G
    Abstract
    In microorganisms, the enzyme acetate kinase (AK) catalyses the formation of ATP from ADP by de-phosphorylation of acetyl phosphate into acetic acid. A mutant strain of Clostridium acetobutylicum lacking acetate kinase activity is expected to have reduced acetate and acetone production compared to the wild type. In this work, a C. acetobutylicum mutant strain with a selectively disrupted ack gene, encoding AK, was constructed and genetically and physiologically characterized. The ack           (-) strain showed a reduction in acetate kinase activity of more than 97% compared to the wild type. The fermentation profiles of the ack           (-) and wild-type strain were compared using two different fermentation media,...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5619732</comments>
            <pubDate>Tue, 17 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5619732</guid>        </item>
        <item>
            <title>Enzymatic biotransformation of ginsenoside Rb1 to 20(S)-Rg3 by recombinant β-glucosidase from Microbacterium esteraromaticum.</title>
            <link>http://www.medworm.com/index.php?rid=5619731&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22249721%26dopt%3DAbstract</link>
            <description>Authors: Quan LH, Min JW, Yang DU, Kim YJ, Yang DC
    Abstract
    Microbacterium esteraromaticum was isolated from ginseng field. The β-glucosidase gene (bgp1) from M. esteraromaticum was cloned and expressed in Escherichia coli BL21 (DE3). The bgp1 gene consists of 2,496 bp encoding 831 amino acids which have homology to the glycosyl hydrolase family 3 protein domain. The recombinant β-glucosidase enzyme (Bgp1) was purified and characterized. The molecular mass of purified Bgp1 was 87.5 kDa, as determined by SDS-PAGE. Using 0.1 mg ml(-1) enzyme in 20 mM sodium phosphate buffer at 37°C and pH 7.0, 1.0 mg ml(-1) ginsenoside Rb1 was transformed into 0.444 mg ml(-1) ginsenoside Rg3 within 6 h. The Bgp1 sequentially hydrolyzed the outer and inner glucose attached to the C-20 po...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5619731</comments>
            <pubDate>Tue, 17 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5619731</guid>        </item>
        <item>
            <title>SUMO fusion system facilitates soluble expression and high production of bioactive human fibroblast growth factor 23 (FGF23).</title>
            <link>http://www.medworm.com/index.php?rid=5619730&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22249722%26dopt%3DAbstract</link>
            <description>Authors: Liu X, Chen Y, Wu X, Li H, Jiang C, Tian H, Tang L, Wang D, Yu T, Li X
    Abstract
    As a key humoral regulator of phosphate homeostasis and its involvement in the pathogenesis of human disease, human fibroblast growth factor 23 (hFGF23) has become a particularly attractive therapeutic target. To prepare soluble and bioactive recombinant human FGF23 to meet the increasing demand in its pharmacological application, small ubiquitin-related modifier (SUMO)-FGF23 fusion gene and FGF23 non-fusion gene were amplified by standard PCR methods and cloned into vector pET-22b and pET-3c, then transformed into Escherichia coli Rosetta (DE3) and BL21 (DE3). The best combination of plasmid and host strain was screened, and only Rosetta (DE3)/pET-SUMO-FGF23 was screened for rhFGF23 protein ex...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5619730</comments>
            <pubDate>Tue, 17 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5619730</guid>        </item>
        <item>
            <title>Characterization of alcohol dehydrogenase 3 of the thermotolerant methylotrophic yeast Hansenula polymorpha.</title>
            <link>http://www.medworm.com/index.php?rid=5619729&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22249723%26dopt%3DAbstract</link>
            <description>In this study, we identified and characterized mitochondrial alcohol dehydrogenase 3 from the thermotolerant methylotrophic yeast Hansenula polymorpha (HpADH3). The amino acid sequence of HpADH3 shares over 70% of its identity with the alcohol dehydrogenases of other yeasts and exhibits the highest similarity of 91% with the alcohol dehydrogenase 1 of H. polymorpha. However, unlike the cytosolic HpADH1, HpADH3 appears to be a mitochondrial enzyme, as a mitochondrial targeting extension exists at its N terminus. The recombinant HpADH3 overexpressed in Escherichia coli showed similar catalytic efficiencies for ethanol oxidation and acetaldehyde reduction. The HpADH3 displayed substrate specificities with clear preferences for medium chain length primary alcohols and acetaldehyde for an oxida...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5619729</comments>
            <pubDate>Tue, 17 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5619729</guid>        </item>
        <item>
            <title>Degradation of the novel herbicide ZJ0273 by Amycolatopsis sp. M3-1 isolated from soil.</title>
            <link>http://www.medworm.com/index.php?rid=5619728&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22249724%26dopt%3DAbstract</link>
            <description>In this study, 15 bacteria capable of utilizing ZJ0273 as the sole carbon source were isolated from soil. One of the isolates belonged to the family Amycolatopsis and was designated to Amycolatopsis sp. M3-1; at 30°C and pH 7.0, degradation rate of ZJ0273 could reach at 59.3% and 68.5% in 25 days and 60 days, respectively. Furthermore, six metabolites (M1-M6) during the degradation of ZJ0273 by Amycolatopsis sp. M3-1 were identified by a combination with multi-position (14)C-labeled compounds (B-ZJ0273 and C-ZJ0273), chromatography, liquid scintillation spectrometer, and LC-MS, a novel pathway of ZJ0273 degradation by Amycolatopsis sp. M3-1 was proposed based on the identified metabolites and their biodegradation courses. ZJ0273 was initially hydrolyzed into M1 (4-(2-(4,6-dimethoxypyrim...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5619728</comments>
            <pubDate>Tue, 17 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5619728</guid>        </item>
        <item>
            <title>Optimization of enzymatic hydrolysis of pretreated rice straw and ethanol production.</title>
            <link>http://www.medworm.com/index.php?rid=5619727&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22249725%26dopt%3DAbstract</link>
            <description>Authors: Singh A, Bishnoi NR
    Abstract
    Cellulase, Tween 80, and β-glucosidase loading were studied and optimized by response surface methodology to improve saccharification. Microwave alkali-pretreated rice straw used as substrate for onsite enzyme production by Aspergillus heteromorphus and Trichoderma reesei. The highest enzymatic hydrolysis (84%) was obtained from rice straw at crude enzyme loading of 10 FPU/gds of cellulase, 0.15% Tween 80, and 100 international unit/g dry solids of β-glucosidase activities. Enzymatic hydrolyzate of pretreated rice straw was used for ethanol production by Saccharomyces cerevisiae, Scheffersomyces stipitis, and by co-culture of both. The yield of ethanol was 0.50, 0.47, and 0.48 g(p)/g(s) by S. cerevisiae, S. stipitis, and by co-culture, res...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5619727</comments>
            <pubDate>Tue, 17 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5619727</guid>        </item>
        <item>
            <title>Characterization of a new ScbR-like γ-butyrolactone binding regulator (SlbR) in Streptomyces coelicolor.</title>
            <link>http://www.medworm.com/index.php?rid=5619741&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22246527%26dopt%3DAbstract</link>
            <description>Authors: Yang YH, Song E, Kim JN, Lee BR, Kim EJ, Park SH, Kim WS, Park HY, Jeon JM, Rajesh T, Kim YG, Kim BG
    Abstract
    γ-Butyrolactones in Streptomyces are well recognized as bacterial hormones, and they affect secondary metabolism of Streptomyces. γ-Butyrolactone receptors are considered important regulatory proteins, and various γ-butyrolactone synthases and receptors have been reported in Streptomyces. Here, we characterized a new regulator, SCO0608, that interacted with SCB1 (γ-butyrolactone of Streptomyces coelicolor) and bound to the scbR/A and adpA promoters. The SCO0608 protein sequences are not similar to those of any known γ-butyrolactone binding proteins in Streptomyces such as ScbR from S. coelicolor or ArpA from Streptomyces griseus. Interestingly, SCO0608 functio...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5619741</comments>
            <pubDate>Sat, 14 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5619741</guid>        </item>
        <item>
            <title>Mercury-resistant rhizobial bacteria isolated from nodules of leguminous plants growing in high Hg-contaminated soils.</title>
            <link>http://www.medworm.com/index.php?rid=5619740&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22246528%26dopt%3DAbstract</link>
            <description>Authors: Ruiz-Díez B, Quiñones MA, Fajardo S, López MA, Higueras P, Fernández-Pascual M
    Abstract
    A survey of symbiotic bacteria from legumes grown in high mercury-contaminated soils (Almadén, Spain) was performed to produce a collection of rhizobia which could be well adapted to the environmental conditions of this region and be used for restoration practices. Nineteen Hg-tolerant rhizobia were isolated from nodules of 11 legume species (of the genera Medicago, Trifolium, Vicia, Lupinus, Phaseolus, and Retama) and characterized. Based on their growth on Hg-supplemented media, the isolates were classified into three susceptibility groups. The minimum inhibitory concentrations (MICs) and the effective concentrations that produce 50% mortality identified the patterns of mercury t...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5619740</comments>
            <pubDate>Sat, 14 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5619740</guid>        </item>
        <item>
            <title>Evaluation of aroma active compounds in Tuber fruiting bodies by gas chromatography-olfactometry in combination with aroma reconstitution and omission test.</title>
            <link>http://www.medworm.com/index.php?rid=5619739&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22246529%26dopt%3DAbstract</link>
            <description>Authors: Liu RS, Li DC, Li HM, Tang YJ
    Abstract
    The aroma active compounds of three Tuber fruiting bodies (i.e., Tuber himalayense, Tuber indicum, and Tuber sinense) were firstly systematically evaluated by instrumental gas chromatography-olfactometry combining with quantitative analysis, aroma reconstitution, and omission tests. Twelve aroma active compounds were characterized by aroma extract dilution analysis, and 3-(methylthio) propanal, 3-methylbutanal, and 1-octen-3-ol with the highest flavor dilution (FD) factor (i.e., 1,024-2,048) were suggested as key contributors to the aroma. Odor activity value (OAV) was employed to determine the relative contribution of each compound to the aroma, and the compound with the highest FD factor also had the highest OAV (i.e., 10,234-242,95...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5619739</comments>
            <pubDate>Sat, 14 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5619739</guid>        </item>
        <item>
            <title>Modifying the product pattern of Clostridium acetobutylicum                 : Physiological effects of disrupting the acetate and acetone formation pathways.</title>
            <link>http://www.medworm.com/index.php?rid=5619738&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22246530%26dopt%3DAbstract</link>
            <description>In this study, a set of five knock-out mutants with defects in the central fermentative metabolism were generated using the ClosTron technology, including the construction of targeted double knock-out mutants of C. acetobtuylicum ATCC 824. While disruption of the acetate biosynthetic pathway had no significant impact on the metabolite distribution, mutants with defects in the acetone pathway, including both acetoacetate decarboxylase (Adc)-negative and acetoacetyl-CoA:acyl-CoA transferase (CtfAB)-negative mutants, exhibited high amounts of acetate in the fermentation broth. Distinct butyrate increase and decrease patterns during the course of fermentations provided experimental evidence that butyrate, but not acetate, is re-assimilated via an Adc/CtfAB-independent pathway in C. acetobutyli...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5619738</comments>
            <pubDate>Sat, 14 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5619738</guid>        </item>
        <item>
            <title>Developing fungal pigments for &quot;painting&quot; vascular plants.</title>
            <link>http://www.medworm.com/index.php?rid=5619742&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22237673%26dopt%3DAbstract</link>
            <description>Developing fungal pigments for &quot;painting&quot; vascular plants.
    Appl Microbiol Biotechnol. 2012 Jan 13;
    Authors: Robinson SC
    Abstract
    The use of fungal pigments as color additives to wood as a method to increase forest revenue is a relatively new, but quickly developing field. Sugar maple (Acer saccharum) is currently the primary utilized hardwood for spalting and appears to be the best suited North American hardwood for such purposes. The combination of Trametes versicolor and Bjerkandera adusta has been identified in several instances as a strong fungal pairing for zone line production; however, Xylaria polymorpha is capable of creating zone lines without the antagonism of a secondary fungus. Few fungal pigments have been developed for reliable use; Scytalidium cuboideum is ca...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5619742</comments>
            <pubDate>Fri, 13 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5619742</guid>        </item>
        <item>
            <title>Preparation and characterization of a thermostable enzyme (Mn-SOD) immobilized on supermagnetic nanoparticles.</title>
            <link>http://www.medworm.com/index.php?rid=5619743&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22237672%26dopt%3DAbstract</link>
            <description>In this study, the recombinant thermostable manganese superoxide dismutase (Mn-SOD) of Thermus thermophilus wl was purified and covalently immobilized onto supermagnetic 3-APTES-modified Fe(3)O(4)@SiO(2) nanoparticles using glutaraldehyde method to prepare the Mn-SOD bound magnetic nanoparticles. The Mn-SOD nanoparticles were characterized by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, X-ray diffraction, transmission electron microscopy, and vibrating sample magnetometer analysis. The results indicated that the diameter of Mn-SOD nanoparticles was 40 (± 5) nm, and its saturation magnetization value was 27.9 emu/g without remanence or coercivity. By comparison with the free Mn-SOD, it was found that the immobilized Mn-SOD on nanoparticles exhibited better resistance to temp...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5619743</comments>
            <pubDate>Thu, 12 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5619743</guid>        </item>
        <item>
            <title>Hot or not? Discovery and characterization of a thermostable alditol oxidase from Acidothermus cellulolyticus 11B.</title>
            <link>http://www.medworm.com/index.php?rid=5619752&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22231860%26dopt%3DAbstract</link>
            <description>We describe the discovery, isolation and characterization of a highly thermostable alditol oxidase from Acidothermus cellulolyticus 11B. This protein was identified by searching the genomes of known thermophiles for enzymes homologous to Streptomyces coelicolor A3(2) alditol oxidase (AldO). A gene (sharing 48% protein sequence identity to AldO) was identified, cloned and expressed in Escherichia coli. Following 6xHis tag purification, characterization revealed the protein to be a covalent flavoprotein of 47 kDa with a remarkably similar reactivity and substrate specificity to that of AldO. A steady-state kinetic analysis with a number of different polyol substrates revealed lower catalytic rates but slightly altered substrate specificity when compared to AldO. Thermostability measurements...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5619752</comments>
            <pubDate>Wed, 11 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5619752</guid>        </item>
        <item>
            <title>Screening of enzymatic activities for the depolymerisation of the marine bacterial exopolysaccharide HE800.</title>
            <link>http://www.medworm.com/index.php?rid=5619750&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22234531%26dopt%3DAbstract</link>
            <description>This study reports the screening for enzymes capable of depolymerising the EPS HE800. A large diversity of enzyme sources has been studied: commercially available glycoside hydrolases with broad substrate specificity, lyases, and proteases as well as growing microorganisms. Interestingly, we found that the genus Enterococcus and, more particularly, the strain Enterococcus faecalis were able to depolymerise the EPS HE800. Partial characterization of the enzymatic activity gives evidence for a random and incomplete depolymerisation pattern that yields low-molecular-weight products of 40,000 g mol(-1). Genomic analysis and activity assays allowed the identification of a relevant open reading frame (ORF) which encodes an endo-N-acetyl-galactosaminidase. This study establishes the foundation...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5619750</comments>
            <pubDate>Wed, 11 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5619750</guid>        </item>
        <item>
            <title>Modelling growth of, and removal of Zn and Hg by a wild microalgal consortium.</title>
            <link>http://www.medworm.com/index.php?rid=5619749&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22234532%26dopt%3DAbstract</link>
            <description>Authors: Monteiro CM, Brandão TR, Castro PM, Malcata FX
    Abstract
    Microorganisms isolated from sites contaminated with heavy metals usually possess a higher removal capacity than strains from regular cultures. Heavy metal-containing soil samples from an industrial dumpsite in Northern Portugal were accordingly collected; following enrichment under metal stress, a consortium of wild microalgae was obtained. Their ability to grow in the presence of, and their capacity to recover heavy metals was comprehensively studied; the datasets thus generated were fitted to by a combined model of biomass growth and metal uptake, derived from first principles. After exposure to 15 and 25 mg/L Zn(2+) for 6 days, the microalgal consortium reached similar, or higher cell density than the control; ...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5619749</comments>
            <pubDate>Wed, 11 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5619749</guid>        </item>
        <item>
            <title>Tryptophan catabolism via kynurenine production in Streptomyces coelicolor: identification of three genes coding for the enzymes of tryptophan to anthranilate pathway.</title>
            <link>http://www.medworm.com/index.php?rid=5619748&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22234533%26dopt%3DAbstract</link>
            <description>In this study, we describe three adjacent genes of S. coelicolor (SCO3644, SCO3645, and SCO3646), demonstrating their involvement in the tryptophan-to-anthranilate pathway: SCO3644 codes for a KFA, SCO3645 for a KYN and SCO3646 for a TDO. Therefore, these genes can be considered as homologous respectively to kynB, kynU, and kynA of other microorganisms and belong to a constitutive catabolic pathway in S. coelicolor, which expression increases during the stationary phase of a culture grown in the presence of tryptophan. Moreover, the S. coelicolor ΔkynU strain, in which SCO3645 gene is deleted, produces higher amounts of CDA compared to the wild-type strain. Overall, these results describe a pathway, which is used by S. coelicolor to catabolize tryptophan and that could be inactivated to i...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5619748</comments>
            <pubDate>Wed, 11 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5619748</guid>        </item>
        <item>
            <title>Improvement of glutathione production by metabolic engineering the sulfate assimilation pathway of Saccharomyces cerevisiae.</title>
            <link>http://www.medworm.com/index.php?rid=5619747&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22234534%26dopt%3DAbstract</link>
            <description>This study showed that the engineering of sulfur metabolism in S. cerevisiae proves more valuable than addition of cysteine as a way to boost GSH production due to the increases in both the intracellular GSH content and the cell growth.
    PMID: 22234534 [PubMed - as supplied by publisher] (Source: Applied Microbiology and Biotechnology)</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5619747</comments>
            <pubDate>Wed, 11 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5619747</guid>        </item>
        <item>
            <title>Biosorption behavior and mechanism of heavy metals by the fruiting body of jelly fungus (Auricularia polytricha) from aqueous solutions.</title>
            <link>http://www.medworm.com/index.php?rid=5619746&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22234535%26dopt%3DAbstract</link>
            <description>Authors: Huang H, Cao L, Wan Y, Zhang R, Wang W
    Abstract
    The aim of this study was to investigate the biosorption characteristics of Cd(2+), Cu(2+), and Pb(2+) by the fruiting body of jelly fungus Auricularia polytricha. Batch experiments were conducted to characterize the kinetics, equilibrium, and mechanisms of the biosorption process. Optimum values of pH 5, biomass dosage 4 g L(-1), and contact time 60 min provided maximum biosorption capacities of A. polytricha for Cd(2+), Cu(2+), and Pb(2+) of 63.3, 73.7, and 221 mg g(-1), respectively. The maximum desorption was achieved using 0.05 mol L(-1) HNO(3) as an elute. The fruiting body was reusable at least for six cycles of operations. The pseudo-second-order model was the best to describe the biosorption processes among ...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5619746</comments>
            <pubDate>Wed, 11 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5619746</guid>        </item>
        <item>
            <title>Fermentative production of isobutene.</title>
            <link>http://www.medworm.com/index.php?rid=5619745&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22234536%26dopt%3DAbstract</link>
            <description>Authors: van Leeuwen BN, van der Wulp AM, Duijnstee I, van Maris AJ, Straathof AJ
    Abstract
    Isobutene (2-methylpropene) is one of those chemicals for which bio-based production might replace the petrochemical production in the future. Currently, more than 10 million metric tons of isobutene are produced on a yearly basis. Even though bio-based production might also be achieved through chemocatalytic or thermochemical methods, this review focuses on fermentative routes from sugars. Although biological isobutene formation is known since the 1970s, extensive metabolic engineering is required to achieve economically viable yields and productivities. Two recent metabolic engineering developments may enable anaerobic production close to the theoretical stoichiometry of 1isobutene + 2CO(2)...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5619745</comments>
            <pubDate>Wed, 11 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5619745</guid>        </item>
        <item>
            <title>Characterization and application of fusidane antibiotic biosynethsis enzyme 3-ketosteroid-∆(1)-dehydrogenase in steroid transformation.</title>
            <link>http://www.medworm.com/index.php?rid=5619744&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22234537%26dopt%3DAbstract</link>
            <description>In this study, a 3-ketosteroid-∆(1)-dehydrogenase (kstD(F)) involved in fusidane antibiotic biosynthesis from Aspergillus fumigatus CICC 40167 was characterized for use in steroid transformation. KstD(F) encodes a polypeptide consisting of 637 amino acid residues. It shows 51% amino acid identity with a kstD from Thermomicrobium roseum DSM 5159. Expression of kstD(F) in Escherichia coli and Pichia pastoris showed that all kstD(F) activity is located in the cytoplasm. This indicates that it is a soluble intracytoplasmic enzyme, unlike most kstDs from bacteria, which are membrane-bound. The expression of kstD(F) was performed in P. pastoris, both intracellularly and extracelluarly. The intracellularly expressed protein displayed good activity in steroid transformation, while the extracellu...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5619744</comments>
            <pubDate>Wed, 11 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5619744</guid>        </item>
        <item>
            <title>Efficient biocatalyst for large-scale synthesis of cephalosporins, obtained by combining immobilization and site-directed mutagenesis of penicillin acylase.</title>
            <link>http://www.medworm.com/index.php?rid=5577589&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22228258%26dopt%3DAbstract</link>
            <description>We describe the rational design of a new efficient biocatalyst and the development of a sustainable green process for the synthesis of cephalosporins bearing a NH(2) group on the acyl side chain. The new biocatalyst was developed starting from the WT penicillin acylase (PA) from Escherichia coli by combining enzyme mutagenesis, in position α146 and β24 (βF24A/αF146Y), and immobilization on an appropriate modified industrial support, glyoxyl Eupergit C250L. The obtained derivative was used in the kinetically controlled synthesis of cephalexin, cefprozil and cefaclor and compared to the WT-PA and an already described mutant, PA-βF24A, with improved properties. The new biocatalyst posses a very high ratio between the rates of the synthesis and two undesired hydrolyses (acylating ester an...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5577589</comments>
            <pubDate>Sun, 08 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5577589</guid>        </item>
        <item>
            <title>Engineering Corynebacterium glutamicum for the production of pyruvate.</title>
            <link>http://www.medworm.com/index.php?rid=5577586&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22228312%26dopt%3DAbstract</link>
            <description>Authors: Wieschalka S, Blombach B, Eikmanns BJ
    Abstract
    A Corynebacterium glutamicum strain with inactivated pyruvate dehydrogenase complex and a deletion of the gene encoding the pyruvate:quinone oxidoreductase produces about 19 mM L: -valine, 28 mM L: -alanine and about 55 mM pyruvate from 150 mM glucose. Based on this double mutant C. glutamicum △aceE △pqo, we engineered C. glutamicum for efficient production of pyruvate from glucose by additional deletion of the ldhA gene encoding NAD(+)-dependent L: -lactate dehydrogenase (LdhA) and introduction of a attenuated variant of the acetohydroxyacid synthase (△C-T IlvN). The latter modification abolished overflow metabolism towards L: -valine and shifted the product spectrum to pyruvate production. In shake flasks, the resu...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5577586</comments>
            <pubDate>Sun, 08 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5577586</guid>        </item>
        <item>
            <title>Silica gel-encapsulated AtzA biocatalyst for atrazine biodegradation.</title>
            <link>http://www.medworm.com/index.php?rid=5577588&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22228259%26dopt%3DAbstract</link>
            <description>Authors: Reátegui E, Reynolds E, Kasinkas L, Aggarwal A, Sadowsky MJ, Aksan A, Wackett LP
    Abstract
    Encapsulation of recombinant Escherichia coli cells expressing a biocatalyst has the potential to produce stable, long-lasting enzyme activity that can be used for numerous applications. The current study describes the use of this technology with recombinant E. coli cells expressing the atrazine-dechlorinating enzyme AtzA in a silica/polymer porous gel. This novel recombinant enzyme-based method utilizes both adsorption and degradation to remove atrazine from water. A combination of silica nanoparticles (Ludox TM40), alkoxides, and an organic polymer was used to synthesize a porous gel. Gel curing temperatures of 23 or 45 °C were used either to maintain cell viability or to render ...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5577588</comments>
            <pubDate>Sat, 07 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5577588</guid>        </item>
        <item>
            <title>Perstraction of intracellular pigments by submerged cultivation of Monascus in nonionic surfactant micelle aqueous solution.</title>
            <link>http://www.medworm.com/index.php?rid=5577587&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22228260%26dopt%3DAbstract</link>
            <description>Authors: Hu Z, Zhang X, Wu Z, Qi H, Wang Z
    Abstract
    &quot;Milking processing&quot; describes the cultivation of microalgae in a water-organic solvent two-phase system that consists of simultaneous fermentation and secretion of intracellular product. It is usually limited by the conflict between the biocompatibility of the organic solvent to the microorganisms and the ability of the organic solvent to secret intracellular product into its extracellular broth. In the present work, submerged cultivation of Monascus in the nonionic surfactant Triton X-100 micelle aqueous solution for pigment production is exploited, in which the fungus Monascus remains actively growing. Permeabilization of intracellular pigments across the cell membrane and extraction of the pigments to the nonionic surfactant m...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5577587</comments>
            <pubDate>Sat, 07 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5577587</guid>        </item>
        <item>
            <title>CYP264B1 from Sorangium cellulosum So ce56: a fascinating norisoprenoid and sesquiterpene hydroxylase.</title>
            <link>http://www.medworm.com/index.php?rid=5577593&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22223101%26dopt%3DAbstract</link>
            <description>We report here the characterization of CYP264B1 from Sorangium cellulosum So ce56 as a novel sesquiterpene hydroxylase. CYP264B1 was able to convert various sesquiterpenes including nootkatone and norisoprenoids (α-ionone and β-ionone). Nootkatone, an important grapefruit aromatic sesquiterpenoid, was hydroxylated mainly at position C-13. The product has been shown to have the highest antiproliferative activity compared with other nootkatone derivatives. In addition, CYP264B1 was found to hydroxylate α- and β-ionone, important aroma compounds of floral scents, regioselectively at position C-3. The products, 3-hydroxy-β-ionone and 13-hydroxy-nootkatone, were confirmed by (1)H and (13)C NMR. The kinetics of the product formation was analyzed by high-performance liquid chromatography, an...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5577593</comments>
            <pubDate>Fri, 06 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5577593</guid>        </item>
        <item>
            <title>Modification of the TRX2 gene dose in Saccharomyces cerevisiae affects hexokinase 2 gene regulation during wine yeast biomass production.</title>
            <link>http://www.medworm.com/index.php?rid=5577592&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22223102%26dopt%3DAbstract</link>
            <description>Authors: Gómez-Pastor R, Pérez-Torrado R, Matallana E
    Abstract
    In the industrial yeast biomass production process, cells undergo an oxidative and other stresses which worsen the quality of the produced biomass. The overexpression of the thioredoxin codifying gene TRX2 in a wine Saccharomyces cerevisiae strain increases resistance to oxidative stress and industrial biomass production yield. We observed that variations in the TRX2 gene dose in wine yeast strains are relevant to determine the fermentative capacity throughout the industrial biomass production process. So, we studied the molecular changes using a transcriptomic approach under these conditions. The results provide an overview of the different metabolic pathways affected during industrial biomass production by TRX2 gene...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5577592</comments>
            <pubDate>Fri, 06 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5577592</guid>        </item>
        <item>
            <title>Characterization of the mitochondrial NAD(+)-dependent isocitrate dehydrogenase of the oleaginous yeast Rhodosporidium toruloides.</title>
            <link>http://www.medworm.com/index.php?rid=5577591&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22223103%26dopt%3DAbstract</link>
            <description>Authors: Yang F, Zhang S, Zhou YJ, Zhu Z, Lin X, Zhao ZK
    Abstract
    Early biochemical studies have demonstrated that lipid accumulation by oleaginous yeasts is linked to the activity of the NAD(+)-dependent isocitrate dehydrogenase (Idh). However, molecular study of Idh of oleaginous microorganisms remains limited. Here, we present the cloning of a mitochondrial NAD(+)-specific Idh from Rhodosporidium toruloides (RtIdh), an excellent microbial lipid producer that uses carbohydrates as the carbon source. The evolutionary relationship analyses among RtIdhs and other yeast Idhs revealed that RtIdh had a closer relationship with the Idhs of Ustilago maydis and Schizophyllum commune. We expressed the RtIDH gene in the yeast Saccharomyces cerevisiae idhΔ mutant. Under the nitrogen-limited...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5577591</comments>
            <pubDate>Fri, 06 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5577591</guid>        </item>
        <item>
            <title>Enhanced electrode-reducing rate during the enrichment process in an air-cathode microbial fuel cell.</title>
            <link>http://www.medworm.com/index.php?rid=5577590&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22223104%26dopt%3DAbstract</link>
            <description>Authors: Ishii S, Logan BE, Sekiguchi Y
    Abstract
    The improvement in electricity generation during the enrichment process of a microbial consortium was analyzed using an air-cathode microbial fuel cell (MFC) repeatedly fed with acetate that was originally inoculated with sludge from an anaerobic digester. The anodic maximum current density produced by the anode biofilm increased from 0.12 mA/cm(2) at day 28 to 1.12 mA/cm(2) at day 105. However, the microbial cell density on the carbon cloth anode increased only three times throughout this same time period from 0.21 to 0.69 mg protein/cm(2), indicating that the biocatalytic activity of the consortium was also enhanced. The microbial activity was calculated to have a per biomass anode-reducing rate of 374 μmol electron g protei...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5577590</comments>
            <pubDate>Fri, 06 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5577590</guid>        </item>
        <item>
            <title>A kinetic modeling for carbon metabolism in sequencing batch reactor under multiple aerobic/anoxic conditions.</title>
            <link>http://www.medworm.com/index.php?rid=5577601&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22218765%26dopt%3DAbstract</link>
            <description>Authors: Fan J, Vanrolleghem PA, Lu S
    Abstract
    In order to further investigate activated sludge system for better carbon metabolism and nitrogen removal with less energy consumption, a new kinetic model was established. The detailed description of the proposed model was introduced for understanding the mechanisms involved in the activated sludge system, especially simultaneous substrate storage and biomass growth (SSSG) processes and soluble microbial product generation. The evaluation of the proposed model was demonstrated by a lab-scale sequencing batch reactor (SBR) operated with three different sets, i.e., aeration/non-aeration (set 1), non-aeration/aeration/non-aeration (set 2), and alternating aeration/non-aeration (set 3) processes. The purpose was to investigate carbon meta...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5577601</comments>
            <pubDate>Thu, 05 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5577601</guid>        </item>
        <item>
            <title>Improving the performance of an end-point PCR assay commonly used for the detection of Bacteroidales pertaining to cow feces.</title>
            <link>http://www.medworm.com/index.php?rid=5577600&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22218766%26dopt%3DAbstract</link>
            <description>Authors: Liu R, Chan CF, Lun CH, Lau SC
    Abstract
    Bacteroidales are normal gut flora of warm-blooded animals. Since each host species carries a different diversity of Bacteroidales, the detection of host-associated gene markers of Bacteroidales has emerged as a promising tool for the tracking of the source of fecal pollution in aquatic ecosystems. To detect cow-associated Bacteroidales, a commonly used method has been an end-point PCR assay with the 16S rRNA genes primers CF128F (cow-associated) and Bac708R (all Bacteroidales). The PCR assay has demonstrated high rates of true-positive detection (i.e., high sensitivity) in all previous studies. However, the assay also had high rates of false-positive detection to the samples of non-target hosts in some cases (i.e., low specificity)....</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5577600</comments>
            <pubDate>Thu, 05 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5577600</guid>        </item>
        <item>
            <title>Expression of a library of fungal β-glucosidases in Saccharomyces cerevisiae for the development of a biomass fermenting strain.</title>
            <link>http://www.medworm.com/index.php?rid=5577599&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22218767%26dopt%3DAbstract</link>
            <description>Authors: Wilde C, Gold ND, Bawa N, Tambor JH, Mougharbel L, Storms R, Martin VJ
    Abstract
    Converting cellulosic biomass to ethanol involves the enzymatic hydrolysis of cellulose and the fermentation of the resulting glucose. The yeast Saccharomyces cerevisiae is naturally ethanologenic, but lacks the enzymes necessary to degrade cellulose to glucose. Towards the goal of engineering S. cerevisiae for hydrolysis of and ethanol production from cellulose, 35 fungal β-glucosidases (BGL) from the BGL1 and BGL5 families were screened for their ability to be functionally expressed and displayed on the cell surface. Activity assays revealed that the BGL families had different substrate specificities, with only the BGL1s displaying activity on their natural substrate, cellobiose. However, gr...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5577599</comments>
            <pubDate>Thu, 05 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5577599</guid>        </item>
        <item>
            <title>Metabolic control of Clostridium thermocellum via inhibition of hydrogenase activity and the glucose transport rate.</title>
            <link>http://www.medworm.com/index.php?rid=5577598&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22218768%26dopt%3DAbstract</link>
            <description>Authors: Li HF, Knutson BL, Nokes SE, Lynn BC, Flythe MD
    Abstract
    Clostridium thermocellum has the ability to catabolize cellulosic biomass into ethanol, but acetic acid, lactic acid, carbon dioxide, and hydrogen gas (H(2)) are also produced. The effect of hydrogenase inhibitors (H(2), carbon monoxide (CO), and methyl viologen) on product selectivity was investigated. The anticipated effect of these hydrogenase inhibitors was to decrease acetate production. However, shifts to ethanol and lactate production are also observed as a function of cultivation conditions. When the sparge gas of cellobiose-limited chemostat cultures was switched from N(2) to H(2), acetate declined, and ethanol production increased 350%. In resting cell suspensions, lactate increased when H(2) or CO was the ...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5577598</comments>
            <pubDate>Thu, 05 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5577598</guid>        </item>
        <item>
            <title>Expanding the set of rhodococcal Baeyer-Villiger monooxygenases by high-throughput cloning, expression and substrate screening.</title>
            <link>http://www.medworm.com/index.php?rid=5577597&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22218769%26dopt%3DAbstract</link>
            <description>This study also sheds light on the catalytic capacity of this large set of BVMOs that is present in this specific actinomycete. Furthermore, a comparative sequence analysis revealed a new BVMO-typifying sequence motif. This motif represents a useful tool for effective future genome mining efforts.
    PMID: 22218769 [PubMed - as supplied by publisher] (Source: Applied Microbiology and Biotechnology)</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5577597</comments>
            <pubDate>Thu, 05 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5577597</guid>        </item>
        <item>
            <title>Microbial and fungal protease inhibitors-current and potential applications.</title>
            <link>http://www.medworm.com/index.php?rid=5577596&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22218770%26dopt%3DAbstract</link>
            <description>Authors: Sabotič J, Kos J
    Abstract
    Proteolytic enzymes play essential metabolic and regulatory functions in many biological processes and also offer a wide range of biotechnological applications. Because of their essential roles, their proteolytic activity needs to be tightly regulated. Therefore, small molecules and proteins that inhibit proteases can be versatile tools in the fields of medicine, agriculture and biotechnology. In medicine, protease inhibitors can be used as diagnostic or therapeutic agents for viral, bacterial, fungal and parasitic diseases as well as for treating cancer and immunological, neurodegenerative and cardiovascular diseases. They can be involved in crop protection against plant pathogens and herbivorous pests as well as against abiotic stress such as d...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5577596</comments>
            <pubDate>Thu, 05 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5577596</guid>        </item>
        <item>
            <title>Simultaneous removal of phosphorus and nitrogen in a sequencing batch biofilm reactor with transgenic bacteria expressing polyphosphate kinase.</title>
            <link>http://www.medworm.com/index.php?rid=5577595&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22218771%26dopt%3DAbstract</link>
            <description>Authors: Du H, Yang L, Wu J, Xiao L, Wang X, Jiang L
    Abstract
    To improve phosphorus removal from wastewater, we constructed a high-phosphate-accumulating microorganism, KTPPK, using Pseudomonas putida KT2440 as a host. The expression plasmid was constructed by inserting and expressing polyphosphate kinase gene (ppk) from Microcystis aeruginosa NIES-843 into broad-host-range plasmid, pBBR1MCS-2. KTPPK was then added to a sequencing batch biofilm reactor (SBBFR) using lava as a biological carrier. The results showed that SBBFR with KTPPK not only efficiently removed COD, NH(3)-N, and NO             (3)                  (-)           -N but also had a high removal capacity for PO             (4)                  (3-)           -P, resulting in a low phosphorus concentration remaining ...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5577595</comments>
            <pubDate>Thu, 05 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5577595</guid>        </item>
        <item>
            <title>The impact of dissolved organic carbon on the spatial variability of methanogenic archaea communities in natural wetland ecosystems across China.</title>
            <link>http://www.medworm.com/index.php?rid=5577594&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22218772%26dopt%3DAbstract</link>
            <description>Authors: Liu D, Ding W, Jia Z, Cai Z
    Abstract
    Significant spatial variation in CH(4) emissions is a well-established feature of natural wetland ecosystems. To understand the key factors affecting CH(4) production, the variation in community structure of methanogenic archaea, in relation to substrate and external environmental influences, was investigated in selected wetlands across China, using denaturing gradient gel electrophoresis. Case study areas were the subtropical Poyang wetland, the warm-temperate Hongze wetland, the cold-temperate Sanjiang marshes, and the alpine Ruoergai peatland on the Qinghai-Tibetan Plateau. The topsoil layer in the Hongze wetland exhibited the highest population of methanogens; the lowest was found in the Poyang wetland. Maximum CH(4) production occu...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5577594</comments>
            <pubDate>Thu, 05 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5577594</guid>        </item>
        <item>
            <title>Internal loop photobiodegradation reactor (ILPBR) for accelerated degradation of sulfamethoxazole (SMX).</title>
            <link>http://www.medworm.com/index.php?rid=5577604&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22215070%26dopt%3DAbstract</link>
            <description>Authors: Yan N, Xia S, Xu L, Zhu J, Zhang Y, Rittmann BE
    Abstract
    The internal loop photobiodegradation reactor (ILPBR) was evaluated for the degradation of the pharmaceutical sulfamethoxazole (SMX) using batch experiments following three protocols: photolysis alone (P), biodegradation alone (B), and intimately coupled photolysis and biodegradation (P&amp;B). SMX was removed more rapidly by P&amp;B than by either P or B alone, and the corresponding dissolved organic carbon (DOC) removals by P&amp;B also were higher. The faster SMX removal probably was due to a synergy between photolysis and the rapid biodegradation of SMX by the biofilm. The greater DOC removal was brought about by the presence of biofilm bacteria able to biodegrade photolysis products. Ammonium N released during p...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5577604</comments>
            <pubDate>Wed, 04 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5577604</guid>        </item>
        <item>
            <title>Directed evolution and structural prediction of cellobiohydrolase II from the thermophilic fungus Chaetomium thermophilum.</title>
            <link>http://www.medworm.com/index.php?rid=5577603&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22215071%26dopt%3DAbstract</link>
            <description>In this study, the wild-type cbh2 gene of the thermophilic fungus Chaetomium thermophilum encoding cellobiohydrolase II (CBHII) was mutagenized through in vitro directed evolution. The resulting Pichia pastoris yeast library was screened, and two transformants were selected for enhanced CBHII activities that were not attributed to increased gene copy numbers. The optimum fermentation times of the two mutant transformants were shortened to 4-5 days after methanol induction compared to 6 days for the wild-type. The optimum reaction temperature (60 °C) and pH level (5 or 6) of the mutant CBHII proteins, designated CBHIIX16 and CBHIIX305, were higher than those of wild-type CBHII (50 °C and pH 4). Kept at 80 °C for 1 h, CBHIIX16 and CBHIIX305 retained &amp;gt;50% of their activities, whil...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5577603</comments>
            <pubDate>Wed, 04 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5577603</guid>        </item>
        <item>
            <title>Aerobic bioreduction of nickel(II) to elemental nickel with concomitant biomineralization.</title>
            <link>http://www.medworm.com/index.php?rid=5577602&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22215072%26dopt%3DAbstract</link>
            <description>Authors: Zhan G, Li D, Zhang L
    Abstract
    Although microorganisms have the potential to reduce metals, products with elementary forms are unusual. In the present study, a strain of Pseudomonas sp. MBR was tested for its ability to reduce metal ions to their elementary forms coupled to biomineralization under aerobic conditions. The Pseudomonas sp. MBR strain was able to reduce metals such as Fe(III), Mn(II), Cu(II), Ni(II), Cd(II), Co(II), Al(III), Se(IV), and Te(IV) as electron acceptors to elementary forms using citrate, lactate, pyruvate, succinate, malate, glucose, or ethanol as electron donors. Growth and reduction during biomineralization occurred within the pH range of 6.0 to 11.0 and temperature range of 4 to 40 °C, with an optimum growth temperature of 28 °C. The resista...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5577602</comments>
            <pubDate>Wed, 04 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5577602</guid>        </item>
        <item>
            <title>Overexpression of the PHO84 gene causes heavy metal accumulation and induces Ire1p-dependent unfolded protein response in Saccharomyces cerevisiae cells.</title>
            <link>http://www.medworm.com/index.php?rid=5559040&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22207212%26dopt%3DAbstract</link>
            <description>Authors: Ofiteru AM, Ruta LL, Rotaru C, Dumitru I, Ene CD, Neagoe A, Farcasanu IC
    Abstract
    Pho84p, the protein responsible for the high-affinity uptake and transport of inorganic phosphate across the plasma membrane, is also involved in the low-affinity uptake of heavy metals in the Saccharomyces cerevisiae cells. In the present study, the effect of PHO84 overexpression upon the heavy metal accumulation by yeast cells was investigated. As PHO84 overexpression triggered the Ire1p-dependent unfolded protein response, abundant plasma membrane Pho84p could be achieved only in ire1Δ cells. Under environmental surplus, PHO84 overexpression augmented the metal accumulation by the wild type, accumulation that was exacerbated by the IRE1 deletion. The pmr1Δ cells, lacking the gene that en...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5559040</comments>
            <pubDate>Fri, 30 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5559040</guid>        </item>
        <item>
            <title>Selection of a whole-cell biocatalyst for methyl parathion biodegradation.</title>
            <link>http://www.medworm.com/index.php?rid=5559039&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22207213%26dopt%3DAbstract</link>
            <description>Authors: Yang J, Liu R, Jiang H, Yang Y, Qiao C
    Abstract
    Whole-cell biocatalyst has the potential to become a cost-effective alternative to conventional enzyme methods for solving ecological and energy issues. However, cytosolic-expressing biocatalyst systems are critically disadvantaged due to the low permeability of the cell membrane. To overcome substrate transport barrier, periplasmic secretion and surface display biocatalysts were developed by expressing signal peptides or anchor proteins in Escherichia coli. In this work, six carriers were compared in regard to whole-cell activity of methyl parathion hydrolase (MPH). Our results indicate that the surface display systems yielded one to three times whole-cell activity than the periplasmic secretion systems. Although periplasmic...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5559039</comments>
            <pubDate>Fri, 30 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5559039</guid>        </item>
        <item>
            <title>Production of bioactive, SUMO-modified, and native-like TNF-α of the rhesus monkey, Macaca mulatta, in Escherichia coli.</title>
            <link>http://www.medworm.com/index.php?rid=5559038&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22207214%26dopt%3DAbstract</link>
            <description>Authors: Jia D, Yang H, Wan L, Cheng J, Lu X
    Abstract
    Biotechnologically produced tumor necrosis factor alpha (TNF-α) neutralizing agents have proven efficient in patients suffering from disparate autoimmune diseases. The rhesus monkey (Macaca mulatta) could be developed as a model for human autoimmune disease. Consequently, a large amount of M. mulatta TNF-α (mmTNFα) is required to further understand TNF-α-related pathogenesis and evaluate novel human TNF-α (hTNFα) neutralizing agents. We therefore attempted to express mmTNFα by using a small ubiquitin-like modifier (SUMO) fusion system. The synthetic gene, encoding the fusion protein SUMO-mmTNFα, was inserted into a pQE30 plasmid and was transformed into Escherichia coli M15. The fusion protein was expressed as both solub...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5559038</comments>
            <pubDate>Fri, 30 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5559038</guid>        </item>
        <item>
            <title>An ELISA based on the repeated foot-and-mouth disease virus 3B epitope peptide can distinguish infected and vaccinated cattle.</title>
            <link>http://www.medworm.com/index.php?rid=5559037&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22207215%26dopt%3DAbstract</link>
            <description>Authors: Gao M, Zhang R, Li M, Li S, Cao Y, Ma B, Wang J
    Abstract
    To develop a strategy of differentiating infected from vaccinated animals (DIVA) with foot-and-mouth disease virus (FMDV), a short (27aa) peptide containing three conserved linear B cell epitopes of the FMDV 3B nonstructural protein was designed. This novel BF peptide was synthesized using a gene splicing by overlap extension protocol with preferred codons for Escherichia coli. The resultant eight tandem repeat multimer (1, 2, 4, 6, 8, 16, 24, and 32BF) were expressed as soluble fusion proteins in E. coli. An indirect ELISA was developed based on the recombinant 8BF protein with the aim of specifically distinguishing antibodies induced by FMDV infection but not those induced by vaccination. Using the cut-off value of...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5559037</comments>
            <pubDate>Fri, 30 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5559037</guid>        </item>
        <item>
            <title>Genes involved in alkane degradation in the Alcanivorax hongdengensis strain A-11-3.</title>
            <link>http://www.medworm.com/index.php?rid=5559036&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22207216%26dopt%3DAbstract</link>
            <description>Authors: Wang W, Shao Z
    Abstract
    Alcanivorax hongdengensis A-11-3 is a newly identified type strain isolated from the surface water of the Malacca and Singapore Straits that can degrade a wide range of alkanes. To understand the degradation mechanism of this strain, the genes encoding alkane hydroxylases were obtained by PCR screening and shotgun sequencing of a genomic fosmid library. Six genes involved in alkane degradation were found, including alkB1, alkB2, p450-1, p450-2, p450-3 and almA. Heterogeneous expression analysis confirmed their functions as alkane oxidases in Pseudomonas putida GPo12 (pGEc47ΔB) or Pseudomonas fluorescens KOB2Δ1. Q-PCR revealed that the transcription of alkB1 and alkB2 was enhanced in the presence of n-alkanes C(12) to C(24); three p450 genes were u...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5559036</comments>
            <pubDate>Fri, 30 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5559036</guid>        </item>
        <item>
            <title>Performances of two biotrickling filters in treating H(2)S-containing waste gases and analysis of corresponding bacterial communities by pyrosequencing.</title>
            <link>http://www.medworm.com/index.php?rid=5559035&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22207217%26dopt%3DAbstract</link>
            <description>Authors: Li J, Ye G, Sun D, Sun G, Zeng X, Xu J, Liang S
    Abstract
    Two identical biotrickling filters named BTFa and BTFb were run in parallel to examine their performances in removing hydrogen sulfide. BTFa was filled with ceramic granules, and BTFb was filled with volcanic rocks. The results showed that BTFb was more robust than BTFa under acidic conditions. At empty bed residence times (EBRTs) of 20 and 15 s, the removal efficiency of BTFa was close to 100%. At EBRTs of 10 and 5 s, the removal efficiency of BTFa slightly decreased. The removal efficiencies of BTFa decreased by different degrees at the end of each stage, dropping to 94%, 81%, 60%, and 71%, respectively. However, the H(2)S removal efficiency in BTFb consistently reached 99% throughout the experiment. Pyrosequenci...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5559035</comments>
            <pubDate>Fri, 30 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5559035</guid>        </item>
        <item>
            <title>Surface display of monkey metallothionein α tandem repeats and EGFP fusion protein on Pseudomonas putida X4 for biosorption and detection of cadmium.</title>
            <link>http://www.medworm.com/index.php?rid=5559043&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22205441%26dopt%3DAbstract</link>
            <description>Authors: He X, Chen W, Huang Q
    Abstract
    Monkey metallothionein α domain tandem repeats (4mMTα), which exhibit high cadmium affinity, have been displayed for the first time on the surface of a bacterium using ice nucleation protein N-domain (inaXN) protein from the Xanthomonas campestris pv (ACCC-10049) as an anchoring motif. The shuttle vector pIME, which codes for INAXN-4mMTα-EGFP fusion, was constructed and used to target 4mMTα and EGFP on the surface of Pseudomonas putida X4 (CCTCC-209319). The surface location of the INAXN-4mMTα-EGFP fusion was further verified by western blot analysis and immunofluorescence microscopy. The growth of X4 showed resistance to cadmium presence. The presence of surface-exposed 4mMTα on the engineered strains was four times higher than that of...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5559043</comments>
            <pubDate>Thu, 29 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5559043</guid>        </item>
        <item>
            <title>Enhancement of sialylation on humanized IgG-like bispecific antibody by overexpression of α2,6-sialyltransferase derived from Chinese hamster ovary cells.</title>
            <link>http://www.medworm.com/index.php?rid=5559042&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22205442%26dopt%3DAbstract</link>
            <description>Authors: Onitsuka M, Kim WD, Ozaki H, Kawaguchi A, Honda K, Kajiura H, Fujiyama K, Asano R, Kumagai I, Ohtake H, Omasa T
    Abstract
    Improvement of glycosylation is one of the most important topics in the industrial production of therapeutic antibodies. We have focused on terminal sialylation with alpha-2,6 linkage, which is crucial for anti-inflammatory activity. In the present study, we have successfully cloned cDNA of beta-galactosyl alpha-2,6 sialyltransferase (ST6Gal I) derived from Chinese hamster ovary (CHO) cells regardless of reports that stated this was not endogenously expressed in CHO cells. After expressing cloned ST6Gal I in Escherichia coli, the transferase activity was confirmed by HPLC and lectin binding assay. Then, we applied ST6Gal I to alpha-2,6 sialylation of the...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5559042</comments>
            <pubDate>Thu, 29 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5559042</guid>        </item>
        <item>
            <title>Changes in functional diversity of soil microbial community with addition of antibiotics sulfamethoxazole and chlortetracycline.</title>
            <link>http://www.medworm.com/index.php?rid=5559041&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22205443%26dopt%3DAbstract</link>
            <description>Authors: Liu F, Wu J, Ying GG, Luo Z, Feng H
    Abstract
    Potential effects of antibiotics on agricultural soil microflora have recently become increasing concerns with antibiotic-contaminated biosolid now being used in agricultural land. However, changes of soil microbial community function caused by the antibiotic-associated disturbance are less addressed. This paper investigated the changes in microbial functional diversity by spiking sulfamethoxazole (SMX) and chlortetracycline (CTC) in a loam paddy soil and then incubating for 21 days. The dose-effect and time-dependent changes of antibiotic-associated disturbance on soil microbial community were analyzed with the soils sampled at 7 and 21 days using Biolog EcoPlate. At day 7 following treatment, SMX decreased functional diversi...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5559041</comments>
            <pubDate>Thu, 29 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5559041</guid>        </item>
        <item>
            <title>Impact of impurities in biodiesel-derived crude glycerol on the fermentation by Clostridium pasteurianum ATCC 6013.</title>
            <link>http://www.medworm.com/index.php?rid=5559051&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22202963%26dopt%3DAbstract</link>
            <description>In this study, we analyzed the effect of each impurity present in the biodiesel-derived crude glycerol on the growth and metabolism of glycerol by C. pasteurianum. The crude glycerol contains methanol, salts (in the form of potassium chloride or sulfate), and fatty acids that were not transesterified. Salt and methanol were found to have no negative effects on the growth and metabolism of the bacteria on glycerol. The fatty acid with a higher degree of unsaturation, linoleic acid, was found to have strong inhibitory effect on the utilization of glycerol by the bacteria. The fatty acid with lower or no degrees of unsaturation such as stearic and oleic acid were found to be less detrimental to substrate utilization. The removal of fatty acids from crude glycerol by acid precipitation resulte...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5559051</comments>
            <pubDate>Wed, 28 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5559051</guid>        </item>
        <item>
            <title>Enzymatic synthesis of S-adenosylhomocysteine: immobilization of recombinant S-adenosylhomocysteine hydrolase from Corynebacterium glutamicum (ATCC 13032).</title>
            <link>http://www.medworm.com/index.php?rid=5559050&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22202964%26dopt%3DAbstract</link>
            <description>Authors: Lozada-Ramírez JD, Sánchez-Ferrer A, García-Carmona F
    Abstract
    Recombinant S-adenosylhomocysteine hydrolase from Corynebacterium glutamicum (CgSAHase) was covalently bound to Eupergit® C. The maximum yield of bound protein was 91% and the catalytic efficiency was 96.9%. When the kinetic results for the immobilized enzyme were compared with those for the soluble enzyme, no decrease in the catalytic efficiency of the former was detected. Both soluble and immobilized enzymes showed similar optimum pH and temperature ranges. The reuse of immobilized CgSAHase caused a loss of synthetic activity due to NAD(+) release, although the binding to the support was sufficiently strong for up to 5 cycles with 95% conversion efficiency. The immobilized enzyme was incubated every 3 c...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5559050</comments>
            <pubDate>Wed, 28 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5559050</guid>        </item>
        <item>
            <title>Cultivation-independent analysis of archaeal and bacterial communities of the formation water in an Indian coal bed to enhance biotransformation of coal into methane.</title>
            <link>http://www.medworm.com/index.php?rid=5559049&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22202965%26dopt%3DAbstract</link>
            <description>Authors: Singh DN, Kumar A, Sarbhai MP, Tripathi AK
    Abstract
    Biogenic origin of the significant proportion of coal bed methane has indicated the role of microbial communities in methanogenesis. By using cultivation-independent approach, we have analysed the archaeal and bacterial community present in the formation water of an Indian coal bed at 600-700 m depth to understand their role in methanogenesis. Presence of methanogens in the formation water was inferred by epifluorescence microscopy and PCR amplification of mcrA gene. Archaeal 16S rRNA gene clone library from the formation water metagenome was dominated by methanogens showing similarity to Methanobacterium, Methanothermobacter and Methanolinea whereas the clones of bacterial 16S rRNA gene library were closely related to A...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5559049</comments>
            <pubDate>Wed, 28 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5559049</guid>        </item>
        <item>
            <title>Bactericidal activity of Musca domestica cecropin (Mdc) on multidrug-resistant clinical isolate of Escherichia coli.</title>
            <link>http://www.medworm.com/index.php?rid=5559048&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22202966%26dopt%3DAbstract</link>
            <description>Authors: Lu X, Shen J, Jin X, Ma Y, Huang Y, Mei H, Chu F, Zhu J
    Abstract
    The housefly (Musca domestica) larvae have been used clinically to cure osteomyelitis, decubital necrosis, lip boil, ecthyma and malnutritional stagnation ever since the Ming/Qing Dynasty (1368 Anno Domini) till now, in China. In prior research, we have cloned and characterized a new gene of antimicrobial peptide cecropin from M. domestica larvae. This peptide was potently active against Gram-positive and Gram-negative bacteria standard strain. In the present study, we evaluated the possibility of Mdc to be a potential bactericidal agent against clinical isolates of multidrug-resistant (MDR) Escherichia coli and to elucidate the related antimicrobial mechanisms. Antimicrobial activity assays indicated a minim...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5559048</comments>
            <pubDate>Wed, 28 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5559048</guid>        </item>
        <item>
            <title>Stability, oviposition attraction, and larvicidal activity of binary toxin from Bacillus sphaericus expressed in Escherichia coli.</title>
            <link>http://www.medworm.com/index.php?rid=5559047&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22202967%26dopt%3DAbstract</link>
            <description>In this study, the binA and binB genes were cloned and the recombinant BinAB protein was expressed in three strains of Escherichia coli. These recombinant strains were used in a toxicity assay against Culex quinquefasciatus larvae. The highest expression level was achieved when both proteins were expressed in a single operon construct. The BinAB protein expressed in the E. coli Arctic strain showed higher larvicidal activity than either of the recombinant proteins from the E. coli Ril or pLysS strains. Furthermore, it had the highest oviposition attraction (49.1%, P &amp;lt; 0.05). These data suggest that biologically active recombinant BinA and BinB toxins might be useful in mosquito control programs, delivered by inactivated bacterial cells or in traps.
    PMID: 22202967 [PubMed - as su...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5559047</comments>
            <pubDate>Wed, 28 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5559047</guid>        </item>
        <item>
            <title>Quantification and characterization of β-lactam resistance genes in 15 sewage treatment plants from East Asia and North America.</title>
            <link>http://www.medworm.com/index.php?rid=5559046&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22202968%26dopt%3DAbstract</link>
            <description>Authors: Yang Y, Zhang T, Zhang XX, Liang DW, Zhang M, Gao DW, Zhu HG, Huang QG, Fang HH
    Abstract
    The emerging antibiotic resistance genes in the aquatic environment have aroused public concern. As β-lactam is the most widely used group of antibiotics, β-lactam resistance genes were selected to investigate their distribution and diversity in the activated sludge from 15 geographically different sewage treatment plants (STPs) of China, Singapore, USA, and Canada. Specific PCR and quantitative real-time PCR (q-PCR) were used to investigate the occurrence and abundance of nine β-lactam resistance genes. Five genes (OXA-1, OXA-2, OXA-10, ampC, and TEM-1) were detected in most of the sludge collected, while three genes (mecA, CTX-M-1, and SME) were not found in any sludge sample. The...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5559046</comments>
            <pubDate>Wed, 28 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5559046</guid>        </item>
        <item>
            <title>Quercetin treatment changes fluxes in the primary metabolism and increases culture longevity and recombinant α(1)-antitrypsin production in human AGE1.HN cells.</title>
            <link>http://www.medworm.com/index.php?rid=5559045&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22202969%26dopt%3DAbstract</link>
            <description>Authors: Niklas J, Nonnenmacher Y, Rose T, Sandig V, Heinzle E
    Abstract
    Addition of the flavonoid quercetin to cultivations of the α(1)-antitrypsin (A1AT) producing human AGE1.HN.AAT cell line resulted in alterations of the cellular physiology and a remarkable improvement of the overall performance of these cells. In a first screening in 96-well plate format, toxicity and the effect of quercetin on the lactate/glucose ratio was analyzed. It was found that quercetin treatment reduced the lactate/glucose ratio dose dependently. An increase in culture longevity, viable cell density (160% of control), and A1AT concentration (from 0.39 g/L in the control to 0.76 g/L with quercetin, i.e., 195% of the control) was observed in batch cultivation with 10 μM quercetin compared to the con...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5559045</comments>
            <pubDate>Wed, 28 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5559045</guid>        </item>
        <item>
            <title>Plant exudates promote PCB degradation by a rhodococcal rhizobacteria.</title>
            <link>http://www.medworm.com/index.php?rid=5559044&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22202970%26dopt%3DAbstract</link>
            <description>Authors: Toussaint JP, Pham TT, Barriault D, Sylvestre M
    Abstract
    Rhodococcus erythropolis U23A is a polychlorinated biphenyl (PCB)-degrading bacterium isolated from the rhizosphere of plants grown on a PCB-contaminated soil. Strain U23A bphA exhibited 99% identity with bphA1 of Rhodococcus globerulus P6. We grew Arabidopsis thaliana in a hydroponic axenic system, collected, and concentrated the plant secondary metabolite-containing root exudates. Strain U23A exhibited a chemotactic response toward these root exudates. In a root colonizing assay, the number of cells of strain U23A associated to the plant roots (5.7 × 10(5) CFU g(-1)) was greater than the number remaining in the surrounding sand (4.5 × 10(4) CFU g(-1)). Furthermore, the exudates could support the growt...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5559044</comments>
            <pubDate>Wed, 28 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5559044</guid>        </item>
        <item>
            <title>MALDI-TOF MS in microbiological diagnostics-identification of microorganisms and beyond (mini review).</title>
            <link>http://www.medworm.com/index.php?rid=5546648&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22198716%26dopt%3DAbstract</link>
            <description>Authors: Wieser A, Schneider L, Jung J, Schubert S
    Abstract
    Few developments in microbiological diagnostics have had such a rapid impact on species level identification of microorganisms as matrix-assisted laser desorption/ionization time of flight mass spectrometry (MALDI-TOF MS). Conventional differentiation methods rely on biochemical criteria and require additional pre-testing and lengthy incubation procedures. In comparison, MALDI-TOF MS can identify bacteria and yeast within minutes directly from colonies grown on culture plates. This radically new, methodically simple approach profoundly reduces the cost of consumables and time spent on diagnostics. The reliability and accuracy of the method have been demonstrated in numerous studies and different systems are already commerc...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5546648</comments>
            <pubDate>Sun, 25 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5546648</guid>        </item>
        <item>
            <title>In search of sustainable chemical processes: cloning, recombinant expression, and functional characterization of the 7α- and 7β-hydroxysteroid dehydrogenases from Clostridium absonum.</title>
            <link>http://www.medworm.com/index.php?rid=5546647&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22198717%26dopt%3DAbstract</link>
            <description>Authors: Ferrandi EE, Bertolesi GM, Polentini F, Negri A, Riva S, Monti D
    Abstract
    Nicotinamide adenine dinucleotide phosphate-dependent 7α-hydroxysteroid dehydrogenase (7α-HSDH) and 7β-hydroxysteroid dehydrogenases (7β-HSDH) from Clostridium absonum catalyze the epimerization of primary bile acids through 7-keto bile acid intermediates and may be suitable as biocatalysts for the synthesis of bile acids derivatives of pharmacological interest. C. absonum 7α-HSDH has been purified to homogeneity and the N-terminal sequence has been determined by Edman sequencing. After PCR amplifications of a gene fragment with degenerate primers, cloning of the complete gene (786 nt) has been achieved by sequencing of C. absonum genomic DNA. The sequence coding for the 7β-HSDH (783 nt) has ...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5546647</comments>
            <pubDate>Sun, 25 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5546647</guid>        </item>
        <item>
            <title>Characterization of a thermostable β-glucuronidase from Thermotoga maritima expressed in Arabidopsis thaliana.</title>
            <link>http://www.medworm.com/index.php?rid=5546646&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22198718%26dopt%3DAbstract</link>
            <description>Authors: Xu J, Tian YS, Peng RH, Zhu B, Gao JJ, Yao QH
    Abstract
    TmGUSI, a gene identical to that encoding a thermostable β-glucuronidase in the hyperthermophilic anaerobe Thermotoga maritima, has been synthesized using a PCR-based two-step DNA synthesis and codon optimization for plants, and expressed in both Escherichia coli and Arabidopsis thaliana. TmGUSI expressed in transformed E. coli cells exhibited maximum hydrolytic activity at 65 °C and pH 6.5 and retained more than 80% activity after incubation at 85 °C for 30 min. TmGUSI activity in transgenic A. thaliana plants containing TmGUSI was also stable over the temperature range 65-80 °C. Our data suggest that β-glucuronidase from T. maritima can serve as a useful thermostable marker in higher plants.
    PMID: 221987...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5546646</comments>
            <pubDate>Sat, 24 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5546646</guid>        </item>
        <item>
            <title>Synthesis of heparosan oligosaccharides by Pasteurella multocida PmHS2 single-action transferases.</title>
            <link>http://www.medworm.com/index.php?rid=5546610&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22198719%26dopt%3DAbstract</link>
            <description>Authors: Chavaroche AA, van den Broek LA, Boeriu C, Eggink G
    Abstract
    Pasteurella multocida heparosan synthase PmHS2 is a dual action glycosyltransferase that catalyzes the polymerization of heparosan polymers in a non-processive manner. The two PmHS2 single-action transferases, obtained previously by site-directed mutagenesis, have been immobilized on Ni(II)-nitrilotriacetic acid agarose during the purification step. A detailed study of the polymerization process in the presence of non-equal amounts of PmHS2 single-action transferases revealed that the glucuronyl transferase (PmHS2-GlcUA(+)) is the limiting catalyst in the polymerization process. Using experimental design, it was determined that the N-acetylglucosaminyl transferase (PmHS2-GlcNAc(+)) plays an important role in the ...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5546610</comments>
            <pubDate>Sat, 24 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5546610</guid>        </item>
        <item>
            <title>A novel high-throughput B1H-ChIP method for efficiently validating and screening specific regulator-target promoter interactions.</title>
            <link>http://www.medworm.com/index.php?rid=5546656&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22189860%26dopt%3DAbstract</link>
            <description>In this study, we integrated bacterial one-hybrid technique (B1H) with classical chromatin immunoprecipitation (ChIP) assay to develop an innovative B1H-ChIP method, which has the advantages of being high-throughput, low cost, and easy-to-perform. Using this method, we validated two pairs of previously reported PDIs and further successfully discovered five novel target genes for Mce2R and four novel regulators of the gene dnaA in the human pathogen Mycobacterium tuberculosis. New PDI data suggest that Mce2R may play novel roles in the regulation of multi-drug resistance, cell wall synthesis, and intracellular growth of M. tuberculosis, and there exists a probable selective regulation of dnaA under different host conditions. Our findings provide important new information for understanding u...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5546656</comments>
            <pubDate>Thu, 22 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5546656</guid>        </item>
        <item>
            <title>Ixr1p and the control of the Saccharomyces cerevisiae hypoxic response.</title>
            <link>http://www.medworm.com/index.php?rid=5546655&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22189861%26dopt%3DAbstract</link>
            <description>Authors: Vizoso-Vázquez A, Lamas-Maceiras M, Becerra M, González-Siso MI, Rodríguez-Belmonte E, Cerdán ME
    Abstract
    In Saccharomyces cerevisiae, adaptation to hypoxia/anaerobiosis requires the transcriptional induction or derepression of multiple genes organized in regulons controlled by specific transcriptional regulators. Ixr1p is a transcriptional regulatory factor that causes aerobic repression of several hypoxic genes (COX5B, TIR1, and HEM13) and also the activation of HEM13 during hypoxic growth. Analysis of the transcriptome of the wild-type strain BY4741 and its isogenic derivative Δixr1, grown in aerobic and hypoxic conditions, reveals differential regulation of genes related not only to the hypoxic and oxidative stress responses but also to the re-adaptation of catabo...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5546655</comments>
            <pubDate>Thu, 22 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5546655</guid>        </item>
        <item>
            <title>Regio- and enantio-selective glycosylation of tetrahydroprotoberberines by Gliocladium deliquescens NRRL1086 resulting in unique alkaloidal glycosides.</title>
            <link>http://www.medworm.com/index.php?rid=5546654&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22189862%26dopt%3DAbstract</link>
            <description>Authors: Ge HX, Zhang J, Kai C, Liu JH, Yu BY
    Abstract
    The microbial transformation of a series of tetrahydroprotoberberines (THPBs, 1-5) by Gliocladium deliquescens NRRL1086 was investigated. In this research, the novel glycosylation of tetrahydroberberrubine (1) was observed with fast rate and high regio- and enantio-selectivity. One pair of unique enantiomorphic alkaloidal glycosides T-1 and T-2 was isolated and their structures were elucidated unambiguously by HR-MS, CD, 1D and 2D NMR spectrum. It is interesting that different amounts of glucose in the potato broth medium could influence the ratio of T-1 and T-2; in the 1.5% glucose medium, the ratio was about 15:1 and the yield of the S-form product T-1 may reach the theoretical maximum yield of about 50% which could provide o...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5546654</comments>
            <pubDate>Thu, 22 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5546654</guid>        </item>
        <item>
            <title>Culture-independent methods for studying environmental microorganisms: methods, application, and perspective.</title>
            <link>http://www.medworm.com/index.php?rid=5546653&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22189863%26dopt%3DAbstract</link>
            <description>Authors: Su C, Lei L, Duan Y, Zhang KQ, Yang J
    Abstract
    Since the application of molecular methods, culture-independent methods (CIMs) have been developed to study microbial communities from various environments. In the past 20 years, several methods based on the direct amplification and analyses of the small subunit ribosomal RNA gene have been developed to directly study environmental microorganisms. These methods include denaturing/temperature gradient gel electrophoresis, single-strand-conformation polymorphism, restriction fragment length polymorphism, terminal restriction fragment length polymorphism, and quantitative polymerase chain reaction (PCR). Similarly, non-PCR-based molecular techniques, such as microarray and fluorescence in situ hybridization have also been adopte...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5546653</comments>
            <pubDate>Thu, 22 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5546653</guid>        </item>
        <item>
            <title>The great screen anomaly-a new frontier in product discovery through functional metagenomics.</title>
            <link>http://www.medworm.com/index.php?rid=5546652&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22189864%26dopt%3DAbstract</link>
            <description>This article is an opinionating review of functional metagenomic screening of natural microbial communities, with a focus on the optimization of new product discovery. It first summarizes current major bottlenecks in functional metagenomics and then provides an overview of the general metagenomic assessment strategies, with a focus on the challenges that are met in the screening for, and selection of, target genes in metagenomic libraries. To identify possible screening limitations, strategies to achieve optimal gene expression are reviewed, examining the molecular events all the way from the transcription level through to the secretion of the target gene product.
    PMID: 22189864 [PubMed - as supplied by publisher] (Source: Applied Microbiology and Biotechnology)</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5546652</comments>
            <pubDate>Thu, 22 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5546652</guid>        </item>
        <item>
            <title>Production of 10-hydroxystearic acid from oleic acid and olive oil hydrolyzate by an oleate hydratase from Lysinibacillus fusiformis.</title>
            <link>http://www.medworm.com/index.php?rid=5546651&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22189865%26dopt%3DAbstract</link>
            <description>Authors: Kim BN, Joo YC, Kim YS, Kim KR, Oh DK
    Abstract
    A recombinant enzyme from Lysinibacillus fusiformis was expressed, purified, and identified as an oleate hydratase because the hydration activity of the enzyme was the highest for oleic acid (with a k           (cat) of 850 min(-1) and a K           (m) of 540 μM), followed by palmitoleic acid, γ-linolenic acid, linoleic acid, myristoleic acid, and α-linolenic acid. The optimal reaction conditions for the enzymatic production of 10-hydroxystearic acid were pH 6.5, 35 °C, 4% (v/v) ethanol, 2,500 U ml(-1) (8.3 mg ml(-1)) of enzyme, and 40 g l(-1) oleic acid. Under these conditions, 40 g l(-1) (142 mM) oleic acid was converted into 40 g l(-1) (133 mM) 10-hydroxystearic acid for 150 min, with a molar yield of 94% a...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5546651</comments>
            <pubDate>Thu, 22 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5546651</guid>        </item>
        <item>
            <title>A novel thermoacidophilic and thermostable endo-β-1,4-glucanase from Phialophora sp. G5: its thermostability influenced by a distinct β-sheet and the carbohydrate-binding module.</title>
            <link>http://www.medworm.com/index.php?rid=5546650&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22189866%26dopt%3DAbstract</link>
            <description>This study presents an excellent endoglucanase with potential use in the bioconversion of lignocellulosic materials and provides good ideas for the improvement of enzyme thermostability.
    PMID: 22189866 [PubMed - as supplied by publisher] (Source: Applied Microbiology and Biotechnology)</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5546650</comments>
            <pubDate>Thu, 22 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5546650</guid>        </item>
        <item>
            <title>Recombinant expression, purification, and antimicrobial activity of a novel hybrid antimicrobial peptide LFT33.</title>
            <link>http://www.medworm.com/index.php?rid=5546649&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22189867%26dopt%3DAbstract</link>
            <description>Authors: Feng X, Liu C, Guo J, Song X, Li J, Xu W, Li Z
    Abstract
    With great therapeutic potential against antibiotic-resistant bacteria, viruses, and even parasites, antimicrobial peptides (AMPs) have received increased interest as pharmaceutical agents in recent years. It is a worthy yet challenging work to carry out the implement and improvement of AMPs production using bioengineering techniques. In the present study, a novel hybrid peptide LFT33 was designed derived from LfcinB and thanatin. The cDNA fragment encoding LFT33 with preferred codons of Escherichia coli was chemically synthesized and ligated into the vector pET32a(+) to express the LFT33 fusion protein. The fusion protein was successfully expressed in soluble form in E. coli induced under optimized conditions. After ...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5546649</comments>
            <pubDate>Thu, 22 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5546649</guid>        </item>
        <item>
            <title>Biochemical and genetic analysis of a cutinase-type polyesterase from a thermophilic Thermobifida alba AHK119.</title>
            <link>http://www.medworm.com/index.php?rid=5531093&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22183084%26dopt%3DAbstract</link>
            <description>Authors: Thumarat U, Nakamura R, Kawabata T, Suzuki H, Kawai F
    Abstract
    Recombinant polyesterase (Est119) from Thermobifida alba AHK119 was purified by two chromatography steps. The final protein was observed as a single band in SDS-PAGE, and the specific activity of Est119 for p-nitrophenyl butyrate was 2.30 u/mg. Purified Est119 was active with aliphatic and aliphatic-co-aromatic polyesters. Kinetic data indicated that p-nitrophenyl butyrate (pNPB) or hexanoate was the best substrate for Est119 among p-nitrophenyl acyl esters. Calcium was required for full activity and thermostability of Est119, which was stable at 50 °C for 16 h. Three-dimensional modeling and biochemical characterization showed that Est119 is a typical cutinase-type enzyme that has the compact ternary struc...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5531093</comments>
            <pubDate>Tue, 20 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5531093</guid>        </item>
        <item>
            <title>Structure, function and selective inhibition of bacterial acetyl-coa carboxylase.</title>
            <link>http://www.medworm.com/index.php?rid=5531092&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22183085%26dopt%3DAbstract</link>
            <description>Authors: Polyak SW, Abell AD, Wilce MC, Zhang L, Booker GW
    Abstract
    Acetyl-CoA carboxylase (ACC) catalyses the first committed step in fatty acid biosynthesis: a metabolic pathway required for several important biological processes including the synthesis and maintenance of cellular membranes. ACC employs a covalently attached biotin moiety to bind a carboxyl anion and then transfer it to acetyl-CoA, yielding malonyl-CoA. These activities occur at two different subsites: the biotin carboxylase (BC) and carboxyltransferase (CT). Structural biology, together with small molecule inhibitor studies, has provided new insights into the molecular mechanisms that govern ACC catalysis, specifically the BC and CT subunits. Here, we review these recent findings and highlight key differences be...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5531092</comments>
            <pubDate>Tue, 20 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5531092</guid>        </item>
        <item>
            <title>Study of the role played by NfsA, NfsB nitroreductase and NemA flavin reductase from Escherichia coli in the conversion of ethyl 2-(2'-nitrophenoxy)acetate to 4-hydroxy-(2H)-1,4-benzoxazin-3(4H)-one (D-DIBOA), a benzohydroxamic acid with interesting biological properties.</title>
            <link>http://www.medworm.com/index.php?rid=5531095&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22173483%26dopt%3DAbstract</link>
            <description>Authors: Valle A, Le Borgne S, Bolívar J, Cabrera G, Cantero D
    Abstract
    Benzohydroxamic acids, such as 4-hydroxy-(2H)-1,4-benzoxazin-3(4H)-one (D-DIBOA), exhibit interesting herbicidal, fungicidal and bactericidal properties. Recently, the chemical synthesis of D-DIBOA has been simplified to only two steps. In a previous paper, we demonstrated that the second step could be replaced by a biotransformation using Escherichia coli to reduce the nitro group of the precursor, ethyl 2-(2'-nitrophenoxy)acetate and obtain D-DIBOA. The NfsA and NfsB nitroreductases and the NemA xenobiotic reductase of E. coli have the capacity to reduce one or two nitro groups from a wide variety of nitroaromatic compounds, which are similar to the precursor. By this reason, we hypothesised that these three...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5531095</comments>
            <pubDate>Sat, 17 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5531095</guid>        </item>
        <item>
            <title>Best practices for fungal germplasm repositories and perspectives on their implementation.</title>
            <link>http://www.medworm.com/index.php?rid=5531094&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22179706%26dopt%3DAbstract</link>
            <description>Authors: Wiest A, Schnittker R, Plamann M, McCluskey K
    Abstract
    In over 50 years, the Fungal Genetics Stock Center has grown to become a world-recognized biological resource center. Along with this growth comes the development and implementation of myriad practices for the management and curation of a diverse collection of filamentous fungi, yeast, and molecular genetic tools for working with the fungi. These practices include techniques for the testing, manipulation, and preservation of individual fungal isolates as well as for processing of thousands of isolates in parallel. In addition to providing accurate record keeping, an electronic managements system allows the observation of trends in strain distribution and in sample characteristics. Because many ex situ fungal germplasm...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5531094</comments>
            <pubDate>Sat, 17 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5531094</guid>        </item>
        <item>
            <title>Synthesis and assembly of fungal melanin.</title>
            <link>http://www.medworm.com/index.php?rid=5531097&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22173481%26dopt%3DAbstract</link>
            <description>Authors: Eisenman HC, Casadevall A
    Abstract
    Melanin is a unique pigment with myriad functions that is found in all biological kingdoms. It is multifunctional, providing defense against environmental stresses such as ultraviolet (UV) light, oxidizing agents and ionizing radiation. Melanin contributes to the ability of fungi to survive in harsh environments. In addition, it plays a role in fungal pathogenesis. Melanin is an amorphous polymer that is produced by one of two synthetic pathways. Fungi may synthesize melanin from endogenous substrate via a 1,8-dihydroxynaphthalene (DHN) intermediate. Alternatively, some fungi produce melanin from L: -3,4-dihydroxyphenylalanine (L: -dopa). The detailed chemical structure of melanin is not known. However, microscopic studies show that it ha...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5531097</comments>
            <pubDate>Fri, 16 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5531097</guid>        </item>
        <item>
            <title>An engineered Escherichia coli having a high intracellular level of ATP and enhanced recombinant protein production.</title>
            <link>http://www.medworm.com/index.php?rid=5531096&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22173482%26dopt%3DAbstract</link>
            <description>Authors: Kim HJ, Kwon YD, Lee SY, Kim P
    Abstract
    Artificial amplification of gluconeogenic phosphoenolpyruvate carboxykinase (PCK) under glycolytic conditions enables Escherichia coli to maintain a greater intracellular ATP concentration during its growth phase. To demonstrate the biotechnological benefit of E. coli harboring a high intracellular ATP concentration, we compared the recombinant protein synthesis of a soluble protein (enhanced green fluorescence protein, GFP) with that of a secretory protein (alkaline protease, AP), under control of the T7 promoter in E. coli BL21(DE3) overexpressing PCK. According to the batch fermentations, the strain overexpressing PCK produced more GFP and AP with a lower increase in biomass than the control strain. In a chemostat culture (D =...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5531096</comments>
            <pubDate>Fri, 16 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5531096</guid>        </item>
        <item>
            <title>Simulated microgravity affects semicarbazide-sensitive amine oxidase expression in recombinant Escherichia coli by HPLC-ESI-QQQ analysis.</title>
            <link>http://www.medworm.com/index.php?rid=5531104&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22170102%26dopt%3DAbstract</link>
            <description>In this study, an SSAO-transformed Escherichia coli BL21 was constructed firstly. Then, a sensitive, selective, and accurate method based on high-performance liquid chromatography electrospray ionization triple quadrupole (HPLC-ESI-QQQ) was developed to determine the amount of SSAO in the E. coli BL21. The limit of detection and limit of quantification were 5.0 and 10 fmol, respectively. Finally, SSAO expression in the recombinant E. coli BL21 was evaluated with various gravity and temperature conditions by HPLC-ESI-QQQ analysis. It is interesting that the tendency in the alteration of SSAO under simulated microgravity showed temperature difference. At 18 °C, the amount of SSAO in the inclusion bodies and soluble fractions under the simulated microgravity increased by 83% and 116%, resp...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5531104</comments>
            <pubDate>Thu, 15 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5531104</guid>        </item>
        <item>
            <title>Evaluation of the toxic effects of arsenite, chromate, cadmium, and copper using a battery of four bioassays.</title>
            <link>http://www.medworm.com/index.php?rid=5531103&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22170103%26dopt%3DAbstract</link>
            <description>Authors: Ko KS, Lee PK, Kong IC
    Abstract
    The sensitivities of four different kinds of bioassays to the toxicities of arsenite, chromate, cadmium, and copper were compared. The different bioassays exhibited different sensitivities, i.e., they responded to different levels of toxicity of each of the different metals. However, with the exception of the α-glucosidase enzyme activity, arsenite was the most toxic compound towards all the tested organisms, exhibiting the highest toxic effect on the seeds of Lactuca, with an EC(50) value of 0.63 mg/L. The sensitivities of Lactuca and Raphanus were greater than the sensitivities of two other kinds of seeds tested. Therefore, these were the seeds appropriate for use in a seed germination assay. A high revertant mutagenic ratio (5:1) of Sal...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5531103</comments>
            <pubDate>Thu, 15 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5531103</guid>        </item>
        <item>
            <title>Conserved and specific responses to hypoxia in Aspergillus oryzae and Aspergillus nidulans determined by comparative transcriptomics.</title>
            <link>http://www.medworm.com/index.php?rid=5531102&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22170104%26dopt%3DAbstract</link>
            <description>Authors: Terabayashi Y, Shimizu M, Kitazume T, Masuo S, Fujii T, Takaya N
    Abstract
    Hypoxia imposes stress on filamentous fungi that require oxygen to proliferate. Global transcription analysis of Aspergillus oryzae grown under hypoxic conditions found that the expression of about 50% of 4,244 affected genes was either induced or repressed more than 2-fold. A comparison of these genes with the hypoxically regulated genes of Aspergillus nidulans based on their predicted amino acid sequences classified them as bi-directional best hit (BBH), one-way best hit (extra homolog, EH), and no-hit (non-syntenic genes, NSG) genes. Clustering analysis of the BBH genes indicated that A. oryzae and A. nidulans down-regulated global translation and transcription under hypoxic conditions, respective...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5531102</comments>
            <pubDate>Thu, 15 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5531102</guid>        </item>
        <item>
            <title>Production, characterisation and immunogenicity of a plant-made Plasmodium antigen-the 19 kDa C-terminal fragment of Plasmodium yoelii merozoite surface protein 1.</title>
            <link>http://www.medworm.com/index.php?rid=5531101&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22170105%26dopt%3DAbstract</link>
            <description>This study adds to an increasing body of research supporting the feasibility of plants as both a factory for the production of malaria antigens, and as a safe and affordable platform for oral delivery of a temperature-stable malaria vaccine.
    PMID: 22170105 [PubMed - as supplied by publisher] (Source: Applied Microbiology and Biotechnology)</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5531101</comments>
            <pubDate>Thu, 15 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5531101</guid>        </item>
        <item>
            <title>Applied modern biotechnology for cultivation of Ganoderma and development of their products.</title>
            <link>http://www.medworm.com/index.php?rid=5531100&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22170106%26dopt%3DAbstract</link>
            <description>This article will expand people's common knowledge on Ganoderma, and provide a beneficial reference for research and industrial production.
    PMID: 22170106 [PubMed - as supplied by publisher] (Source: Applied Microbiology and Biotechnology)</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5531100</comments>
            <pubDate>Thu, 15 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5531100</guid>        </item>
        <item>
            <title>Enhancement of transglutaminase production in Streptomyces mobaraensis as achieved by treatment with excessive MgCl(2).</title>
            <link>http://www.medworm.com/index.php?rid=5531099&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22170107%26dopt%3DAbstract</link>
            <description>In this study, we first tested the capacity for eight different salts as stress-mediated bioprocesses in the production of transglutaminase (TGase). A significant effect on the cell growth and TGase production was obtained with the highest yield of TGase being observed at 96 h of incubation (4.3 U/ml) when the basic medium was supplemented 0.10 M MgCl(2), as opposed to that observed with the basic medium control (2.1 U/ml at 120 h). Data from Western blot assays showed that transformation of pro-TGase to its mature enzyme occurred more rapidly in MgCl(2) medium. Furthermore, total protease, metalloprotease, and serine protease were also synthesized at a faster rate in the medium containing MgCl(2). The results demonstrate that MgCl(2) enhanced the production of key proteases involved ...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5531099</comments>
            <pubDate>Thu, 15 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5531099</guid>        </item>
        <item>
            <title>Enhanced activity of Thermotoga maritima cellulase 12A by mutating a unique surface loop.</title>
            <link>http://www.medworm.com/index.php?rid=5531098&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22170108%26dopt%3DAbstract</link>
            <description>Authors: Cheng YS, Ko TP, Huang JW, Wu TH, Lin CY, Luo W, Li Q, Ma Y, Huang CH, Wang AH, Liu JR, Guo RT
    Abstract
    Cellulase 12A from Thermotoga maritima (TmCel12A) is a hyperthermostable β-1,4-endoglucanase. We recently determined the crystal structures of TmCel12A and its complexes with oligosaccharides. Here, by using site-directed mutagenesis, the role played by Arg60 and Tyr61 in a unique surface loop of TmCel12A was investigated. The results are consistent with the previously observed hydrogen bonding and stacking interactions between these two residues and the substrate. Interestingly, the mutant Y61G had the highest activity when compared with the wild-type enzyme and the other mutants. It also shows a wider range of working temperatures than does the wild type, along with r...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5531098</comments>
            <pubDate>Thu, 15 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5531098</guid>        </item>
        <item>
            <title>Impact of an indigenous microbial enhanced oil recovery field trial on microbial community structure in a high pour-point oil reservoir.</title>
            <link>http://www.medworm.com/index.php?rid=5531124&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22159733%26dopt%3DAbstract</link>
            <description>In this study, monitoring of microbial community displayed a comprehensive alteration of microbial populations during the field trial to remedy the deficiency of culture-dependent monitoring methods. The results would help to develop and apply more MEOR processes.
    PMID: 22159733 [PubMed - as supplied by publisher] (Source: Applied Microbiology and Biotechnology)</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5531124</comments>
            <pubDate>Tue, 13 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5531124</guid>        </item>
        <item>
            <title>Effects of dissolved organic matter (DOM) at environmentally relevant carbon concentrations on atrazine degradation by Chelatobacter heintzii SalB.</title>
            <link>http://www.medworm.com/index.php?rid=5531123&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22159734%26dopt%3DAbstract</link>
            <description>In conclusion, DOM supplied as both mDOM and eDOM did not inhibit AT degradation at environmentally relevant concentrations, and stimulation can be found for selected DOM samples and this is partly related to its effect on growth.
    PMID: 22159734 [PubMed - as supplied by publisher] (Source: Applied Microbiology and Biotechnology)</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5531123</comments>
            <pubDate>Tue, 13 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5531123</guid>        </item>
        <item>
            <title>Biological synthesis of quercetin 3-O-N-acetylglucosamine conjugate using engineered Escherichia coli expressing UGT78D2.</title>
            <link>http://www.medworm.com/index.php?rid=5531122&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22159735%26dopt%3DAbstract</link>
            <description>Authors: Kim BG, Sung SH, Ahn JH
    Abstract
    Biotransformation of flavonoids using Escherichia coli harboring nucleotide sugar-dependent uridine diphosphate-dependent glycosyltransferases (UGTs) commonly results in the production of a glucose conjugate because most UGTs are specific for UDP-glucose. The Arabidopsis enzyme AtUGT78D2 prefers UDP-glucose as a sugar donor and quercetin as a sugar acceptor. However, in vitro, AtUGT78D2 could use UDP-N-acetylglucosamine as a sugar donor, and whole cell biotransformation of quercetin using E. coli harboring AtUGT78D2 produced quercetin 3-O-N-acetylglucosamine. In order to increase the production of quercetin 3-O-N-acetylglucosamine via biotransformation, two E. coli mutant strains deleted in phosphoglucomutase (pgm) or glucose-1-phosphate ur...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5531122</comments>
            <pubDate>Tue, 13 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5531122</guid>        </item>
        <item>
            <title>Combinatorial modulation of galP and glk gene expression for improved alternative glucose utilization.</title>
            <link>http://www.medworm.com/index.php?rid=5531121&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22159736%26dopt%3DAbstract</link>
            <description>Authors: Lu J, Tang J, Liu Y, Zhu X, Zhang T, Zhang X
    Abstract
    Phosphoenolpyruvate (PEP) is an important precursor for anaerobic production of succinate and malate. Although inactivating PEP/carbohydrate phosphotransferase systems (PTS) could increase PEP supply, the resulting strain had a low glucose utilization rate. In order to improve anaerobic glucose utilization rate for efficient production of succinate and malate, combinatorial modulation of galactose permease (galP) and glucokinase (glk) gene expression was carried out in chromosome of an Escherichia coli strain with inactivated PTS. Libraries of artificial regulatory parts, including promoter and messenger RNA stabilizing region (mRS), were firstly constructed in front of β-galactosidase gene (lacZ) in E. coli chromosome...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5531121</comments>
            <pubDate>Tue, 13 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5531121</guid>        </item>
        <item>
            <title>Polyclonal antibody against conserved sequences of mce1A protein blocks MTB infection in macrophages.</title>
            <link>http://www.medworm.com/index.php?rid=5531120&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22159737%26dopt%3DAbstract</link>
            <description>Authors: Sivagnanam S, Namasivayam N, Chellam R
    Abstract
    The pathogenesis of Mycobacterium tuberculosis is largely due to its ability to enter and survive within human macrophages. It is suggested that a specific protein namely mammalian cell entry protein is involved in the pathogenesis and the specific gene for this protein mce1A has been identified in several pathogenic organisms such as Rickettsia, Shigella, Escherichia coli, Helicobacter, Streptomyces, Klebsiella, Vibrio, Neisseria, Rhodococcus, Nocardioides, Saccharopolyspora erthyrae, and Pseudomonas. Analysis of mce1 operons in the above mentioned organisms through bioinformatics tools has revealed the presence of unique sequences (conserved regions) suggesting that these sequences may be involved in the process of infectio...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5531120</comments>
            <pubDate>Tue, 13 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5531120</guid>        </item>
        <item>
            <title>Assessing the impact of alumina nanoparticles in an anaerobic consortium: methanogenic and humus reducing activity.</title>
            <link>http://www.medworm.com/index.php?rid=5531119&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22159738%26dopt%3DAbstract</link>
            <description>Authors: Alvarez LH, Cervantes FJ
    Abstract
    The impact of γ-Al(2)O(3) nanoparticles (NP) on specific methanogenic activity (SMA) and humus reducing activity (HRA) in an anaerobic consortium was evaluated. SMA in sludge incubations without γ-Al(2)O(3) was always higher compared with those performed in the presence of 100 g/L of γ-Al(2)O(3). Nevertheless, the SMA in incubations with γ-Al(2)O(3) was not completely inhibited, indicating that some methanogenic microorganisms were physiologically active even in the presence of γ-Al(2)O(3) NP during the incubation period (~400 h). SMA and HRA of the anaerobic consortium were also conducted in the presence of γ-Al(2)O(3) NP coated with humic acids (HA). Microbial HA reduction occurred 3.7-fold faster using HA immobilized on γ-Al(2)...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5531119</comments>
            <pubDate>Tue, 13 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5531119</guid>        </item>
        <item>
            <title>SMP production by activated sludge in the presence of a metabolic uncoupler, 3,3',4',5-tetrachlorosalicylanilide (TCS).</title>
            <link>http://www.medworm.com/index.php?rid=5531118&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22159739%26dopt%3DAbstract</link>
            <description>This study might benefit for a better understanding of the response of activated sludge to metabolic uncouplers like TCS.
    PMID: 22159739 [PubMed - as supplied by publisher] (Source: Applied Microbiology and Biotechnology)</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5531118</comments>
            <pubDate>Tue, 13 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5531118</guid>        </item>
        <item>
            <title>Modulation of guanosine nucleotides biosynthetic pathways enhanced GDP-L: -fucose production in recombinant Escherichia coli.</title>
            <link>http://www.medworm.com/index.php?rid=5531117&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22159740%26dopt%3DAbstract</link>
            <description>In this study, improvement of GDP-L: -fucose production was attempted by manipulating the biosynthetic pathway for guanosine nucleotides in recombinant Escherichia coli-producing GDP-L: -fucose. The effects of overexpression of inosine 5'-monophosphate (IMP) dehydrogenase, guanosine 5'-monophosphate (GMP) synthetase (GuaB and GuaA), GMP reductase (GuaC) and guanosine-inosine kinase (Gsk) on GDP-L: -fucose production were investigated in a series of fed-batch fermentations. Among the enzymes tested, overexpression of Gsk led to a significant improvement of GDP-L: -fucose production. Maximum GDP-L: -fucose concentration of 305.5 ± 5.3 mg l(-1) was obtained in the pH-stat fed-batch fermentation of recombinant E. coli-overexpressing Gsk, which corresponds to a 58% enhancement in the GDP...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5531117</comments>
            <pubDate>Tue, 13 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5531117</guid>        </item>
        <item>
            <title>Erratum to: Corynebacterium glutamicum as a potent biocatalyst for the bioconversion of pentose sugars to value-added products.</title>
            <link>http://www.medworm.com/index.php?rid=5531116&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22159741%26dopt%3DAbstract</link>
            <description>Authors: Gopinath V, Murali A, Dhar KS, Nampoothiri KM
    PMID: 22159741 [PubMed - as supplied by publisher] (Source: Applied Microbiology and Biotechnology)</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5531116</comments>
            <pubDate>Tue, 13 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5531116</guid>        </item>
        <item>
            <title>Effects of polysaccharides from Morchella conica on nitric oxide production in lipopolysaccharide-treated macrophages.</title>
            <link>http://www.medworm.com/index.php?rid=5531166&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22159604%26dopt%3DAbstract</link>
            <description>In conclusion, PMCs inhibited NO production in LPS-induced macrophages through regulating a series of signal pathways, suggesting that PMCs play a potential role on immunomodulation and treating related diseases.
    PMID: 22159604 [PubMed - as supplied by publisher] (Source: Applied Microbiology and Biotechnology)</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5531166</comments>
            <pubDate>Sun, 11 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5531166</guid>        </item>
        <item>
            <title>A combined physiological and proteomic approach to reveal lactic-acid-induced alterations in Lactobacillus casei Zhang and its mutant with enhanced lactic acid tolerance.</title>
            <link>http://www.medworm.com/index.php?rid=5531130&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22159611%26dopt%3DAbstract</link>
            <description>Authors: Wu C, Zhang J, Chen W, Wang M, Du G, Chen J
    Abstract
    Lactobacillus casei has traditionally been recognized as a probiotic and frequently used as an adjunct culture in fermented dairy products, where acid stress is an environmental condition commonly encountered. In the present study, we carried out a comparative physiological and proteomic study to investigate lactic-acid-induced alterations in Lactobacillus casei Zhang (WT) and its acid-resistant mutant. Analysis of the physiological data showed that the mutant exhibited 33.8% higher glucose phosphoenolpyruvate:sugar phosphotransferase system activity and lower glycolytic pH compared with the WT under acidic conditions. In addition, significant differences were detected in both cells during acid stress between intracellul...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5531130</comments>
            <pubDate>Sun, 11 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5531130</guid>        </item>
        <item>
            <title>The effect of acetylated xylan and sugar beet pulp on the expression and secretion of enzymes by Penicillium purpurogenum.</title>
            <link>http://www.medworm.com/index.php?rid=5531126&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22159660%26dopt%3DAbstract</link>
            <description>Authors: Navarrete M, Callegari E, Eyzaguirre J
    Abstract
    Sugar beet pulp is a natural carbon source composed mainly of pectin and cellulose, which is utilized and degraded by the ascomycete Penicillium purpurogenum. The fungus also grows on and degrades acetylated xylan which lacks cellulose and pectin. Both carbon sources have been used in our laboratory to grow the fungus and to purify different enzymes secreted to the medium. The enzymes involved in the complex process of degradation of these carbon sources by the fungus have been explored previously under non-denaturing conditions; multienzyme complexes were separated and some subunits identified by Western blots and mass spectrometry. In this work, proteomic profiles show that the secretome is composed of numerous proteins var...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5531126</comments>
            <pubDate>Sun, 11 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5531126</guid>        </item>
        <item>
            <title>Directed evolution of a highly active Yersinia mollaretii phytase.</title>
            <link>http://www.medworm.com/index.php?rid=5531125&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22159661%26dopt%3DAbstract</link>
            <description>In this study, we report the cloning, characterization, and directed evolution of the Yersinia mollaretii phytase (Ymphytase). Ymphytase has a tetrameric structure with positive cooperativity (Hill coefficient was 2.3) and a specific activity of 1,073 U/mg which is ∼10 times higher than widely used fungal phytases. High-throughput prescreening methods using filter papers or 384-well microtiter plates were developed. Precise subsequent screening for thermostable and active phytase variants was performed by combining absorbance and fluorescence-based detection system in 96-well microtiter plates. Directed evolution yielded after mutant library generation (SeSaM method) and two-step screening (in total ∼8,400 clones) a phytase variant with ∼20% improved thermostability (58°C for 20 m...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5531125</comments>
            <pubDate>Sun, 11 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5531125</guid>        </item>
        <item>
            <title>Characterization of a novel ginsenoside-hydrolyzing α-L: -arabinofuranosidase, AbfA, from Rhodanobacter ginsenosidimutans Gsoil 3054(T).</title>
            <link>http://www.medworm.com/index.php?rid=5531170&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22159603%26dopt%3DAbstract</link>
            <description>Authors: An DS, Cui CH, Sung BH, Yang HC, Kim SC, Lee ST, Im WT, Kim SG
    Abstract
    The gene encoding an α-L: -arabinofuranosidase that could biotransform ginsenoside Rc {3-O-[β-D: -glucopyranosyl-(1-2)-β-D: -glucopyranosyl]-20-O-[α-L: -arabinofuranosyl-(1-6)-β-D: -glucopyranosyl]-20(S)-protopanaxadiol} to ginsenoside Rd {3-O-[β-D: -glucopyranosyl-(1-2)-β-D: -glucopyranosyl]-20-O-β-D: -glucopyranosyl-20(S)-protopanaxadiol} was cloned from a soil bacterium, Rhodanobacter ginsenosidimutans strain Gsoil 3054(T), and the recombinant enzyme was characterized. The enzyme (AbfA) hydrolyzed the arabinofuranosyl moiety from ginsenoside Rc and was classified as a family 51 glycoside hydrolase based on amino acid sequence analysis. Recombinant AbfA expressed in Escherichia coli hydrolyze...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5531170</comments>
            <pubDate>Sat, 10 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5531170</guid>        </item>
        <item>
            <title>The complete genome sequence of Pantoea ananatis AJ13355, an organism with great biotechnological potential.</title>
            <link>http://www.medworm.com/index.php?rid=5531157&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22159605%26dopt%3DAbstract</link>
            <description>Authors: Hara Y, Kadotani N, Izui H, Katashkina JI, Kuvaeva TM, Andreeva IG, Golubeva LI, Malko DB, Makeev VJ, Mashko SV, Kozlov YI
    Abstract
    Pantoea ananatis AJ13355 is a newly identified member of the Enterobacteriaceae family with promising biotechnological applications. This bacterium is able to grow at an acidic pH and is resistant to saturating concentrations of L-glutamic acid, making this organism a suitable host for the production of L-glutamate. In the current study, the complete genomic sequence of P. ananatis AJ13355 was determined. The genome was found to consist of a single circular chromosome consisting of 4,555,536 bp [DDBJ: AP012032] and a circular plasmid, pEA320, of 321,744 bp [DDBJ: AP012033]. After automated annotation, 4,071 protein-coding sequences were identi...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5531157</comments>
            <pubDate>Sat, 10 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5531157</guid>        </item>
        <item>
            <title>Comparative metabolomic analysis of Saccharomyces cerevisiae during the degradation of patulin using gas chromatography-mass spectrometry.</title>
            <link>http://www.medworm.com/index.php?rid=5531151&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22159606%26dopt%3DAbstract</link>
            <description>Authors: Shao S, Zhou T, McGarvey BD
    Abstract
    A comparative metabolomic analysis was conducted on Saccharomyces cerevisiae cells with and without patulin treatment using gas chromatography-mass spectrometry-based approach. A total of 72 metabolites were detected and compared, including 16 amino acids, 29 organic acids and alcohols, 19 sugars and sugar alcohols, 2 nucleotides, and 6 miscellaneous compounds. Principle component analysis showed a clear separation of metabolome between the cells with and without patulin treatment, and most of the identified metabolites contributed to the separation. A close examination of the identified metabolites showed an increased level of most of the free amino acids, an increased level of the intermediates in the tricarboxylic acid cycle, a highe...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5531151</comments>
            <pubDate>Sat, 10 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5531151</guid>        </item>
        <item>
            <title>Bioconversion of lignin model compounds with oleaginous Rhodococci.</title>
            <link>http://www.medworm.com/index.php?rid=5531145&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22159607%26dopt%3DAbstract</link>
            <description>Authors: Kosa M, Ragauskas AJ
    Abstract
    Although economically efficient biomass conversion depends on the utilization of the complete cell wall (biorefinery concept), including polysaccharides and lignin, current biofuels research concentrate mostly on cellulose conversion, while lignin is viewed as a side-product that is used primarily as a thermal resource. Microbiological conversion of lignin is almost exclusive to fungi, usually resulting in increased cell mass and lignolytic enzymes. Some bacteria can also degrade lignin-related compounds using the β-ketoadipate pathway; for example, Rhodococcus opacus DSM 1069 can degrade coniferyl alcohol and grow on it as sole carbon source. Moreover, this strain belongs to the actinomycetes group that is also known for oleaginous species w...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5531145</comments>
            <pubDate>Sat, 10 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5531145</guid>        </item>
        <item>
            <title>Novel magnetic microspheres of P (GMA-b-HEMA): preparation, lipase immobilization and enzymatic activity in two phases.</title>
            <link>http://www.medworm.com/index.php?rid=5531141&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22159608%26dopt%3DAbstract</link>
            <description>Authors: Cui Y, Chen X, Li Y, Liu X, Lei L, Xuan S
    Abstract
    Magnetic oleic-acid-coated Fe(3)O(4) nanoparticles were first introduced into 1, 1-diphenylethylene (DPE)-controlled radical polymerization system to prepare superparamagnetic microspheres for enzyme immobilization by two steps of polymerization. In the presence of DPE, glycidyl methacrylate, 2-hydroxyethyl methacrylate and methacryloxyethyl trimethyl ammonium chloride with charge were selected as copolymering monomers based on their reactive functional group and excellent biocompatibility which were suitable for immobilization of Candida rugosa lipase (CRL). The resulting magnetic microspheres were characterized by means of scanning electron microscope, Fourier transform infrared spectrum, thermogravimetric analysis and v...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5531141</comments>
            <pubDate>Sat, 10 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5531141</guid>        </item>
        <item>
            <title>Identification of suitable ionic liquids for application in the enzymatic hydrolysis of rutin by an automated screening.</title>
            <link>http://www.medworm.com/index.php?rid=5531138&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22159609%26dopt%3DAbstract</link>
            <description>Authors: Temme H, Dethloff O, Pitner WR, Fischer S, Scheurich R, Schulte M, Niemeyer B
    Abstract
    An automated method in milliliter scale was developed for the screening of process parameters concerning the hydrolysis of the flavonoid rutin catalyzed by the rhamnosidase activity of naringinase from Penicillium decumbens. Besides the effect of additives such as ionic liquids and low molecular salts, the productivity in a multiple phase system as well as the recyclability of the enzyme in repetitive batches were studied. The hydrophobic ionic liquid (IL) trihexyl(tetradecyl)phosphonium bis(trifluormethylsulfonyl)imide [P(h(3))t][Tf(2)N] was identified to combine the most favorable characteristics out of 23 investigated ILs with regard to enzyme compatibility, substrate solubility and e...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5531138</comments>
            <pubDate>Sat, 10 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5531138</guid>        </item>
        <item>
            <title>A novel single-chain Fv antibody for connective tissue growth factor against the differentiation of fibroblast into myofibroblast.</title>
            <link>http://www.medworm.com/index.php?rid=5531133&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22159610%26dopt%3DAbstract</link>
            <description>This study was aimed to investigate the effect of a single-chain fragment variable antibody of connective tissue growth factor (anti-CTGF scFv) against the differentiation of fibroblast into myofibroblast. The scFv antibody was firstly expressed in Escherichia coli cells and was then purified by affinity chromatography. The yield scFv protein reached a purity over 95% after purification. Immunoreactivity assay demonstrated that scFv possessed a special affinity toward CTGF. RT-PCR, western blot, and immunofluorescence experiments showed that increased expression of α-smooth muscle actin induced by TGF-β1 could be suppressed by this scFv antibody through inhibiting the phosphorylation of Akt.
    PMID: 22159610 [PubMed - as supplied by publisher] (Source: Applied Microbiology and Biotechn...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5531133</comments>
            <pubDate>Sat, 10 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5531133</guid>        </item>
        <item>
            <title>Continuous bio-catalytic conversion of sugar mixture to acetone-butanol-ethanol by immobilized Clostridium acetobutylicum DSM 792.</title>
            <link>http://www.medworm.com/index.php?rid=5531129&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22159612%26dopt%3DAbstract</link>
            <description>We report the best solvent productivity among wild-type strains using column reactor. The maximum total solvent concentration of 14.32 g L(-1) was obtained at a dilution rate of 0.22 h(-1) with glucose as a substrate compared to 12.64 g L(-1) at 0.5 h(-1) dilution rate with sugar mixture. The maximum solvent productivity (13.66 g L(-1) h(-1)) was obtained at a dilution rate of 1.9 h(-1) with glucose as a substrate whereas solvent productivity (12.14 g L(-1) h(-1)) was obtained at a dilution rate of 1.5 h(-1) with sugar mixture. The immobilized column reactor with wood pulp can become an efficient technology to be integrated with existing pulp mills to convert them into wood-based bio-refineries.
    PMID: 22159612 [PubMed - as supplied by publisher] (Source: Applied Micro...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5531129</comments>
            <pubDate>Sat, 10 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5531129</guid>        </item>
        <item>
            <title>Adaptation mechanisms of bacteria during the degradation of polychlorinated biphenyls in the presence of natural and synthetic terpenes as potential degradation inducers.</title>
            <link>http://www.medworm.com/index.php?rid=5531128&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22159613%26dopt%3DAbstract</link>
            <description>In this study, we examined the effect of polychlorinated biphenyls (PCBs) in the presence of natural and synthetic terpenes and biphenyl on biomass production, lipid accumulation, and membrane adaptation mechanisms of two PCB-degrading bacterial strains Pseudomonas stutzeri and Burkholderia xenovorans LB400. According to the results obtained, it could be concluded that natural terpenes, mainly those contained in ivy leaves and pine needles, decreased adaptation responses induced by PCBs in these strains. The adaptation processes under investigation included growth inhibition, lipid accumulation, composition of fatty acids, cis/trans isomerization, and membrane saturation. Growth inhibition effect decreased upon addition of these natural compounds to the medium. The amount of unsaturated fa...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5531128</comments>
            <pubDate>Sat, 10 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5531128</guid>        </item>
        <item>
            <title>Biotin protein ligase from Corynebacterium glutamicum: role for growth and L: -lysine production.</title>
            <link>http://www.medworm.com/index.php?rid=5531127&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22159614%26dopt%3DAbstract</link>
            <description>Authors: Peters-Wendisch P, Stansen KC, Götker S, Wendisch VF
    Abstract
    Corynebacterium glutamicum is a biotin auxotrophic Gram-positive bacterium that is used for large-scale production of amino acids, especially of L: -glutamate and L: -lysine. It is known that biotin limitation triggers L: -glutamate production and that L: -lysine production can be increased by enhancing the activity of pyruvate carboxylase, one of two biotin-dependent proteins of C. glutamicum. The gene cg0814 (accession number YP_225000) has been annotated to code for putative biotin protein ligase BirA, but the protein has not yet been characterized. A discontinuous enzyme assay of biotin protein ligase activity was established using a 105aa peptide corresponding to the carboxyterminus of the biotin carboxyla...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5531127</comments>
            <pubDate>Sat, 10 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5531127</guid>        </item>
        <item>
            <title>Isolation, characterization, and quantification of Clostridium kluyveri from the bovine rumen.</title>
            <link>http://www.medworm.com/index.php?rid=5531113&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22159841%26dopt%3DAbstract</link>
            <description>Authors: Weimer PJ, Stevenson DM
    Abstract
    A strain of Clostridium kluyveri was isolated from the bovine rumen in a medium containing ethanol as an electron donor and acetate and succinate (common products of rumen fermentation) as electron acceptors. The isolate displayed a narrow substrate range but wide temperature and pH ranges atypical of ruminal bacteria and a maximum specific growth rate near the typical liquid dilution rate of the rumen. Quantitative real-time PCR revealed that C. kluyveri was widespread among bovine ruminal samples but was present at only very low levels (0.00002% to 0.0002% of bacterial 16S rRNA gene copy number). However, the species was present in much higher levels (0.26% of bacterial 16S rRNA gene copy number) in lucerne silage (but not maize silage) t...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5531113</comments>
            <pubDate>Fri, 09 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5531113</guid>        </item>
        <item>
            <title>Polyphasic approach for the characterization of rhizobial symbionts effective in fixing N(2) with common bean (Phaseolus vulgaris L.).</title>
            <link>http://www.medworm.com/index.php?rid=5531112&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22159885%26dopt%3DAbstract</link>
            <description>Authors: Cardoso JD, Hungria M, Andrade DS
    Abstract
    Common bean (Phaseolus vulgaris L.) is a legume that has been reported as highly promiscuous in nodulating with a variety of rhizobial strains, often with low effectiveness in fixing nitrogen. The aim of this work was to assess the symbiotic efficiency of rhizobial strains isolated from common bean seeds, nodules of Arachis hypogaea, Mucuna pruriens, and soils from various Brazilian agroecosystems, followed by the characterization of elite strains identified in the first screening. Forty-five elite strains were analyzed for symbiotic properties (nodulation, plant-growth, and nitrogen-fixation parameters) under greenhouse conditions in pots containing non-sterile soil, and variation in symbiotic performance was observed. Elite stra...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5531112</comments>
            <pubDate>Fri, 09 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5531112</guid>        </item>
        <item>
            <title>Synthesis and characterization of the antibacterial potential of ZnO nanoparticles against extended-spectrum β-lactamases-producing Escherichia coli and Klebsiella pneumoniae isolated from a tertiary care hospital of North India.</title>
            <link>http://www.medworm.com/index.php?rid=5531111&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22159886%26dopt%3DAbstract</link>
            <description>Authors: Ansari MA, Khan HM, Khan AA, Sultan A, Azam A
    Abstract
    The reemergence of infectious diseases and the continuous development of multidrug resistance among a variety of disease-causing bacteria in clinical setting pose a serious threat to public health worldwide. Extended-spectrum β-lactamases (ESBLs) that mediate resistance to third-generation cephalosporin are now observed all over the world in all species of Enterobacteriaceae, especially Escherichia coli and Klebsiella pneumoniae. In this work, ZnO nanoparticles (NPs) were synthesized by the sol-gel method and characterized by powder X-ray diffraction, scanning electron microscopy (SEM) and atomic force microscopy (AFM). The image of synthesized ZnO NPs appeared spherical in SEM with a diameter of ≈19 nm and as hexa...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5531111</comments>
            <pubDate>Fri, 09 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5531111</guid>        </item>
        <item>
            <title>Beneficial effects of Lactobacillus paracasei subsp. paracasei NTU 101 and its fermented products.</title>
            <link>http://www.medworm.com/index.php?rid=5531110&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22159887%26dopt%3DAbstract</link>
            <description>Authors: Chiang SS, Pan TM
    Abstract
    It is well-known that probiotics have a number of beneficial health effects in humans and animals, including the reduction of symptoms in lactose intolerance and enhancement of the bioavailability of nutrients. Probiotics have showed to possess antimutagenic, anticarcinogenic and hypocholesterolemic properties. Further, they were also observed to have antagonistic actions against intestinal and food-borne pathogens, to decrease the prevalence of allergies in susceptible individuals and to have immunomodulatory effects. Typically, the bacteria colonise the intestinal tract first and then reinforce the host defence systems by inducing a generalised mucosal immune response, balanced T-helper cell response, self-limited inflammatory response and secr...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5531110</comments>
            <pubDate>Fri, 09 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5531110</guid>        </item>
        <item>
            <title>CHO cells in biotechnology for production of recombinant proteins: current state and further potential.</title>
            <link>http://www.medworm.com/index.php?rid=5531109&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22159888%26dopt%3DAbstract</link>
            <description>Authors: Kim JY, Kim YG, Lee GM
    Abstract
    Recombinant Chinese hamster ovary cells (rCHO) cells have been the most commonly used mammalian host for large-scale commercial production of therapeutic proteins. Recent advances in cell culture technology for rCHO cells have achieved significant improvement in protein production leading to titer of more than 10 g/L to meet the huge demand from market needs. This achievement is associated with progression in the establishment of high and stable producer and the optimization of culture process including media development. In this review article, we focus on current strategies and achievements in cell line development, mainly in vector engineering and cell engineering, for high and stable protein production in rCHO cells. The approaches that...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5531109</comments>
            <pubDate>Fri, 09 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5531109</guid>        </item>
        <item>
            <title>Long-term field fertilization alters the diversity of autotrophic bacteria based on the ribulose-1,5-biphosphate carboxylase/oxygenase (RubisCO) large-subunit genes in paddy soil.</title>
            <link>http://www.medworm.com/index.php?rid=5531108&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22159889%26dopt%3DAbstract</link>
            <description>Authors: Yuan H, Ge T, Wu X, Liu S, Tong C, Qin H, Wu M, Wei W, Wu J
    Abstract
    Carbon dioxide (CO(2)) assimilation by autotrophic bacteria is an important process in the soil carbon cycle with major environmental implications. The long-term impact of fertilizer on CO(2) assimilation in the bacterial community of paddy soils remains poorly understood. To narrow this knowledge gap, the composition and abundance of CO(2)-assimilating bacteria were investigated using terminal restriction fragment length polymorphism and quantitative PCR of the cbbL gene [that encodes ribulose-1,5-biphosphate carboxylase/oxygenase (RubisCO)] in paddy soils. Soils from three stations in subtropical China were used. Each station is part of a long-term fertilization experiment with three treatments: no fert...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5531108</comments>
            <pubDate>Fri, 09 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5531108</guid>        </item>
        <item>
            <title>Construction of new Pichia pastoris X-33 strains for production of lycopene and β-carotene.</title>
            <link>http://www.medworm.com/index.php?rid=5531107&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22159890%26dopt%3DAbstract</link>
            <description>In this study, we used the non-carotenogenic yeast Pichia pastoris X33 as a receptor for β-carotene-encoding genes, in order to obtain new recombinant strains capable of producing different carotenoidic compounds. We designed and constructed two plasmids, pGAPZA-EBI* and pGAPZA-EBI*L*, containing the genes encoding lycopene and β-carotene, respectively. Plasmid pGAPZA-EBI*, expresses three genes, crtE, crtB, and crtI*, that encode three carotenogenic enzymes, geranylgeranyl diphosphate synthase, phytoene synthase, and phytoene desaturase, respectively. The other plasmid, pGAPZA-EBI*L*, carried not only the three genes above mentioned, but also the crtL* gene, that encodes lycopene β-cyclase. The genes crtE, crtB, and crtI were obtained from Erwinia uredovora, whereas crtL* was cloned fr...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5531107</comments>
            <pubDate>Fri, 09 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5531107</guid>        </item>
        <item>
            <title>Chemically inhibited ATP synthesis promoted detachment of different-age biofilms from membrane surface.</title>
            <link>http://www.medworm.com/index.php?rid=5531106&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22159891%26dopt%3DAbstract</link>
            <description>This study investigated the response of different-age biofilms developed on membrane surface to a chemical uncoupler 3, 3', 4', 5-tetrachlorosalicylanilide (TCS). Results showed that adenosine triphosphate (ATP) dissipation caused by TCS would promote different-age biofilms detachment, whereas chemically inhibited cellular ATP synthesis subsequently suppressed autoinducer-2 (AI-2) and extracellular polymeric substances (EPS) production. The extent of biofilm detachment was found to be closely related to AI-2-regulated EPS contents of bacteria. It was revealed that energy dissipation induced biofilm detachability was controlled by AI-2 regulated cellular communication via AI-2-mediated EPS secretion. This study would lead to a new cleaning strategy of biologically fouled membrane.
    PMID:...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5531106</comments>
            <pubDate>Fri, 09 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5531106</guid>        </item>
        <item>
            <title>Evolution and some functions of the NprR-NprRB quorum-sensing system in the Bacillus cereus group.</title>
            <link>http://www.medworm.com/index.php?rid=5531105&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22159892%26dopt%3DAbstract</link>
            <description>Authors: Rocha J, Flores V, Cabrera R, Soto-Guzmán A, Granados G, Juaristi E, Guarneros G, de la Torre M
    Abstract
    Quorum-sensing (QS) is a bacterial mechanism for regulation of gene expression in response to cell density. In Gram-positive bacteria, oligopeptides are the signaling molecules to elicit QS. The RNPP protein family (Rap, NprR, PlcR, and PrgX) are intracellular QS receptors that bind directly to their specific signaling peptide for regulating the transcription of several genes. NprR is the activator of a neutral protease in Bacillus subtilis, and it has been recently related to sporulation, cry genes transcription and extracellular protease activity in strains from the B. cereus group. In the B. thuringiensis genome, downstream nprR, a gene encoding a putative QS signal...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5531105</comments>
            <pubDate>Fri, 09 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5531105</guid>        </item>
        <item>
            <title>A novel thermostable and glucose-tolerant β-glucosidase from Fervidobacterium islandicum.</title>
            <link>http://www.medworm.com/index.php?rid=5492535&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22146852%26dopt%3DAbstract</link>
            <description>Authors: Jabbour D, Klippel B, Antranikian G
    Abstract
    An open reading frame (ORF) encoding the enzyme β-glucosidase from the extremely thermophilic bacterium Fervidobacterium islandicum has been identified, cloned and sequenced. The bgl1A gene was cloned in a pET-Blue1 vector and transformed in Escherichia coli, resulting in high-level expression of β-glucosidase FiBgl1A that was purified to homogeneity in a two-step purification. FiBgl1A is composed of 459 amino acid residues and showed high homology to glycoside hydrolase family 1 proteins. It exhibited highest activity towards p-nitrophenyl-β-D: -glucopyranoside with an optimum activity at pH 6.0 and 7.0 and at 90 °C. The enzyme is resistant to glucose inhibition. Furthermore, it did not require divalent cations for activi...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5492535</comments>
            <pubDate>Thu, 08 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5492535</guid>        </item>
        <item>
            <title>Metagenomic cellulases highly tolerant towards the presence of ionic liquids-linking thermostability and halotolerance.</title>
            <link>http://www.medworm.com/index.php?rid=5492536&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22143172%26dopt%3DAbstract</link>
            <description>Authors: Ilmberger N, Meske D, Juergensen J, Schulte M, Barthen P, Rabausch U, Angelov A, Mientus M, Liebl W, Schmitz RA, Streit WR
    Abstract
    Cellulose is an important renewable resource for the production of bioethanol and other valuable compounds. Several ionic liquids (ILs) have been described to dissolve water-insoluble cellulose and/or wood. Therefore, ILs would provide a suitable reaction medium for the enzymatic hydrolysis of cellulose if cellulases were active and stable in the presence of high IL concentrations. For the discovery of novel bacterial enzymes with elevated stability in ILs, metagenomic libraries from three different hydrolytic communities (i.e. an enrichment culture inoculated with an extract of the shipworm Teredo navalis, a biogas plant sample and elephant f...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5492536</comments>
            <pubDate>Tue, 06 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5492536</guid>        </item>
        <item>
            <title>Effects of different replicons in conjugative plasmids on transformation efficiency, plasmid stability, gene expression and n-butanol biosynthesis in Clostridium tyrobutyricum.</title>
            <link>http://www.medworm.com/index.php?rid=5492537&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22139042%26dopt%3DAbstract</link>
            <description>In this study, C. tyrobutyricum was used as a host to produce n-butanol by expressing adhE2 gene under the control of a native thiolase promoter using four different conjugative plasmids (pMTL82151, 83151, 84151, and 85151) each with a different replicon (pBP1 from C. botulinum NCTC2916, pCB102 from C. butyricum, pCD6 from Clostridium difficile, and pIM13 from Bacillus subtilis). The effects of different replicons on transformation efficiency, plasmid stability, adhE2 expression and aldehyde/alcohol dehydrogenase activities, and butanol production by different mutants of C. tyrobutyricum were investigated. Among the four plasmids and replicons studied, pMTL82151 with pBP1 gave the highest transformation efficiency, plasmid stability, gene expression, and butanol biosynthesis. Butanol produ...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5492537</comments>
            <pubDate>Sun, 04 Dec 2011 05:00:00 +0100</pubDate>
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        <item>
            <title>Expression and characterization of human proinsulin fused to thioredoxin in Escherichia coli.</title>
            <link>http://www.medworm.com/index.php?rid=5492539&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22139017%26dopt%3DAbstract</link>
            <description>In conclusion, it was possible to obtain with high-yield purified human PI as a fusion protein in E. coli and useful for analytical purposes.
    PMID: 22139017 [PubMed - as supplied by publisher] (Source: Applied Microbiology and Biotechnology)</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5492539</comments>
            <pubDate>Sat, 03 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5492539</guid>        </item>
        <item>
            <title>Physiology, biochemistry and possible applications of microbial caffeine degradation.</title>
            <link>http://www.medworm.com/index.php?rid=5492538&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22139018%26dopt%3DAbstract</link>
            <description>Authors: Gummadi SN, Bhavya B, Ashok N
    Abstract
    Caffeine, a purine alkaloid is a constituent of widely consumed beverages. The scientific evidence which has proved the harm of this alkaloid has paved the way for innumerable research in the area of caffeine degradation. In addition to this, the fact that the by-products of the coffee and tea industry pollute the environment has called for the need of decaffeinating coffee and tea industry's by-products. Though physical and chemical methods for decaffeination are available, the lack of specificity for removal of caffeine in these techniques and their non-eco-friendly nature has opened the area of microbial and enzymatic degradation of caffeine. Another important application of microbial caffeine degradation apart from its advantages ...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5492538</comments>
            <pubDate>Sat, 03 Dec 2011 05:00:00 +0100</pubDate>
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        <item>
            <title>Fungal chitinases: diversity, mechanistic properties and biotechnological potential.</title>
            <link>http://www.medworm.com/index.php?rid=5492543&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22134638%26dopt%3DAbstract</link>
            <description>Authors: Hartl L, Zach S, Seidl-Seiboth V
    Abstract
    Chitin derivatives, chitosan and substituted chito-oligosaccharides have a wide spectrum of applications ranging from medicine to cosmetics and dietary supplements. With advancing knowledge about the substrate-binding properties of chitinases, enzyme-based production of these biotechnologically relevant sugars from biological resources is becoming increasingly interesting. Fungi have high numbers of glycoside hydrolase family 18 chitinases with different substrate-binding site architectures. As presented in this review, the large diversity of fungal chitinases is an interesting starting point for protein engineering. In this review, recent data about the architecture of the substrate-binding clefts of fungal chitinases, in connecti...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5492543</comments>
            <pubDate>Fri, 02 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5492543</guid>        </item>
        <item>
            <title>Immunological features and the ability of inhibitory effects on enzymatic activity of an epitope vaccine composed of cholera toxin B subunit and B cell epitope from Helicobacter pylori urease A subunit.</title>
            <link>http://www.medworm.com/index.php?rid=5492542&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22134639%26dopt%3DAbstract</link>
            <description>In this study, we constructed an epitope vaccine with mucosal adjuvant cholera toxin B subunit (CTB) and an epitope (UreA(183-203)) of H. pylori urease A subunit named CTB-UA. The CTB-UA fusion protein was expressed in Escherichia coli, and the purified protein was used for intraperitoneal immunization experiments in BALB/c mice. The experimental results indicated that anti-CTB-UA antibody could recognize both H. pylori urease A subunit (UreA) and urease B subunit (UreB). Besides, the CTB-UA epitope vaccine had good immunogenicity and immunoreactivity and could induce specific neutralizing antibodies which showed effectively inhibitory effect on the enzymatic activity of H. pylori urease. CTB-UA is a promising molecule to be investigated as H. pylori vaccine antigen candidate.
    PMID: 22...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5492542</comments>
            <pubDate>Fri, 02 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5492542</guid>        </item>
        <item>
            <title>Characterization of a methane-oxidizing biofilm using microarray, and confocal microscopy with image and geostatic analyses.</title>
            <link>http://www.medworm.com/index.php?rid=5492541&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22134640%26dopt%3DAbstract</link>
            <description>Authors: Kim TG, Yi T, Lee EH, Ryu HW, Cho KS
    Abstract
    A mixed methane-oxidizing biofilm was characterized, concurrently using a number of advanced techniques. Community analysis results by microarray exhibited that type II members dominated the methanotrophic community, in which Methylocystis was most abundant, followed by Methylosinus. Observation results by fluorescent in situ hybridization and confocal microscopy showed multiple biofilm colonies that were irregular, bell-shaped, with mean thickness of approximately 20 μm. Image analysis results indicated that the relative abundance of methanotrophs peaked at a depth of about 5 μm. Although the biofilm colonies differed in size, methanotrophs accounted for 4-9%. Gaussian and linear regression results between the biofilm volu...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5492541</comments>
            <pubDate>Fri, 02 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5492541</guid>        </item>
        <item>
            <title>High-level mucosal and systemic immune responses induced by oral administration with Lactobacillus-expressed porcine epidemic diarrhea virus (PEDV) S1 region combined with Lactobacillus-expressed N protein.</title>
            <link>http://www.medworm.com/index.php?rid=5492540&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22134641%26dopt%3DAbstract</link>
            <description>Authors: Di-Qiu L, Jun-Wei G, Xin-Yuan Q, Yan-Ping J, Song-Mei L, Yi-Jing L
    Abstract
    To develop effective mucosal vaccine formulation against porcine epidemic diarrhea virus (PEDV) infection, the DNA fragments encoding spike protein immunodominant region S1 and nucleocapsid N of PEDV were inserted into pPG1 (surface-displayed) or pPG2 (secretory) plasmids followed by electrotransformation into Lactobacillus casei (Lc) to yield four recombinant strains: PG1-S1, PG2-S1, PG1-N, and PG2-N. After intragastric administration, it was observed that live Lc-expressing S1 protein combined with Lc-expressing N protein could elicit much more potent mucosal and systemic immune responses than the former alone (P &amp;lt; 0.001), however slightly inferior to the latter alone (P &amp;gt; 0.05). Fu...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5492540</comments>
            <pubDate>Fri, 02 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5492540</guid>        </item>
        <item>
            <title>Anaerobic xylose fermentation by Spathaspora passalidarum.</title>
            <link>http://www.medworm.com/index.php?rid=5492550&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22124720%26dopt%3DAbstract</link>
            <description>In this study, it is demonstrated that under anaerobic conditions Spathaspora passalidarum showed high ethanol production yield, fast cell growth, and rapid sugar consumption with xylose being consumed after glucose depletion, while P. stipitis was almost unable to utilize xylose under these conditions. It is further demonstrated that for S. passalidarum, the xylose conversion takes place by means of NADH-preferred xylose reductase (XR) and NAD(+)-dependent xylitol dehydrogenase (XDH). Thus, the capacity of S. passalidarum to utilize xylose under anaerobic conditions is possibly due to the balance between the cofactor's supply and demand through this XR-XDH pathway. Only few XRs with NADH preference have been reported so far. 2-Deoxy glucose completely inhibited the conversion of xylose by...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5492550</comments>
            <pubDate>Wed, 30 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5492550</guid>        </item>
        <item>
            <title>Computational identification of gene over-expression targets for metabolic engineering of taxadiene production.</title>
            <link>http://www.medworm.com/index.php?rid=5492549&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22124721%26dopt%3DAbstract</link>
            <description>In this study, metabolic engineering was applied in the context of over-expression targets predicted to improve taxadiene production. Identified targets included genes both within and outside of the isoprenoid precursor pathway. These targets were then tested for experimental over-expression in a heterologous Escherichia coli host designed to support isoprenoid biosynthesis. Results confirmed the computationally predicted improvements and indicated a synergy between targets within the expected isoprenoid precursor pathway and those outside this pathway. The presented algorithm is broadly applicable to other host systems and/or product choices.
    PMID: 22124721 [PubMed - as supplied by publisher] (Source: Applied Microbiology and Biotechnology)</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5492549</comments>
            <pubDate>Wed, 30 Nov 2011 05:00:00 +0100</pubDate>
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        <item>
            <title>Bioleaching in brackish waters-effect of chloride ions on the acidophile population and proteomes of model species.</title>
            <link>http://www.medworm.com/index.php?rid=5492548&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22124722%26dopt%3DAbstract</link>
            <description>This study aimed to investigate the impact of increasing concentrations of chloride ions on the population dynamics of a mixed culture during pyrite bioleaching and apply proteomics to elucidate how two species from this mixed culture alter their proteomes under chloride stress. A mixture consisting of well-known biomining microorganisms and an enrichment culture obtained from an acidic saline drain were tested for their ability to bioleach pyrite in the presence of 0, 3.5, 7, and 20 g L(-1) NaCl. Microorganisms from the enrichment culture were found to out-compete the known biomining microorganisms, independent of the chloride ion concentration. The proteomes of the Gram-positive acidophile Acidimicrobium ferrooxidans and the Gram-negative acidophile Acidithiobacillus caldus grown in t...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5492548</comments>
            <pubDate>Wed, 30 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5492548</guid>        </item>
        <item>
            <title>Recent advances in curdlan biosynthesis, biotechnological production, and applications.</title>
            <link>http://www.medworm.com/index.php?rid=5492547&amp;cid=s_37327_77_f&amp;fid=37327&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22124723%26dopt%3DAbstract</link>
            <description>Authors: Zhan XB, Lin CC, Zhang HT
    Abstract
    Curdlan is a water-insoluble β-(1,3)-glucan produced by Agrobacterium species under nitrogen-limited condition. Its heat-induced gelling properties render curdlan to be very useful in the food industry initially. Recent advances in the understanding of the role curdlan plays in both innate and adaptive immunity lead to its growing applications in biomedicine. Our review focuses on the recent advances on curdlan biosynthesis and the improvements of curdlan fermentation production both from our laboratory and many others as well as the latest advances on the new applications of curdlan and its derivatives particularly in their immunological functions in biomedicine.
    PMID: 22124723 [PubMed - as supplied by publisher] (Source: Applied Mi...</description>
            <author>Applied Microbiology and Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5492547</comments>
            <pubDate>Wed, 30 Nov 2011 05:00:00 +0100</pubDate>
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