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        <title>Biotechnology Letters 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 'Biotechnology Letters' source.</description>
        <link><![CDATA[http://www.medworm.com/rss/search.php?qu=Biotechnology+Letters&t=Biotechnology+Letters&s=Search&f=source]]></link>
        <lastBuildDate>Mon, 06 Feb 2012 18:10:49 +0100</lastBuildDate>
        <item>
            <title>Comparison of the spores of Paenibacillus polymyxa prepared at different temperatures.</title>
            <link>http://www.medworm.com/index.php?rid=5656662&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22294453%26dopt%3DAbstract</link>
            <description>Authors: Huo Z, Zhang N, Raza W, Huang X, Yong X, Liu Y, Wang D, Li S, Shen Q, Zhang R
    Abstract
    Paenibacillus polymyxa SQR-21, which is antagonistic against Fusarium oxysporum, is used as a biocontrol agent and, when mixed with organic substances for solid fermentation, produces a bioorganic fertilizer. The spores of P. polymyxa prepared at different temperatures were characterized with respect to the dipicolinic acid content, heat resistance, fatty acid composition and germination. Spores prepared at 37Â°C showed higher heat resistance than those prepared at 25 and 30Â°C. However, the germination rate was negatively correlated with the sporulation temperature. The maximum germination rate of the spores prepared at 25Â°C was 1.3-times higher than the spores prepared at 30Â°C. The s...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5656662</comments>
            <pubDate>Wed, 01 Feb 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5656662</guid>        </item>
        <item>
            <title>Identification and characterization of stress resistance related genes of Brassica                   rapa.</title>
            <link>http://www.medworm.com/index.php?rid=5656664&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22286206%26dopt%3DAbstract</link>
            <description>Identification and characterization of stress resistance related genes of Brassica          rapa.
    Biotechnol Lett. 2012 Jan 29;
    Authors: Ahmed NU, Park JI, Jung HJ, Seo MS, Kumar TS, Lee IH, Nou IS
    Abstract
    Two biotic stress resistance related genes from the full-length cDNA library of Brassica rapa cv. Osome were identified from EST analysis and determined to be pathogenesis-related (PR) 12 Brassica defensin-like family protein (BrDLFP) and PR-10 Brassica           Betv1 allergen family protein (BrBetv1AFP) after sequence analysis and homology study with other stress resistance related same family genes. In the expression analysis, both genes expressed in different organs and during all developmental growth stages in healthy plants. Expression of BrDLFP significantly incre...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5656664</comments>
            <pubDate>Sun, 29 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5656664</guid>        </item>
        <item>
            <title>Organic solvent-tolerant elastase efficiently hydrolyzes insoluble, cross-linked, protein fiber of eggshell membranes.</title>
            <link>http://www.medworm.com/index.php?rid=5656663&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22286207%26dopt%3DAbstract</link>
            <description>Authors: Takenaka S, Hano S, Cheng M, Yoshida KI, Aoki K
    Abstract
    Eggshell membrane is a mechanically stable and insoluble cross-linked fibrous protein. Pseudomonas aeruginosa strain ME-4 synthesizes a metalloprotease that degrades the eggshell membrane. We cloned the encoding gene in Escherichia coli. The recombinant protease, over-expressed in E. coli, was inactive but addition of acetone to crude cell extracts restored the activity and removed many E. coli proteins. We purified the active, acetone-treated protease to homogeneity in a single chromatography step with 57% recovery. The recombinant protease partially hydrolyzed eggshell membrane and produced more soluble peptides and proteins than commercial elastase, Î±-chymotrypsin, and collagenase. The soluble peptides produced f...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5656663</comments>
            <pubDate>Sun, 29 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5656663</guid>        </item>
        <item>
            <title>Correlation between efficacy and structure of recombinant epitope vaccines against bovine type O foot and mouth disease virus.</title>
            <link>http://www.medworm.com/index.php?rid=5656668&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22286179%26dopt%3DAbstract</link>
            <description>Authors: Fang M, Li J, Wang H, Yang M, Zhang Y, Zhou L, Wei H, Yang G, Yu Y, Wei X, Yu Y, Wang L, Wan M
    Abstract
    To develop recombinant epitope vaccines against foot-and-mouth disease virus (FMDV), genes coding for six recombinant proteins (rP1-rP6) consisting of different combinations of B cell and T cell epitope from VP1 capsid protein (VP1) of type O FMDV were constructed and the 3D structure of these proteins analyzed. This revealed a surface-exposed RGD sequence of B cell epitopes in all six recombinant proteins as that in VP1 of FMDV and rP1, rP2 and rP4 globally mimicked the backbone conformation of the VP1. rP1, rP2 and rP4 stimulated guinea pigs to produce higher level of neutralizing antibodies capable of protecting suckling mice against FMDV challenge. rP1 stimulated cat...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5656668</comments>
            <pubDate>Sat, 28 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5656668</guid>        </item>
        <item>
            <title>Microbial community of aerobic granules for ammonium and sulphide removal in a sequencing batch reactor.</title>
            <link>http://www.medworm.com/index.php?rid=5656667&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22286180%26dopt%3DAbstract</link>
            <description>Authors: Su C, Zhu L, Zhang C, Qi X, Guo Y, Gao R
    Abstract
    Aerobic granules for sulphide and ammonium removal were cultivated in a sequencing batch reactor, and the microbial community of the aerobic granules was investigated by denaturing gradient gel electrophoresis. The loading rate increased from 0.15 to 0.9Â kgÂ S(2-Â )m(-3Â )d(-1), and the removal efficiencies of sulphide, chemical oxygen demand, and NH(4)                (+)-N were higher than 99, 80, and 98%, respectively. However, sludge settleability became poorer when the loading rate exceeded 0.3Â kgÂ S(2-Â )m(-3Â )d(-1). The denitrifying bacteria in the aerobic granules were Thauera sp., Pseudomonas alcaligenes, and uncultured planctomycetes, indicating that multiple N-removing processes occurred simultaneously in the a...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5656667</comments>
            <pubDate>Sat, 28 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5656667</guid>        </item>
        <item>
            <title>Efficient and rapid uptake of magnetic carbon nanotubes into human monocytic cells: implications for cell-based cancer gene therapy.</title>
            <link>http://www.medworm.com/index.php?rid=5656666&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22286181%26dopt%3DAbstract</link>
            <description>Authors: Gul-Uludag H, Lu W, Xu P, Xing J, Chen J
    Abstract
    Monocyte-based gene therapies in cancer have been hampered by either the resistance of these cells to non-viral molecular delivery methods or their poor trafficking to the tumor site after their ex vivo manipulations. Magnetic nanoparticles (MNP)-loaded genetically engineered monocytes can efficiently delivered to tumor site by external magnetic field, but they are not ideal delivery tools due to their spherical shape. Hence, we have investigated the cellular uptake efficiency and cytotoxicity of fluorescein isothiocyanate (FITC)-labelled magnetic carbon nanotubes (FITC-mCNT) in human monocytic leukemia cell line THP-1 for application in cell-based gene therapy against cancer. Uptake of FITC-mCNT into THP-1 cells reached 10...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5656666</comments>
            <pubDate>Sat, 28 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5656666</guid>        </item>
        <item>
            <title>Internal ribosome entry site mediates protein synthesis in yeast Pichia pastoris.</title>
            <link>http://www.medworm.com/index.php?rid=5656665&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22286182%26dopt%3DAbstract</link>
            <description>Authors: Liang S, Lin Y, Li C, Ye Y
    Abstract
    The imitation of translation, as mediated by internal ribosome entry sites, has not yet been reported in Pichia pastoris. An IRES element from Saccharomyces cerevisiae was demonstrated to direct the translation of a dicistronic mRNA in P. pastoris. The 5'-untranslated region of GPR1 mRNA, termed GPR, was cloned into a dual reporter construct containing an upstream Rhizomucor miehei lipase (RML) and a downstream Î²-galactosidase gene (lacZ) from Escherichia coli BL21. After being transformed into P. pastoris, the RML gene and lacZ were simultaneously expressed. The possibility of DNA rearrangement, spurious splicing, or cryptic promoter in the GPR sequence were eliminated, indicating that expression of a second ORF was IRES-dependent. The...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5656665</comments>
            <pubDate>Sat, 28 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5656665</guid>        </item>
        <item>
            <title>Site-directed mutagenesis in bacteriorhodopsin mutants and their characterization for bioelectrical and biotechnological equipment.</title>
            <link>http://www.medworm.com/index.php?rid=5637690&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22270563%26dopt%3DAbstract</link>
            <description>Authors: Saeedi P, Moosaabadi JM, Sebtahmadi SS, Behmanesh M, Mehrabadi JF
    Abstract
    Bacteriorhodopsin (BR) mutagenesis plays an important role in the development of BR-based materials and tools with enhanced optical and electrical properties. Previously reported protocols for generating BR mutations are inefficient for the preparation and purification of mutant proteins. Therefore, a series of BR mutations were generated by using improved methods, which are described in further detail. The functional activity of the recombinant proteins was confirmed by spectroscopic and electrochemical assays. Modified proteins with different wavelengths and activities form a foundation for color-sensitive sensors and can be utilized to produce unique bioelectrical and biotechnological tools and m...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5637690</comments>
            <pubDate>Sat, 21 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5637690</guid>        </item>
        <item>
            <title>Significance of Tyr302, His235 and Asp194 in the Î±-amylase from Bacillus licheniformis.</title>
            <link>http://www.medworm.com/index.php?rid=5619326&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22261861%26dopt%3DAbstract</link>
            <description>Authors: Qin Y, Fang Z, Pan F, Zhao Y, Li H, Wu H, Meng X
    Abstract
    The calcium-binding residues, Tyr302 and His235, and the sodium-binding residue, Asp194, on the activity of Bacillus licheniformis Î±-amylase were investigated using site-directed mutagenesis. Tyr302 and His235 were replaced by Asn and Asp, respectively, to produce the mutants Y302N and H235D; Asp194 was replaced by Ala to produce D194A. The mutant amylases were purified to homogeneity; each was ~53Â kDa. The specific activity of the D194A was 236Â UÂ mg(-1), lower than the specific activity of the wild-type enzyme by 55%. No significant changes of thermostability, optimum temperature, and optimum pH level were observed in D194A. Mutant amylases with H235D and Y302N significantly improved their specific activity by ...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5619326</comments>
            <pubDate>Fri, 20 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5619326</guid>        </item>
        <item>
            <title>Bioconversion of ethyl (R)-4-cyano-3-hydroxybutyate into (R)-ethyl-3-hydroxyglutarate via an indirect pathway by Rhodococcus boritolerans.</title>
            <link>http://www.medworm.com/index.php?rid=5619325&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22261862%26dopt%3DAbstract</link>
            <description>Authors: Yang MJ, Wang XJ, Yang ZY, An J, Xiang WS, Zhang J
    Abstract
    (R)-Ethyl-3-hydroxyglutarate, (R)-3, is an intermediate in the synthesis of the statin side chain. Here, a new two-step, indirect biotransformation pathway involving the formation of ethyl (R)-4-carbamoyl-3-hydroxybutanoate, (R)-2, as an intermediate for (R)-3 production was developed using Rhodococcus boritolerans with ethyl (R)-4-cyano-3-hydroxybutyate, (R)-1, as substrate. Maximum conversion was with 10Â g (R)-1/l, 7Â g cells/l (dry wt), pH 7.5 and 25Â°C. A yield of 98Â Â±Â 0.5% (w/w) was attained within 8Â h.
    PMID: 22261862 [PubMed - as supplied by publisher] (Source: Biotechnology Letters)</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5619325</comments>
            <pubDate>Fri, 20 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5619325</guid>        </item>
        <item>
            <title>Characterization of D: -lactate dehydrogenase from Pediococcus acidilactici that converts phenylpyruvic acid into phenyllactic acid.</title>
            <link>http://www.medworm.com/index.php?rid=5619324&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22261863%26dopt%3DAbstract</link>
            <description>Authors: Mu W, Yu S, Jiang B, Li X
    Abstract
    The gene coding for D: -lactate dehydrogenase (D: -LDH) from Pediococcus acidilactici DSM 20284 was cloned and expressed in E. coli. The recombinant enzyme was purified by nickel-affinity chromatography. It converted phenylpyruvic acid (PPA) to 3-phenyllactic acid maximally at 30Â°C and pH 5.5 with a specific activity of 140 and 422Â U/mg for PPA and pyruvate, respectively. The K           (m), turnover number (k           (cat)), and catalytic efficiency (k           (cat)/K           (m)) for PPA were 2.9Â mM, 305Â s(-1), and 105Â mM(-1) s(-1), respectively.
    PMID: 22261863 [PubMed - as supplied by publisher] (Source: Biotechnology Letters)</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5619324</comments>
            <pubDate>Fri, 20 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5619324</guid>        </item>
        <item>
            <title>RNAi-directed down-regulation of RSV results in increased resistance in rice (Oryza sativa L.).</title>
            <link>http://www.medworm.com/index.php?rid=5619323&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22261864%26dopt%3DAbstract</link>
            <description>Authors: Zhou Y, Yuan Y, Yuan F, Wang M, Zhong H, Gu M, Liang G
    Abstract
    Rice stripe disease (RSD), caused by rice stripe virus (RSV), is a serious disease in temperate rice-growing areas. We have created an RNAi construct containing coat protein gene (CP) and disease specific protein gene (SP) sequences from RSV. The RNAi construct was transformed into two susceptible japonica varieties, Suyunuo and Guanglingxiangjing, to develop resistance against RSD. The homozygous progeny of rice plants in the T(5) and T(7) generations containing RNAi constructs, after self-fertilization were strongly resistant to viral infection. RT-PCR indicated that viral replication of SP and CP in the transgenic plants was significantly inhibited. There were no obvious morphological or developmental diffe...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5619323</comments>
            <pubDate>Fri, 20 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5619323</guid>        </item>
        <item>
            <title>Biotransformation of ginsenosides Re and Rg1 into ginsenosides Rg2 and Rh1 by recombinant Î²-glucosidase.</title>
            <link>http://www.medworm.com/index.php?rid=5619322&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22261865%26dopt%3DAbstract</link>
            <description>Authors: Quan LH, Min JW, Sathiyamoorthy S, Yang DU, Kim YJ, Yang DC
    Abstract
    Ginsenosides Re and Rg1 were transformed by recombinant Î²-glucosidase (Bgp1) to ginsenosides Rg2 and Rh1, respectively. The bgp1 gene consists of 2,496Â bp encoding 831 amino acids which have homology to the glycosyl hydrolase families 3 protein domain. Using 0.1Â mg enzyme ml(-1) in 20Â mM sodium phosphate buffer at 37Â°C and pH 7.0, the glucose moiety attached to the C-20 position of ginsenosides Re and Rg1, was removed: 1Â mg ginsenoside Re ml(-1) was transformed into 0.83Â mg Rg2Â ml(-1) (100% molar conversion) after 2.5Â h and 1Â mg ginsenoside Rg1Â ml(-1) was transformed into 0.6Â mg ginsenoside Rh1Â ml(-1) (78% molar conversion) in 15Â min. Using Bgp1 enzyme, almost all initial ginsenosides Re and...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5619322</comments>
            <pubDate>Fri, 20 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5619322</guid>        </item>
        <item>
            <title>Selection of DNA aptamers that bind to four organophosphorus pesticides.</title>
            <link>http://www.medworm.com/index.php?rid=5619321&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22261866%26dopt%3DAbstract</link>
            <description>Authors: Wang L, Liu X, Zhang Q, Zhang C, Liu Y, Tu K, Tu J
    Abstract
    Single-stranded DNA (ssDNA) aptamers against four organophosphorus pesticides (phorate, profenofos, isocarbophos and omethoate) were simultaneously isolated from an immobilized random ssDNA library by systematic evolution of ligands by exponential enrichment (SELEX) technique. After 12 rounds of in vitro selection, five ssDNA aptamer candidates were selected and their binding affinities were identified by a novel method using a molecular beacon. Two of the five ssDNA sequences, SS2-55 and SS4-54, demonstrated higher affinities and specificities to the four organophosphorus pesticides. They were defined as broad-spectrum aptamers binding to four different targets and their simulated secondary structures showed high...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5619321</comments>
            <pubDate>Fri, 20 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5619321</guid>        </item>
        <item>
            <title>Prokaryotic expression of pathogenesis related protein 1 gene from Nicotiana benthamiana: antifungal activity and preparation of its polyclonal antibody.</title>
            <link>http://www.medworm.com/index.php?rid=5619320&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22261867%26dopt%3DAbstract</link>
            <description>Authors: Zhu F, Xu M, Wang S, Jia S, Zhang P, Lin H, Xi D
    Abstract
    The nucleotide sequence of the pathogenesis-related protein 1(PR-1) gene was obtained from Nicotiana benthamiana using RT-PCR. Restriction enzyme cutting sites of EcoRI and NotI were introduced to the ORF fragments of PR-1, they were then linked together with pET-30a (+) and transformed into E. coli BL21 (DE3). The target protein was induced by 1.5Â mM IPTG, at 37Â°C for 4Â h. The expressed protein was purified by Ni-NTA and an anti-NbPR-1 polyclonal antibody was prepared using rabbits. The antibody could detect the expression of PR-1 in N. benthamiana and other Nicotiana plants. NbPR-1 protein has four Î±-helices and two Î²-sheets by homology modeling. Furthermore, the purified NbPR-1 protein exhibited a broad-spec...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5619320</comments>
            <pubDate>Fri, 20 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5619320</guid>        </item>
        <item>
            <title>Co-expression of the small heat shock protein, Lo18, with Î²-glucosidase in Escherichia coli improves solubilization and reveals various associations with overproduced heterologous protein, GroEL/ES.</title>
            <link>http://www.medworm.com/index.php?rid=5619319&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22261868%26dopt%3DAbstract</link>
            <description>Authors: Ronez F, Desroche N, Arbault P, Guzzo J
    Abstract
    We developed a new system to improve the overproduction of soluble proteins in E. coli based on a plasmid encoding the small heat-shock protein, Lo18, derived from the lactic acid bacterium Oenococcus oeni. The efficiency of this system was compared with that of another system based on production of the E. coli universal chaperone GroEL/ES. A compatible plasmid encoding Î²-glucosidase was constructed for the overproduction and aggregation of this enzyme. Co-expression with Lo18 resulted in an increase in soluble Î²-glucosidase levels similar to that obtained in the GroEL/ES co-expression system. Lo18 was found preferentially in the insoluble fraction, associated with aggregated enzyme. By contrast, GroEL/ES was more abundant...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5619319</comments>
            <pubDate>Fri, 20 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5619319</guid>        </item>
        <item>
            <title>Retrieval of glycoside hydrolase family 9 cellulase genes from environmental DNA by metagenomic gene specific multi-primer PCR.</title>
            <link>http://www.medworm.com/index.php?rid=5619318&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22261869%26dopt%3DAbstract</link>
            <description>Authors: Xiong X, Yin X, Pei X, Jin P, Zhang A, Li Y, Gong W, Wang Q
    Abstract
    A new method, termed metagenomic gene specific multi-primer PCR (MGSM-PCR), is presented that uses multiple gene specific primers derived from an isolated gene from a constructed metagenomic library rather than degenerate primers designed based on a known enzyme family. The utility of MGSM-PCR was shown by applying it to search for homologues of the glycoside hydrolase family 9 cellulase in metagenomic DNA. The success of the multiplex PCR was verified by visualizing products on an agarose gel following gel electrophoresis. A total of 127 homologous genes were amplified with combinatorial multi-primer reactions from 34 soil DNA samples. Multiple alignments revealed extensive sequence diversity among these...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5619318</comments>
            <pubDate>Fri, 20 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5619318</guid>        </item>
        <item>
            <title>Identification and validation of sex-linked SCAR markers in dioecious Hippophae rhamnoides L. (Elaeagnaceae).</title>
            <link>http://www.medworm.com/index.php?rid=5619327&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22245920%26dopt%3DAbstract</link>
            <description>Authors: Korekar G, Sharma RK, Kumar R, Meenu , Bisht NC, Srivastava RB, Ahuja PS, Stobdan T
    Abstract
    The actinorhizal plant seabuckthorn (Hippophae rhamnoides L., Elaeagnaceae) is a wind pollinated dioecious crop. To distinguish male genotypes from female genotypes early in the vegetative growth phase, we have developed robust PCR-based marker(s). DNA bulk samples from 20 male and 20 female plants each were screened with 60 RAPD primers. Two primers, OPA-04 and OPT-06 consistently amplified female-specific (FS) polymorphic fragments of 1,164 and 868Â bp, respectively, that were absent in the male samples. DNA sequence of the two markers did not exhibit significant similarity to previously characterized sequences. A sequence-characterized amplified region marker HrX1 (JQ284019) and...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5619327</comments>
            <pubDate>Fri, 13 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5619327</guid>        </item>
        <item>
            <title>Erratum to: Simultaneous extraction of carotenoids and transfructosylating enzyme from Xanthophyllomyces dendrorhous by a bead beater.</title>
            <link>http://www.medworm.com/index.php?rid=5619328&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22231202%26dopt%3DAbstract</link>
            <description>Authors: Lee SC, Fang TJ
    PMID: 22231202 [PubMed - as supplied by publisher] (Source: Biotechnology Letters)</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5619328</comments>
            <pubDate>Tue, 10 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5619328</guid>        </item>
        <item>
            <title>Momilactione B inhibits protein kinase A signaling and reduces tyrosinase-related proteins 1 and 2 expression in melanocytes.</title>
            <link>http://www.medworm.com/index.php?rid=5576896&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22215377%26dopt%3DAbstract</link>
            <description>Authors: Lee JH, Cho B, Jun HJ, Seo WD, Kim DW, Cho KJ, Lee SJ
    Abstract
    Momilactone B (MB) is a terpenoid phytoalexin present in rice bran that exhibits several biological activities. MB reduced the melanin content in B16 melanocytes melanin content and inhibited tyrosinase activities. Using transcriptome analysis, the genes involved in protein kinase A (PKA) signaling were found to be markedly altered. B16 cells stimulated with MB had decreased concentrations of cAMP protein kinase A activity, and cAMP-response element-binding protein which is a key transcription factor for microphthalmia-associated transcription factor (MITF) expression. Accordingly, the expression of MITF and its target genes, which are essential for melanogenesis, were reduced. MB thus exhibits anti-melanogenic...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5576896</comments>
            <pubDate>Wed, 04 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5576896</guid>        </item>
        <item>
            <title>Accumulation of pyruvate by changing the redox status in Escherichia coli.</title>
            <link>http://www.medworm.com/index.php?rid=5576895&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22215378%26dopt%3DAbstract</link>
            <description>Authors: Ojima Y, Suryadarma P, Tsuchida K, Taya M
    Abstract
    Pyruvate was produced from glucose by Escherichia coli BW25113 that contained formate dehydrogenase (FDH) from Mycobacterium vaccae. In aerobic shake-flask culture (K           (L)           aÂ =Â 4.9Â min(-1)), the recombinant strain produced 6.7Â g pyruvateÂ l(-1) after 24Â h with 4Â g sodium formateÂ l(-1) and a yield of 0.34Â g pyruvateÂ gÂ glucose(-1). These values were higher than those of the original strain (0.2Â gÂ l(-1) pyruvate and 0.02Â g pyruvateÂ gÂ glucose(-1)). Based on the reaction mechanism of FDH, the introduction of FDH into E. coli enhances the accumulation of pyruvate by the regeneration of NADH from NAD(+) since NAD(+) is a shared cosubstrate with the pyruvate dehydrogenase complex, which decarboxyla...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5576895</comments>
            <pubDate>Wed, 04 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5576895</guid>        </item>
        <item>
            <title>Sequencing and de novo analysis of the Chinese Sika deer antler-tip transcriptome during the ossification stage using Illumina RNA-Seq technology.</title>
            <link>http://www.medworm.com/index.php?rid=5576897&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22212490%26dopt%3DAbstract</link>
            <description>Authors: Yao B, Zhao Y, Zhang H, Zhang M, Liu M, Liu H, Li J
    Abstract
    Deer antlers are the only mammalian appendages capable of repeated rounds of regeneration. Every year, deer antlers are shed and regrown from blastema into large branched structures of cartilage and bone. Little is known about the genes involved in antler development particularly during the later stages of ossification. We have produced more than 39 million sequencing reads in a single run using the Illumina sequencing platform. These were assembled into 138,642 unique sequences (mean size: 405Â bp) representing 50 times the number of Sika deer sequences previously available in the NCBI database (as of Nov 2, 2011). Based on a similarity search of a database of known proteins, we identified 43,937 sequences with ...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5576897</comments>
            <pubDate>Tue, 03 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5576897</guid>        </item>
        <item>
            <title>Cell surface properties of Pseudomonas stutzeri in the process of diesel oil biodegradation.</title>
            <link>http://www.medworm.com/index.php?rid=5558138&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22210557%26dopt%3DAbstract</link>
            <description>Authors: Kaczorek E, Jesionowski T, Giec A, Olszanowski A
    Abstract
    Pseudomonas stutzeri, isolated from crude oil-contaminated soil, was used to degrade diesel oil. Of three surfactants, 120Â mg rhamnolipids 1(-1) significantly increased degradation of diesel oil giving 88% loss after 14Â days compared to 54% loss without the surfactant. The system with rhamnolipids was characterised by relatively high particle homogeneity. However, the addition of saponins to diesel oil caused the cells to aggregate (the polydispersity index: 0.542) and the biodegradation of diesel oil was only 46%. The cell yield was 0.22Â gÂ l(-1).
    PMID: 22210557 [PubMed - as supplied by publisher] (Source: Biotechnology Letters)</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5558138</comments>
            <pubDate>Sat, 31 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5558138</guid>        </item>
        <item>
            <title>Efficient formation of cell spheroids using polymer nanofibers.</title>
            <link>http://www.medworm.com/index.php?rid=5558195&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22207145%26dopt%3DAbstract</link>
            <description>In this study, we developed a new method for the suspension cultures of anchorage-dependent animal cells using polymer nanofibers. Poly(lactic-co-glycolic acid) nanofibers (785Â nm in average fiber-diameter, 88Â Î¼m in average fiber-length) fabricated by the electrospinning method were added to each suspension culture of human embryonic kidney 293 cells and human dermal fibroblasts. As compared to no addition of nanofibers to the suspension cultures, nanofibers enhanced cell spheroid formation, thereby reducing cell death resulting from a lack of cell adhesion. Efficient formation of spheroids in the presence of polymer nanofibers may be useful for the suspension cultures of anchorage-dependent cells.
    PMID: 22207145 [PubMed - as supplied by publisher] (Source: Biotechnology Letters)</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5558195</comments>
            <pubDate>Fri, 30 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5558195</guid>        </item>
        <item>
            <title>Improved lycopene production by Blakeslea trispora with isopentenyl compounds and metabolic precursors.</title>
            <link>http://www.medworm.com/index.php?rid=5558174&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22207146%26dopt%3DAbstract</link>
            <description>Authors: Shi YQ, Xin XL, Yuan QP
    Abstract
    The highest lycopene production in mated cultures of Blakeslea trispora was 578Â mg/l by adding 42Â mg geraniol/l to the medium after 48Â h of growth. The control gave 317Â mg/l. Adding isopentenyl alcohol at 40Â mg/l, mevalonic acid at 17.5Â mg/l or dimethyl allyl alcohol at 150Â mg, each after 36Â h growth, gave lycopene yields 62, 45 and 47%, respectively, higher than the control.
    PMID: 22207146 [PubMed - as supplied by publisher] (Source: Biotechnology Letters)</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5558174</comments>
            <pubDate>Fri, 30 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5558174</guid>        </item>
        <item>
            <title>Removing human immunodeficiency virus (HIV) from human blood using immobilized heparin.</title>
            <link>http://www.medworm.com/index.php?rid=5558160&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22207147%26dopt%3DAbstract</link>
            <description>Authors: Nassar RA, Browne EP, Chen J, Klibanov AM
    Abstract
    Heparin covalently attached to a water-insoluble resin suspended in HIV-infected aqueous buffer or whole blood captures the virus; subsequent physical separation of the immobilized heparin reduced the viral titers by over 80 and 50%, respectively. The detoxification concept has been validated by both circulating an HIV-1 solution through a column packed with the heparin-sepharose beads and successively mixing an HIV-1 solution with fresh beads.
    PMID: 22207147 [PubMed - as supplied by publisher] (Source: Biotechnology Letters)</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5558160</comments>
            <pubDate>Fri, 30 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5558160</guid>        </item>
        <item>
            <title>Isolation and functional characterization of polyunsaturated fatty acid elongase (AsELOVL5) gene from black seabream (Acanthopagrus schlegelii).</title>
            <link>http://www.medworm.com/index.php?rid=5545305&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22198347%26dopt%3DAbstract</link>
            <description>Authors: Kim SH, Kim JB, Jang YS, Kim SY, Roh KH, Kim HU, Lee KR, Park JS
    Abstract
    To identify the genes encoding fatty acid elongases for the biosynthesis of polyunsaturated fatty acids (PUFAs), we isolated a cDNA via degenerate PCR and RACE-PCR from Acanthopagrus schlegelii with a high similarity to the ELOVL5-like elongases of mammals and fishes. This gene is termed AsELOVL5 and encodes a 294 amino acid protein. When AsELOVL5 was expressed in Saccharomyces cerevisiae, it conferred an ability to elongate Î³-linolenic acid (18:3 n-6) to di-homo-Î³-linolenic acid (20:3 n-6). In addition, the transformed cells converted arachidonic acid (20:4 n-6) and eicosapentaenpic acid (20:5 n-3) to docosatetraenoic acid (22:4 n-6) and docosapentaenoic acid (22:5 n-3), respectively. These result...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5545305</comments>
            <pubDate>Sat, 24 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5545305</guid>        </item>
        <item>
            <title>Wound healing by a 3.2Â kDa recombinant polypeptide from velvet antler of Cervus                   nippon Temminck.</title>
            <link>http://www.medworm.com/index.php?rid=5545304&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22198348%26dopt%3DAbstract</link>
            <description>Wound healing by a 3.2Â kDa recombinant polypeptide from velvet antler of Cervus          nippon Temminck.
    Biotechnol Lett. 2011 Dec 24;
    Authors: Zha E, Gao S, Pi Y, Li X, Wang Y, Yue X
    Abstract
    Velvet antler (VA) is used in traditional Chinese medicine to treat a wide range of ailments including the enhancement of wound healing. A 3.2Â kDa recombinant polypeptide of VA from sika deer was purified and compared to native polypeptides stimulation growth of NIH3T3 cells. Both stimulated growth in a dose-dependent manner (10-100Â Î¼g/ml). To study its wound healing properties, burn-wounded rats were topically administered with recombinant VA polypeptide or native polypeptide. Rats treated with 0.05 and 0.1% (w/w) polypeptides exhibited significant wound healing. As the yield of...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5545304</comments>
            <pubDate>Sat, 24 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5545304</guid>        </item>
        <item>
            <title>Novel and highly effective chemoenzymatic synthesis of (2R)-2-[4-(4-cyano-2-fluorophenoxy)phenoxy]butylpropanoate based on lipase mediated transesterification.</title>
            <link>http://www.medworm.com/index.php?rid=5527561&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22187074%26dopt%3DAbstract</link>
            <description>Authors: Zhu G, Yao R, Zhu H, Wang H
    Abstract
    (2R)-2-[4-(4-Cyano-2-fluorophenoxy)phenoxy]butylpropanoate (cyhalofop-butyl, CyB) was synthesized by a chemoenzymatic route involving enantioselective transesterification with Candida antarctica lipase B (Novozym 435). The optimum organic solvent, acyl donor, a           (             w           ), reaction temperature and shaking rate for the transesterification were acetonitrile, n-butanol, 0.11, 45Â°C and 200Â rpm, respectively. Under the optimum conditions, the maximum substrate conversion and the enantiomeric purity of the product were 96.9 and &amp;gt;99%, respectively. The total yield and enantiomeric purity of CyB by this chemoenzymatic synthesis were 60.4 and &amp;gt;99%, respectively; 15.3 and 21% higher than that of the traditional ...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5527561</comments>
            <pubDate>Wed, 21 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5527561</guid>        </item>
        <item>
            <title>Freeze drying formulation using microscale and design of experiment approaches: a case study using granulocyte colony-stimulating factor.</title>
            <link>http://www.medworm.com/index.php?rid=5527560&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22187075%26dopt%3DAbstract</link>
            <description>Authors: Grant Y, Matejtschuk P, Bird C, Wadhwa M, Dalby PA
    Abstract
    The lyophilization of proteins in microplates, to assess and optimise formulations rapidly, has been applied for the first time to a therapeutic protein and, in particular, one that requires a cell-based biological assay, in order to demonstrate the broader usefulness of the approach. Factorial design of experiment methods were combined with lyophilization in microplates to identify optimum formulations that stabilised granulocyte colony-stimulating factor during freeze drying. An initial screen rapidly identified key excipients and potential interactions, which was then followed by a central composite face designed optimisation experiment. Human serum albumin and Tween 20 had significant effects on maintaining pr...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5527560</comments>
            <pubDate>Wed, 21 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5527560</guid>        </item>
        <item>
            <title>Microbial production of the drugs violacein and deoxyviolacein: analytical development and strain comparison.</title>
            <link>http://www.medworm.com/index.php?rid=5527559&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22187076%26dopt%3DAbstract</link>
            <description>Authors: Rodrigues AL, GÃ¶cke Y, Bolten C, Brock NL, Dickschat JS, Wittmann C
    Abstract
    Violacein and deoxyviolacein display a broad range of interesting biological properties but their production is rarely distinguished due to the lack of suitable analytical methods. An HPLC method has been developed for the separation and quantification of violacein and deoxyviolacein and can determine the content of both molecules in microbial cultures. A comparison of different production microorganisms, including recombinant Escherichia coli and the natural producer Janthinobacterium lividum, revealed that the formation of violacein and deoxyviolacein is strain-specific but showed significant variation during growth although the ratio between the two compounds remained constant.
    PMID: 22187...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5527559</comments>
            <pubDate>Wed, 21 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5527559</guid>        </item>
        <item>
            <title>Single-colour flow cytometric assay to determine NK cell-mediated cytotoxicity and viability against non-adherent human tumor cells.</title>
            <link>http://www.medworm.com/index.php?rid=5527558&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22187077%26dopt%3DAbstract</link>
            <description>Authors: Thakur A, Zaman A, Hummel J, Jones K, Hortelano G
    Abstract
    A flow cytometry-based cytotoxicity (FCC) assay was developed using a single fluorophore, calcein-acetoxymethyl diacetylester (calcein-AM), to measure NK cell-mediated cytotoxicity. Non-adherent human K562 and U937 target cells were individually labelled with calcein-AM and co-incubated with effector NK cells to measure calcein loss, and therefore calculate target cell cytotoxicity. This FCC assay also provided a measure of sample viability. Notably, cell viability measured by traditional calcein/7-amino-actinomycin D (7-AAD) double labelling and Trypan Blue methods were comparable to the viability calculated using calcein-loss FCC. This FCC assay may also be used with various effector and target cell types and as ...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5527558</comments>
            <pubDate>Wed, 21 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5527558</guid>        </item>
        <item>
            <title>Identification and characterization of novel cellulolytic and hemicellulolytic genes and enzymes derived from German grassland soil metagenomes.</title>
            <link>http://www.medworm.com/index.php?rid=5527557&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22187078%26dopt%3DAbstract</link>
            <description>Authors: Nacke H, Engelhaupt M, Brady S, Fischer C, Tautzt J, Daniel R
    Abstract
    Soil metagenomes represent an unlimited resource for the discovery of novel biocatalysts from soil microorganisms. Three large-inserts metagenomic DNA libraries were constructed from different grassland soil samples and screened for genes conferring cellulase or xylanase activity. Function-driven screening identified a novel cellulase-encoding gene (cel01) and two xylanase-encoding genes (xyn01 and xyn02). From sequence and protein domain analyses, Cel01 (831 amino acids) belongs to glycoside hydrolase family 9 whereas Xyn01 (170 amino acids) and Xyn02 (255 amino acids) are members of glycoside hydrolase family 11. Cel01 harbors a family 9 carbohydrate-binding module, previously found only in xylanases....</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5527557</comments>
            <pubDate>Wed, 21 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5527557</guid>        </item>
        <item>
            <title>Ber e 1 protein: the versatile major allergen from Brazil nut seeds.</title>
            <link>http://www.medworm.com/index.php?rid=5527556&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22187079%26dopt%3DAbstract</link>
            <description>Authors: Alcocer M, Rundqvist L, Larsson G
    Abstract
    Due mainly to its extremely high content of sulphur amino acids, Ber e 1 protein, the major allergen from Brazil nut, has attracted much scientific and press attention. Ber e 1 was the main target protein in early biotechnology transgenic work, in early processing studies of plant storage proteins, in plant vacuolar targeting studies and as the main protein in early nutritional supplementation experiments. Ber e 1 was also one of the first food allergens to be unintentionally transferred from one plant to another and was involved in the first reported case of systemic allergic reaction caused by a food allergen transferred in semen. In this review, many of the Ber e 1 unique biotechnological and structural functions are discussed ...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5527556</comments>
            <pubDate>Wed, 21 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5527556</guid>        </item>
        <item>
            <title>Patch oligodeoxynucleotide synthesis (POS): a novel method for synthesis of long DNA sequences and full-length genes.</title>
            <link>http://www.medworm.com/index.php?rid=5527555&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22187080%26dopt%3DAbstract</link>
            <description>Authors: Yang G, Wang S, Wei H, Ping J, Liu J, Xu L, Zhang W
    Abstract
    Synthesis of long DNA fragments is often associated with mutations and requires multiple DNA manipulation steps. A novel DNA synthesis method, referred to as patch oligodeoxynucleotide synthesis (POS) to assembly long DNA fragments is presented here. This method involves connection of two types of oligodeoxynucleotides: long constructional oligonucleotides (COs) and short patch oligonucleotides (POs). Long COs were connected by a ligase with the aid of POs, which were complementary to both adjacent COs to help remove secondary structures during assembly. The partial double-stranded DNA template that was formed was then amplified by PCR. Accordingly, we synthesized SV40 polyadenylation signal sequences (187Â bp), ...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5527555</comments>
            <pubDate>Wed, 21 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5527555</guid>        </item>
        <item>
            <title>Riboflavin production by Ashbya gossypii.</title>
            <link>http://www.medworm.com/index.php?rid=5527554&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22187081%26dopt%3DAbstract</link>
            <description>Authors: Kato T, Park EY
    Abstract
    Riboflavin is an important nutrient for humans and animals. Industrial production has shifted completely from chemical synthesis to microbial fermentation. First generation riboflavin production was improved by a combination of traditional mutagenesis and genetic engineering, and isolated strains have been used in industry. As the DNA genome of riboflavin producers has the potential to reveal new technologies, DNA microarray, proteomic and metabolic analyses have been applied to the analysis of hyper-riboflavin producers. In this review, disparity mutagenesis technology is introduced as a means of improving riboflavin production by Ashbya gossypii. DNA microarray, proteomic and metabolic analyses of this high riboflavin producer are discussed, as w...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5527554</comments>
            <pubDate>Wed, 21 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5527554</guid>        </item>
        <item>
            <title>Endospore production allows using spray-drying as a possible formulation system of the biocontrol agent Bacillus subtilis CPA-8.</title>
            <link>http://www.medworm.com/index.php?rid=5527553&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22187082%26dopt%3DAbstract</link>
            <description>Authors: YÃ¡nez-Mendizabal V, ViÃ±as I, Usall J, CaÃ±amÃ¡s T, TeixidÃ³ N
    Abstract
    The role of endospore production by Bacillus subtilis CPA-8 on survival during spray-drying was investigated by comparison with a non-spore-forming biocontrol agent Pantoea agglomerans CPA-2. Endospore formation promoted heat resistance in CPA-8 depending on growth time (72Â h cultures were more resistant than 24Â h ones). The survival of CPA-8 and CPA-2 after spray-drying was determined after being grown in optimised media for 24 and 72Â h. Spray-dried 72Â h CPA-8 had the best survival (32%), while CPA-2 viability was less than 2%. CPA-8 survival directly related with its ability to produce endospores. Spray-dried CPA-8 reduced Monilinia fructicola conidia germination similarly to fresh cells, demons...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5527553</comments>
            <pubDate>Wed, 21 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5527553</guid>        </item>
        <item>
            <title>Secretory production of cell wall components by Saccharomyces cerevisiae protoplasts in static liquid culture.</title>
            <link>http://www.medworm.com/index.php?rid=5527562&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22170509%26dopt%3DAbstract</link>
            <description>Authors: Aoyagi H, Ishizaka M, Tanaka H
    Abstract
    When protoplasts of Saccharomyces cerevisiae T7 and IFO 0309 are cultured in a static liquid culture at 2.5Â Ã—Â 10(6) protoplasts/ml, cell wall regeneration does not occur and cell wall components (CWC) are released into the culture broth. By using a specialized fluorometer, the concentrations of CWC could be measured on the basis of the fluorescence intensity of the CWC after staining with Fluostain I. The inoculum concentration, pH, and osmotic pressure of the medium were important factors for the production of CWC in culture. Under optimal culture conditions, S. cerevisiae T7 protoplasts produced 0.91Â mg/ml CWC after 24Â h. The CWC induced the tumor necrosis factor-Î± production about 1.3 times higher than that of the commercial...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5527562</comments>
            <pubDate>Thu, 15 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5527562</guid>        </item>
        <item>
            <title>Structural determination and chemical esterification of the sophorolipids produced by Candida bombicola grown on glucose and Î±-linolenic acid.</title>
            <link>http://www.medworm.com/index.php?rid=5527563&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22167634%26dopt%3DAbstract</link>
            <description>Authors: Gupta R, Prabhune AA
    Abstract
    The extracellular surface-active glycolipids produced by the yeast, Candida bombicola when grown on glucose and Î±-linolenic acid, were analyzed by HPLC with electro-spray ionization (ESI-MS) and collision-induced dissociation mass spectrometry. The analysis confirmed that the sophorolipid (SL) mixture contained three different forms of C18:3 SL molecules: free acid, lactone and a diacetylated lactone, which has not been reported previously. Also a minor amount of diacetylated lactone form of C18:1 SL was detected. Further, the SL mixture was subjected to chemical esterification reaction with sodium methoxide. The reaction product was analyzed with ESI-MS and confirmed to be the single homogenous esterified product containing C18:3 moieties in...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5527563</comments>
            <pubDate>Wed, 14 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5527563</guid>        </item>
        <item>
            <title>High-level expression and characterization of a highly thermostable chitosanase from Aspergillus fumigatus in Pichia pastoris.</title>
            <link>http://www.medworm.com/index.php?rid=5527572&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22160328%26dopt%3DAbstract</link>
            <description>Authors: Chen X, Zhai C, Kang L, Li C, Yan H, Zhou Y, Yu X, Ma L
    Abstract
    The sequence of an endo-chitosanase gene (CSN) from Aspergillus fumigatus was optimized based on the preferred codons of Pichia pastoris and synthesized in vitro through overlapping PCR (CSN-P). The gene was cloned into a yeast expression vector, pHBM905A, and secretorily expressed in Pichia pastoris GS115. The yield of CSN-P reached ~3Â mg/ml with a high-density fermentation in a 14Â l fermenter and the enzyme activity was ~25,000Â U/ml. The enzyme had half-lives of 2.5Â h at 80Â°C, 1Â h at 90Â°C and 32Â min at 100Â°C. It retained 70% activity after incubation with 10Â M urea at room temperature for 30Â min. This enzyme was used for a large-scale preparation of oligosaccharides: 3Â g enzyme converted 200Â kg...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5527572</comments>
            <pubDate>Sun, 11 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5527572</guid>        </item>
        <item>
            <title>Development and structure of a novel barrier membrane composed of drug-loaded poly(lactic-co-glycolic acid) particles for guided bone regeneration.</title>
            <link>http://www.medworm.com/index.php?rid=5527571&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22160329%26dopt%3DAbstract</link>
            <description>Authors: Son JS, Kim SG, Jin SC, Piao ZG, Lee SY, Oh JS, Kim CS, Kim BH, Jeong MA
    Abstract
    A novel barrier membrane composed of poly(lactic-co-glycolic acid) particles loaded with dexamethasone (DEX) as a bioactive molecule was produced via a modified nanoprecipitation method without any mixing. The particle membranes had a bilayer structure: one side was smooth and had a compact surface that was connected to larger particles, while the opposite side was rough, porous and connected to smaller particles. Additionally, a cross-section of the particle membrane had a porous structure with nano and micro sized irregular pores. Process optimization revealed that NaCl concentration in the water phase, with acetone as solvent and water as a non-solvent, played critical roles in determining...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5527571</comments>
            <pubDate>Sun, 11 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5527571</guid>        </item>
        <item>
            <title>Fed-batch versus batch cultures of Yarrowia lipolytica for Î³-decalactone production from methyl ricinoleate.</title>
            <link>http://www.medworm.com/index.php?rid=5527570&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22160330%26dopt%3DAbstract</link>
            <description>Authors: Gomes N, Teixeira JA, Belo I
    Abstract
    Constant medium feeding rate and intermittent fed-batch fermentation strategies were investigated aiming to increase the yields of Î³-decalactone production by Yarrowia lipolytica, using methyl ricinoleate as substrate and ricinoleic acid source. The accumulation of another compound, 3-hydroxy-Î³-decalactone, was also analyzed since it derives from the direct precursor of Î³-decalactone thereby providing information about the enzymatic activities of the pathway. Both strategies were compared with the traditional batch mode in terms of overall productivity and yield in respect to the substrate. Although the productivity of Î³-decalactone was considerably higher in the batch mode (168Â mgÂ l(-1)Â h(-1)), substrate conversion to lactone (...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5527570</comments>
            <pubDate>Sun, 11 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5527570</guid>        </item>
        <item>
            <title>Extracellular protease in Actinomycetes culture supernatants inhibits and detaches Staphylococcus                   aureus biofilm formation.</title>
            <link>http://www.medworm.com/index.php?rid=5527569&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22160331%26dopt%3DAbstract</link>
            <description>This study suggests that protease treatment could be a feasible tool to reduce and eradicate S. aureus biofilms.
    PMID: 22160331 [PubMed - as supplied by publisher] (Source: Biotechnology Letters)</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5527569</comments>
            <pubDate>Sun, 11 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5527569</guid>        </item>
        <item>
            <title>Examining the feasibility of bulk commodity production in Escherichia coli.</title>
            <link>http://www.medworm.com/index.php?rid=5527574&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22160295%26dopt%3DAbstract</link>
            <description>Authors: Vickers CE, Klein-Marcuschamer D, KrÃ¶mer JO
    Abstract
    Escherichia coli is currently used by many research institutions and companies around the world as a platform organism for the development of bio-based production processes for bulk biochemicals. A given bulk biochemical bioprocess must be economically competitive with current production routes. Ideally the viability of each bioprocess should be evaluated prior to commencing research, both by metabolic network analysis (to determine the maximum theoretical yield of a given biocatalyst) and by techno-economic analysis (TEA; to determine the conditions required to make the bioprocess cost-competitive). However, these steps are rarely performed. Here we examine theoretical yields and review available TEA for bulk biochemic...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5527574</comments>
            <pubDate>Sat, 10 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5527574</guid>        </item>
        <item>
            <title>Increase in pectin deposition by overexpression of an ERF gene in cultured cells of Arabidopsis thaliana.</title>
            <link>http://www.medworm.com/index.php?rid=5527573&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22160296%26dopt%3DAbstract</link>
            <description>Authors: Nakano T, Naito Y, Kakegawa K, Ohtsuki N, Tsujimoto-Inui Y, Shinshi H, Suzuki K
    Abstract
    Ethylene-responsive transcription factor (ERF) family genes, which are involved in regulation of metabolic pathways and/or are useful for metabolic engineering, were investigated in the cultured cells of Arabidopsis thaliana. The pectin content in the gelatinous precipitates after the ethanol precipitation of extracts derived from calli of a transgenic cell line, A17, overexpressing an ERF gene (At1g44830), increased in comparison with the control. Expression of genes involved in pectin biosynthesis was up-regulated in the A17 calli. Overexpression of the ERF gene coordinately activates the pectin biosynthetic pathway genes and increases the content of pectin. These results therefore w...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5527573</comments>
            <pubDate>Sat, 10 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5527573</guid>        </item>
        <item>
            <title>Mining of miRNAs and potential targets from gene oriented clusters of transcripts sequences of the anti-malarial plant, Artemisia annua.</title>
            <link>http://www.medworm.com/index.php?rid=5527568&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22160362%26dopt%3DAbstract</link>
            <description>Authors: PÃ©rez-Quintero AL, Sablok G, Tatarinova TV, Conesa A, Kuo J, LÃ³pez C
    Abstract
    miRNAs involved in the biosynthesis of artemisinin, an anti-malarial compound form the plant Artemisia annua, have been identified using computational approaches to find conserved pre-miRNAs in available A. annua UniGene collections. Eleven pre-miRNAs were found from nine families. Targets predicted for these miRNAs were mainly transcription factors for conserved miRNAs. No target genes involved in artemisinin biosynthesis were found. However, miR390 was predicted to target a gene involved in the trichome development, which is the site of synthesis of artemisinin and could be a candidate for genetic transformation aiming to increase the content of artemisinin. Phylogenetic analyses were carried...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5527568</comments>
            <pubDate>Fri, 09 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5527568</guid>        </item>
        <item>
            <title>Fibroblast growth factor 2-functionalized collagen matrices for skeletal muscle tissue engineering.</title>
            <link>http://www.medworm.com/index.php?rid=5527567&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22160363%26dopt%3DAbstract</link>
            <description>Authors: Yun YR, Lee S, Jeon E, Kang W, Kim KH, Kim HW, Jang JH
    Abstract
    Fibroblast growth factor 2 (FGF2) protein plays important roles in wound healing and tissue regeneration. Collagen is clinically used for wound care applications. We investigated the potential value of FGF2-functionalized collagen matrices for skeletal muscle tissue engineering. When C2C12 cells were treated with FGF2, cell adhesion increased after 3 and 5Â days compared to the control (PÂ &amp;lt;Â 0.05). Wound healing activity of FGF2 was slightly higher than the control through cell migration. Cell proliferation activity of FGF2-functionalized collagen matrices on C2C12 cells also increased. Taken together, FGF2 stimulated C2C12 myoblast growth by promoting cell adhesion, proliferation and wound healing activit...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5527567</comments>
            <pubDate>Fri, 09 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5527567</guid>        </item>
        <item>
            <title>Application of PVA-derived porous media to accelerate biodegradation (composting) of organic solid substrates.</title>
            <link>http://www.medworm.com/index.php?rid=5527566&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22160365%26dopt%3DAbstract</link>
            <description>Authors: Chang HD, Chen CY
    Abstract
    Poly(vinyl alcohol) (PVA)-derived cubes with fine pores and high water-binding and microbial adhesion capacities, enhanced the biodegradation of organic solid substrates with the temperature of the mixture increasing to over 65Â°C on the second day and being maintained ~60Â°C for the following 3Â days, averaging at least 15Â°C higher than the control. The amount of CO(2) evolved also reflected a higher level of biodegradation. The compost made with PVA porous cubes for 2Â weeks improved lettuce cultivation and crop losses decreased by at least 10% compared with the control. Thus PVA porous cubes can facilitate the production of mature compost for plants.
    PMID: 22160365 [PubMed - as supplied by publisher] (Source: Biotechnology Letters)</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5527566</comments>
            <pubDate>Fri, 09 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5527566</guid>        </item>
        <item>
            <title>Enhancing acid tolerance of Leuconostoc mesenteroides with glutathione.</title>
            <link>http://www.medworm.com/index.php?rid=5527565&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22160366%26dopt%3DAbstract</link>
            <description>Authors: Kim JE, Eom HJ, Kim Y, Ahn JE, Kim JH, Han NS
    Abstract
    Leuconostoc mesenteroides is a commercially important lactic acid bacterium currently used as a starter for kimchi and kefir. However, its sensitivity to acid stress limits its performance. L. mesenteroides was grown in a medium supplemented with 3.2 or 6.4Â mM glutathione (GSH), and cell survival rates were measured during a long-term mild acid challenge (pH 4.0). As a result, GSH was imported by the cells and protected against acid stress; thereafter it was consumed as a nutrient. Acid stress resistance of starter cultures of this bacterium can thus be improved by cultivating it in media supplemented with GSH.
    PMID: 22160366 [PubMed - as supplied by publisher] (Source: Biotechnology Letters)</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5527565</comments>
            <pubDate>Fri, 09 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5527565</guid>        </item>
        <item>
            <title>Polyamines increase carpospore output and growth during in vitro cultivation of Hydropuntia cornea.</title>
            <link>http://www.medworm.com/index.php?rid=5527564&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22160367%26dopt%3DAbstract</link>
            <description>Authors: GuzmÃ¡n-UriÃ³stegui A, Robaina R, Freile-PelegrÃ­n Y, Robledo D
    Abstract
    Carpospore output and development in the marine red alga Hydropuntia cornea J. Agardh. were increased by adding polyamines (PAs) (putrescine, spermidine and spermine) singly or in combinations at 10(-9), 10(-6) and 10(-3)Â M. Cell divisions after spore release and development of apical axis between 17 and 21Â days characterized carpospore development. PAs increased carpospore development by promoting cell divisions to form cell masses between day 2 and 3. Morphogenesis to develop apical axes occurred at day 7. Spermine at 10(-6)Â M and a combination of putrescine 10(-9)Â MÂ +Â spermidine 10(-9)Â MÂ +Â spermine 10(-9)Â M gave a higher number of carpospores and enhanced their further development to spor...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5527564</comments>
            <pubDate>Fri, 09 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5527564</guid>        </item>
        <item>
            <title>Use of the Cre-loxP recombination system as an estimate for Agrobacterium-mediated co-transformation of tobacco leaves.</title>
            <link>http://www.medworm.com/index.php?rid=5472944&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22130741%26dopt%3DAbstract</link>
            <description>Authors: Liang MT, Yang CP, Xie ZP, Staehelin C
    Abstract
    Agrobacterium           tumefaciens-mediated transformation of tobacco leaves (Nicotiana tabacum) is used to study gene expression in a heterologous genetic background. Here, the Cre-loxP recombination system was used to detect T-DNA transfer by two A. tumefaciens cells harboring different binary vectors. Cre, under the control of the CaMV 35S promoter, was cloned into one vector, and a loxP cassette into another vector. A mixture of A.           tumefaciens, in which each cell contained either a Cre- or loxP-vector, was co-infiltrated into tobacco leaves. After two days, excision of loxP-flanked DNA was detected by PCR and used as an estimate for co-transformation events. Strongest excision (&amp;gt;Â 50%) was observed when the ...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5472944</comments>
            <pubDate>Thu, 01 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5472944</guid>        </item>
        <item>
            <title>Production of p-acetaminophenol by whole-cell catalysis using Escherichia coli overexpressing bacterial aryl acylamidase.</title>
            <link>http://www.medworm.com/index.php?rid=5472943&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22130742%26dopt%3DAbstract</link>
            <description>Authors: Ko HJ, Bang WG, Kim KH, Choi IG
    Abstract
    Aryl acylamidase (EC 3.5.1.13, AAA) acts on the amide bond between aryl and acyl groups. Whole cells of Escherichia coli overexpressing a novel bacterial AAA synthesized p-acetaminophenol (p-AAP) from p-aminophenol (p-AP, aryl compound) and acetate (acyl donor). Optimum conditions were pH 5.5 and 35Â°C with 100Â mM p-AP and 600Â mM sodium acetate in 100Â mM sodium phosphate buffer including 1% (v/v) Triton X-100 for 60Â h. 13.1Â g p-AAP l(-1) was produced with a conversion yield of 87%.
    PMID: 22130742 [PubMed - as supplied by publisher] (Source: Biotechnology Letters)</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5472943</comments>
            <pubDate>Thu, 01 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5472943</guid>        </item>
        <item>
            <title>Overexpression of alfalfa mitochondrial HSP23 in prokaryotic and eukaryotic model systems confers enhanced tolerance to salinity and arsenic stress.</title>
            <link>http://www.medworm.com/index.php?rid=5472946&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22127759%26dopt%3DAbstract</link>
            <description>Authors: Lee KW, Cha JY, Kim KH, Kim YG, Lee BH, Lee SH
    Abstract
    The cloning and characterization of a gene (MsHSP23) coding for a heat shock protein in alfalfa in a prokaryotic and model plant system is described. MsHSP23 contains a 633Â bp ORF encoding a polypeptide of 213 amino acids and exhibits greater sequence similarity to mitochondrial sHSPs from dicotyledons than to those from monocotyledons. When expressed in bacteria, recombinant MsHSP23 conferred tolerance to salinity and arsenic stress. Furthermore, MsHSP23 was cloned in a plant expressing vector and transformed into tobacco, a eukaryotic model organism. The transgenic plants exhibited enhanced tolerance to salinity and arsenic stress under ex vitro conditions. In comparison to wild type plants, the transgenic plants e...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5472946</comments>
            <pubDate>Wed, 30 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5472946</guid>        </item>
        <item>
            <title>Reduced glutamine concentration improves protein production in growth-arrested CHO-DG44 and HEK-293E cells.</title>
            <link>http://www.medworm.com/index.php?rid=5472945&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22127760%26dopt%3DAbstract</link>
            <description>Authors: Rajendra Y, Kiseljak D, Baldi L, Hacker DL, Wurm FM
    Abstract
    For most cultivated mammalian cells, glutamine is an essential medium component. However, glutamine consumption results in the production of ammonia, a cytotoxic byproduct. Here we investigated the effect of glutamine reduction on recombinant protein production and ammonia accumulation in transiently transfected CHO and HEK-293E cells maintained under conditions of growth arrest. Maximum transient recombinant protein yields were observed in HEK-293E cultures without glutamine and in CHO cultures with 2Â mM glutamine. The initial concentration of glutamine correlated with the level of ammonia accumulation in each culture. For both a stable CHO-derived cell line and a polyclonal population of recombinant CHO cells ...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5472945</comments>
            <pubDate>Wed, 30 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5472945</guid>        </item>
        <item>
            <title>Glycosylation of various flavonoids by recombinant oleandomycin glycosyltransferase from Streptomyces antibioticus in batch and repeated batch modes.</title>
            <link>http://www.medworm.com/index.php?rid=5472947&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22116386%26dopt%3DAbstract</link>
            <description>Authors: Choi SH, Ryu M, Yoon YJ, Kim DM, Lee EY
    Abstract
    An oleandomycin glycosyltransferase (OleD GT) gene from Streptomyces antibioticus was functionally expressed in Escherichia coli BL21 (DE3) with various molecular chaperones. The purified recombinant OleD GT catalyzed glycosylation of various flavonoids: apigenin, chrysin, daidzein, genistein, kaempferol, luteolin, 4-methylumbelliferone, naringenin, quercetin and resveratrol with UDP-glucose. 4.6Â Î¼g OleD GT was readily immobilized onto 1Â mg hybrid nanoparticles of Fe(3)O(4)/silica/NiO on the basis of the affinity between His-tag and NiO nanoparticles with retention of 90% activity. In batch reaction, more than 90% naringenin (20Â Î¼M) was converted to its glycoside in 5Â h. The immobilized OleD GT was efficiently reused f...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5472947</comments>
            <pubDate>Fri, 25 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5472947</guid>        </item>
        <item>
            <title>Enhancement of rutin in Fagopyrum esculentum hairy root cultures by the Arabidopsis transcription factor AtMYB12.</title>
            <link>http://www.medworm.com/index.php?rid=5472948&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22113884%26dopt%3DAbstract</link>
            <description>Authors: Park NI, Li X, Thwe AA, Lee SY, Kim SG, Wu Q, Park SU
    Abstract
    Common buckwheat (Fagopyrum esculentum Moench) is rich in phenolic compounds and may be useful for the treatment of metabolic syndrome in humans. To improve the production of rutin in buckwheat, we overexpressed the flavonol-specific transcription factor, AtMYB12 using Agrobacterium rhizogenes into hairy root culture systems. This induced the expression of flavonoid biosynthetic genes encoding phenylalanine ammonia lyase, cinnamate 4-hydroxylase, 4-coumarate:CoA ligase, chalcone synthase, chalcone isomerase, flavone 3-hydroxylase, flavonoid 3'-hydroxylase, and flavonol synthase. This led to the accumulation of rutin in buckwheat hairy roots up to 0.9Â mg/g dry wt. PAP1 expression, however, did not correlate wit...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5472948</comments>
            <pubDate>Thu, 24 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5472948</guid>        </item>
        <item>
            <title>Over-expression of pcvA involved in vesicle-vacuolar fusion affects the conidiation and penicillin production in Penicillium chrysogenum.</title>
            <link>http://www.medworm.com/index.php?rid=5472952&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22109934%26dopt%3DAbstract</link>
            <description>Authors: Xu X, Yang J, An Y, Pan Y, Liu G
    Abstract
    Rab GTPase is required for vesicle-vacuolar fusion during the vacuolar biogenesis in fungi. Rab GTPase-encoding gene, pcvA, was cloned from Penicillium chrysogenum: it contained five introns and its predicted protein contained the conserved Rab GTPase domain involved in GTP-binding and hydrolysis. Over-expression of pcvA significantly stimulated the vesicle-vacuolar fusion but repressed the conidiation and decreased conidial tolerance against thermal stress. Penicillin production was decreased in the pcvA over-expressed strain suggesting that pcvA is involved in vesicle-vacuolar fusion participates in the penicillin biosynthesis in P. chrysogenum.
    PMID: 22109934 [PubMed - as supplied by publisher] (Source: Biotechnology Letters...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5472952</comments>
            <pubDate>Wed, 23 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5472952</guid>        </item>
        <item>
            <title>Improved cardenolide production in Calotropis gigantea hairy roots using mechanical wounding and elicitation.</title>
            <link>http://www.medworm.com/index.php?rid=5472951&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22109935%26dopt%3DAbstract</link>
            <description>Authors: Sun J, Xiao J, Wang X, Yuan X, Zhao B
    Abstract
    A hairy root culture system of Calotropis gigantea was established and effects of mechanical wounding (MW) and elicitors [methyl jasmonate (MJ), yeast extract (YE) and chitosan (CS)] on cardenolide production were investigated. All treatments stimulated the production of cardenolide in hairy root cultures of C. gigantea. CS was the most effective elicitor, followed by MJ. YE and MW also improved cardenolide yield in individual treatments. The highest cardenolide yield (1,050Â Â±Â 55Â mg/l) was obtained after adding 50Â mg CS/l for 20Â days, which was 2.7-fold higher than the control.
    PMID: 22109935 [PubMed - as supplied by publisher] (Source: Biotechnology Letters)</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5472951</comments>
            <pubDate>Wed, 23 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5472951</guid>        </item>
        <item>
            <title>A strong promoter, PMagpd, provides a tool for high gene expression in entomopathogenic fungus, Metarhizium acridum.</title>
            <link>http://www.medworm.com/index.php?rid=5472950&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22109936%26dopt%3DAbstract</link>
            <description>This study provides an applicable promoter for over-expression of target genes in M. acridum.
    PMID: 22109936 [PubMed - as supplied by publisher] (Source: Biotechnology Letters)</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5472950</comments>
            <pubDate>Wed, 23 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5472950</guid>        </item>
        <item>
            <title>Enhancement of anthraquinone production in Morinda citrifolia cell suspension cultures after stimulation of the proline cycle with two proline analogs.</title>
            <link>http://www.medworm.com/index.php?rid=5472949&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22109937%26dopt%3DAbstract</link>
            <description>Authors: Quevedo CV, Perassolo M, Giulietti AM, Talou JR
    Abstract
    Synthesis of anthraquinones (AQs) involves the shikimate and 2-C-methyl-D-erythritol 4-phosphate pathways. The proline cycle is linked to the pentose phosphate pathway (PPP) to generate NADPH needed in the first steps of this pathway. The effect of two proline analogs, azetidine-2-carboxylic acid (A2C) and thiazolidine-4-carboxylic acid (T4C), were evaluated in Morinda citrifolia suspension cultures. Both analogs gave higher proline accumulation after 6 and 10Â days (68 and 179% after 6Â days with A2C at 25 and 50Â Î¼M, respectively, and 111% with T4C added at 100Â Î¼M). Induction of the proline cycle increased the AQ content after 6Â days (~40% for 50Â Î¼M A2C and 100Â Î¼M T4C). Whereas A2C (50Â Î¼M) increased only ...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5472949</comments>
            <pubDate>Wed, 23 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5472949</guid>        </item>
        <item>
            <title>Metabolic engineering of Escherichia coli for 1-butanol biosynthesis through the inverted aerobic fatty acid Î²-oxidation pathway.</title>
            <link>http://www.medworm.com/index.php?rid=5472958&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22105550%26dopt%3DAbstract</link>
            <description>Authors: Gulevich AY, Skorokhodova AY, Sukhozhenko AV, Shakulov RS, Debabov VG
    Abstract
    The basic reactions of the clostridial 1-butanol biosynthesis pathway can be regarded to be the inverted reactions of the fatty acid Î²-oxidation pathway. A pathway for the biosynthesis of fuels and chemicals was recently engineered by combining enzymes from both aerobic and anaerobic fatty acid Î²-oxidation as well as enzymes from other metabolic pathways. In the current study, we demonstrate the inversion of the entire aerobic fatty acid Î²-oxidation cycle for 1-butanol biosynthesis. The constructed markerless and plasmidless Escherichia coli strain BOX-3 (MG1655 lacI           (             Q           )           attB-P(             trc-ideal-4)-SD(Ï†10)-adhE(Glu568Lys) attB-P(             t...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5472958</comments>
            <pubDate>Tue, 22 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5472958</guid>        </item>
        <item>
            <title>Correlation of antibody production rate with glucose and lactate metabolism in Chinese hamster ovary cells.</title>
            <link>http://www.medworm.com/index.php?rid=5472957&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22105551%26dopt%3DAbstract</link>
            <description>Authors: Chen F, Ye Z, Zhao L, Liu X, Fan L, Tan WS
    Abstract
    A linear relationship was found between the antibody production rate (q           (mAb)) and the glucose and lactate consumption rate (q           (GL)) in Chinese hamster ovary cells. Under a series of q           (mAb)-perturbing conditions, q           (GL) was determined and a linear relationship between q           (mAb) and q           (GL) was further established (R           (             2           )Â =Â 0.914). Mitochondrial dehydrogenase activity was monitored in all the q           (mAb)-perturbing conditions and showed a linear correlation with q           (GL) (R           (2)Â =Â 0.874) as well as with q           (mAb). Taken collectively, our results establish that the metabolic parameter, q           (G...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5472957</comments>
            <pubDate>Tue, 22 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5472957</guid>        </item>
        <item>
            <title>Establishment and characterization of outer root sheath (ORS) cell line from Jining grey goat.</title>
            <link>http://www.medworm.com/index.php?rid=5472956&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22105552%26dopt%3DAbstract</link>
            <description>Authors: Cui Z, Hu Y, Wang H, Zeng Y, Dong B, Zhu H, Dong Z, Liu Z
    Abstract
    A new line of outer root sheath (ORS) cells was established from hair follicles of Jining grey goat by using a mechanical separation combined with enzyme digestion. Cell morphology is described at different phases. The chromosome analysis of ORS cells, identification of the ORS cells and morphological reversion test were detected at the 4th and 40th passages. The ORS cells were healthy and the growth characteristics were stable with a population doubling time of 52Â h. Chromosome analysis showed that &amp;gt;58% of cells were diploid. Test for ORS cell line CK19 expression was positive. This newly established ORS cell line not only lays the foundation for further studying on the growth, regeneration, developmen...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5472956</comments>
            <pubDate>Tue, 22 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5472956</guid>        </item>
        <item>
            <title>Mutations in isocitrate dehydrogenase 2 accelerate glioma cell migration via matrix metalloproteinase-2 and 9.</title>
            <link>http://www.medworm.com/index.php?rid=5472955&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22105553%26dopt%3DAbstract</link>
            <description>Authors: Fu Y, Zheng Y, Li K, Huang R, Zheng S, An N, Liang A
    Abstract
    The gene encoding isocitrate dehydrogenase (IDH) is somatically mutated predominantly in secondary glioblastoma multiforme. Glioma-specific mutations in IDH1 always produced a single amino acid substitution at R132, but mutations in IDH2 were exclusively at R172 which was the analogous site to R132 in IDH1. Mutations of IDH1 and IDH2 led to simultaneous loss and gain of activities in the production of Î±-ketoglutarate and 2-hydroxyglutarate, respectively. Matrix metalloproteinases (MMPs) are zinc-dependent endoproteinases involved in the degradation of the extracellular matrix. The exact role of IDH2 mutant on MMPs activity and cell migration has not been fully studied. Here, we show that in response to IDH2 mut...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5472955</comments>
            <pubDate>Tue, 22 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5472955</guid>        </item>
        <item>
            <title>Efficient COD removal and nitrification in an upflow microaerobic sludge blanket reactor for domestic wastewater.</title>
            <link>http://www.medworm.com/index.php?rid=5472954&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22105554%26dopt%3DAbstract</link>
            <description>Authors: Zheng S, Cui C
    Abstract
    The treatment performance of an upflow microaerobic sludge blanket reactor (UMSB) for synthetic domestic wastewater was investigated at two dissolved oxygen (DO) levels, 0.3-0.5 and 0.7-0.9Â mgÂ l(-1), focusing on nitrification performance. The higher DO level induced complete nitrification of ammonia nitrogen (NH(3)-N), achieving chemical oxygen demand and NH(3)-N removals of 97 and 92%, respectively. There were consistently significantly higher nitrate nitrogen (NO(3)-N) and nitrite nitrogen (NO(2)-N) levels in the effluent, with ~66% of newly-produced oxidised nitrogen as NO(2)-N. Despite the high nitrification efficiency, only about 23% of the removed NH(3)-N amount from the influent was ultimately transformed into oxidised nitrogen due to the s...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5472954</comments>
            <pubDate>Tue, 22 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5472954</guid>        </item>
        <item>
            <title>Vector-mediated chromosomal integration of the glutamate decarboxylase gene in Streptococcus thermophilus.</title>
            <link>http://www.medworm.com/index.php?rid=5472953&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22105555%26dopt%3DAbstract</link>
            <description>Authors: Renye JA, Somkuti GA
    Abstract
    The integrative vector, pINTRS, was used to transfer glutamate decarboxylase (GAD) activity to Streptococcus thermophilus ST128 thereby allowing for the production of Î³-aminobutyric acid (GABA). In pINTRS, the gene encoding glutamate decarboxylase, gadB, was flanked by DNA fragments homologous to a S. thermophilus pseudogene to allow for integration at a non-essential locus on the chromosome. Screening techniques confirmed the insertion of gadB with either its endogenous promoter or the S. thermophilus P2201 promoter, resulting in the generation of recombinant strains, ST128/gadB or ST128/P2201-gadB. Following the integration event unwanted plasmid DNA, specifically the erythromycin resistance gene, was eliminated from the recombinant strains...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5472953</comments>
            <pubDate>Tue, 22 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5472953</guid>        </item>
        <item>
            <title>Biobleaching of wheat straw pulp with recombinant laccase from the hyperthermophilic Thermus thermophilus.</title>
            <link>http://www.medworm.com/index.php?rid=5472975&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22102060%26dopt%3DAbstract</link>
            <description>Authors: Zheng Z, Li H, Li L, Shao W
    Abstract
    The recombinant laccase from Thermus thermophilus was applied to the biobleaching of wheat straw pulp. The best bleaching effect was when the pulp was treated with 3Â U laccaseÂ g(-1) dry pulp at 90Â°C, pH 4.5, 8% consistency for 1.5Â h. Under these conditions, the pulp brightness was increased by 3.3% ISO, and the pulp kappa number was decreased by 5.6Â U. Enzymatic treatment improved the bleachability of wheat straw pulp but caused no damage to the pulp fibers. The use of enzyme-treated pulp saved 25% H(2)O(2) consumption in subsequent peroxide bleaching without decreasing the final brightness. Pulp biobleaching in the presence of 5Â mM ABTS further increased the pulp brightness by 1.5% ISO. This is the first report on the application...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5472975</comments>
            <pubDate>Sat, 19 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5472975</guid>        </item>
        <item>
            <title>Fusion of HSA influences TNF-Î± neutralizing activity of shTNFRs.</title>
            <link>http://www.medworm.com/index.php?rid=5415228&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22083716%26dopt%3DAbstract</link>
            <description>Authors: Zhan J, Chen Y, Yuan HY, Li H, Lu H
    Abstract
    Soluble human tumor necrosis factor receptors (shTNFRI and shTNFRII) are antagonists of tumor necrosis factor-Î± (TNF-Î±) and are under clinical investigation as therapy for autoimmune diseases and transplant rejection. However, shTNFRI and shTNFRII are limited for clinical usage because of their short half-lives in vivo. Recombinant TNF-Î± receptors (infliximab and etanercept) are used in treatment of rheumatoid arthritis and Crohn's disease but are also being tested for a number of other autoimmune diseases. Human serum albumin (HSA) has been used to construct long-acting fusion proteins. Here, we report the effect of fusion of HSA with shTNFRI and with shTNFRII on shTNFR's neutralizing activity against TNF-Î±. HSA fusion prot...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5415228</comments>
            <pubDate>Tue, 15 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5415228</guid>        </item>
        <item>
            <title>Small RNA RyhB as a potential tool used for metabolic engineering in Escherichia coli.</title>
            <link>http://www.medworm.com/index.php?rid=5415227&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22083717%26dopt%3DAbstract</link>
            <description>Authors: Kang Z, Wang X, Li Y, Wang Q, Qi Q
    Abstract
    Small RNA (RyhB) was overexpressed artificially using an arabinose-inducible system in Escherichia coli and resulted in more succinate (7-fold) accumulation, which suggested that RyhB had a strong effect on sdhCDAB genes. Acetate was also increased indicating that RyhB had a comprehensive influence on glucose central metabolism. RyhB might therefore be useful for metabolic engineering of E. coli.
    PMID: 22083717 [PubMed - as supplied by publisher] (Source: Biotechnology Letters)</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5415227</comments>
            <pubDate>Tue, 15 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5415227</guid>        </item>
        <item>
            <title>Virus-binding activity of the truncated C subunit of porcine aminopeptidase N expressed in Escherichia coli.</title>
            <link>http://www.medworm.com/index.php?rid=5415226&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22083718%26dopt%3DAbstract</link>
            <description>Authors: Sun D, Shi H, Chen J, Guo D, Liu Q, He X, Bao J, Wang Y, Qiu H, Feng L
    Abstract
    Seven overlapping truncated forms of the C subunit of porcine aminopeptidase N (pAPN-C) were expressed in Escherichia coli. By western blotting and ELISA test, all recombinant proteins were recognized by the antibody against native porcine aminopeptidase N. Recombinant proteins, rpAPN-C2 (aa 623-722) and rpAPN-C3 (aa 673-772), had the highest binding activity with swine transmissible gastroenteritis virus among the truncated pAPN-C recombinant proteins. The overlapping region (aa 673-722) between rpAPN-C2 and rpAPN-C3 is indicated to play a key role in viral binding.
    PMID: 22083718 [PubMed - as supplied by publisher] (Source: Biotechnology Letters)</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5415226</comments>
            <pubDate>Tue, 15 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5415226</guid>        </item>
        <item>
            <title>NIRF, a novel ubiquitin ligase, interacts with hepatitis B virus core protein and promotes its degradation.</title>
            <link>http://www.medworm.com/index.php?rid=5415230&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22072112%26dopt%3DAbstract</link>
            <description>Authors: Qian G, Jin F, Chang L, Yang Y, Peng H, Duan C
    Abstract
    Hepatitis B virus (HBV) core protein (HBc) is a major component of viral nucleocapsid and a multifunctional protein involved in viral maturation and release. It is unstable and present in cells at low level because of K96 lysine residue, which is a ubiquitin acceptor site. Np95/ICBP90-like RING finger protein (NIRF) has auto-ubiquitination activity which is the hallmark of a ubiquitin ligase. In the present study, ubiquitin ligase, NIRF, binds to HBc and leads to the proteasome-mediated degradation of HBc in vivo. NIRF down-regulates HBc protein level, resulting in the decrease of the amount of HBV particles in supernatant of HepG2.2.15 cells. However knockdown of NIRF significantly increases endogenous HBc protein le...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5415230</comments>
            <pubDate>Thu, 10 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5415230</guid>        </item>
        <item>
            <title>Preparation of encapsulated alliinase in alginate microparticles.</title>
            <link>http://www.medworm.com/index.php?rid=5415229&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22072113%26dopt%3DAbstract</link>
            <description>Authors: Ko JA, Lee YL, Jeong HJ, Park HJ
    Abstract
    Alliinase (alkylsulphenate lyase, EC 4.4.1.4), which catalyses the production of allicin, was immobilized in alginate microparticles. Addition of pyridoxal 5'-phosphate to the microparticles enhanced alliinase activity. Encapsulated alliinase were significantly higher (30 and 22%, respectively) than those of non-encapsulated alliinase at 60Â°C and at pH 2. Therefore, microencapsulation of alliinase with alginate can offer an effective way of sustaining enzyme activity during oral administration and passage through the stomach.
    PMID: 22072113 [PubMed - as supplied by publisher] (Source: Biotechnology Letters)</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5415229</comments>
            <pubDate>Thu, 10 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5415229</guid>        </item>
        <item>
            <title>Cloning and characterization of a novel tyrosine ammonia lyase-encoding gene involved in bagremycins biosynthesis in Streptomyces sp.</title>
            <link>http://www.medworm.com/index.php?rid=5415231&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22065278%26dopt%3DAbstract</link>
            <description>Authors: Zhu Y, Liao S, Ye J, Zhang H
    Abstract
    Tyrosine ammonia lyase catalyzes the deamination of L: -tyrosine to trans-coumaric acid. A novel tyrosine ammonia lyase-encoding gene, bagA, was cloned and sequenced from bagremycins-producing strain Streptomyces sp. TÃ¼ 4128 whose protein product contains a Ala-Ser-Gly segment in the active site. The disruption of the bagA gene abolished trans-coumaric acid and bagremycins production. trans-coumaric acid restored the formation of bagremycin A in the mutant, but not bagremycin B. Thus, trans-coumaric acid is a precursor for biosynthesis of bagremycins and the bagA gene codes for tyrosine ammonia lyase to synthesize trans-coumaric acid. This is a novel bacterial tal gene reported in actinomycetes for the second time and for the first ti...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5415231</comments>
            <pubDate>Tue, 08 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5415231</guid>        </item>
        <item>
            <title>Quercetin production from rutin by a thermostable Î²-rutinosidase from Pyrococcus furiosus.</title>
            <link>http://www.medworm.com/index.php?rid=5377594&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22052256%26dopt%3DAbstract</link>
            <description>Authors: Nam HK, Hong SH, Shin KC, Oh DK
    Abstract
    Pyrococcus furiosus Î²-glucosidase converted rutin to quercetin and rutinose disaccharide with a ratio of 1:1, with no glucose, L: -rhamnose, and isoquercitrin, indicating that the enzyme is a Î²-rutinosidase. The specific activity for flavonoid glycosides followed the order of isoquercitrinÂ &amp;gt;Â quercitrinÂ &amp;gt;Â rutin. The conversion of rutin to quercetin was optimal at pH 5.0 and 95Â°C in the presence of 0.5% dimethyl sulfoxide with a half-life of 101Â h, a k           (cat) of 1.6Â min(-1), and a K           (m) of 0.3Â mM. Under the improved conditions, the enzyme produced 6.5Â mM quercetin from 10Â mM rutin after 150Â min, with a molar yield of 65% and a productivity of 2.6Â mM/h. This productivity is the highest reported th...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5377594</comments>
            <pubDate>Fri, 04 Nov 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5377594</guid>        </item>
        <item>
            <title>Construction of engineered fructosyl peptidyl oxidase for enzyme sensor applications under normal atmospheric conditions.</title>
            <link>http://www.medworm.com/index.php?rid=5377593&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22052257%26dopt%3DAbstract</link>
            <description>Authors: Kim S, Nibe E, Tsugawa W, Kojima K, Ferri S, Sode K
    Abstract
    Current enzymatic methods for the analysis of glycated proteins use flavoenzymes that catalyze the oxidative deglycation of fructosyl peptides, designated as fructosyl peptidyl oxidases (FPOXs). However, as FPOXs are oxidases, the signals derived from electron mediator-type electrochemical monitoring based on them are affected by dissolved O(2). Improvement of dye-mediated dehydrogenase activity of FPOXs and its application to enzyme electrode construction were therefore undertaken. Saturation mutagenesis study on Asn56 of FPOX from Phaeosphaeria nodorum, produced mutants with marked decreases in the catalytic ability to employ O(2) as the electron acceptor, while showing higher dye-mediated dehydrogenase activit...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5377593</comments>
            <pubDate>Fri, 04 Nov 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5377593</guid>        </item>
        <item>
            <title>High-level expression of the Penicillium notatum glucose oxidase gene in Pichia pastoris using codon optimization.</title>
            <link>http://www.medworm.com/index.php?rid=5377591&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22052258%26dopt%3DAbstract</link>
            <description>Authors: Gao Z, Li Z, Zhang Y, Huang H, Li M, Zhou L, Tang Y, Yao B, Zhang W
    Abstract
    The glucose oxidase (GOD) gene from Penicillium notatum was expressed in Pichia pastoris. The 1,815Â bp gene, god-w, encodes 604 amino acids. Recombinant GOD-w had optimal activity at 35-40Â°C and pH 6.2 and was stable, from pH 3 to 7 maintainingÂ &amp;gt;75% maximum activity after incubation at 50Â°C for 1Â h. GOD-w worked as well as commercial GODs to improve bread making. To achieve high-level expression of recombinant GOD in P. pastoris, 272 nucleotides involving 228 residues were mutated, consistent with the codon bias of P. pastoris. The optimized recombinant GOD-m yielded 615 U ml(-1) (2.5Â g protein l(-1)) in a 3Â l fermentor-410% higher than GOD-w (148 U ml(-1)), and thus is a low-cost altern...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5377591</comments>
            <pubDate>Fri, 04 Nov 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5377591</guid>        </item>
        <item>
            <title>Regioselective glucosidation of trans-resveratrol in Escherichia coli expressing glucosyltransferase from Phytolacca americana.</title>
            <link>http://www.medworm.com/index.php?rid=5377597&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22048846%26dopt%3DAbstract</link>
            <description>Authors: Ozaki SI, Imai H, Iwakiri T, Sato T, Shimoda K, Nakayama T, Hamada H
    Abstract
    A glucosyltransferase (GT) of Phytolacca americana (PaGT3) was expressed in Escherichia coli and purified for the synthesis of two O-Î²-glucoside products of trans-resveratrol. The reaction was moderately regioselective with a ratio of 4'-O-Î²-glucoside: 3-O-Î²-glucoside at 10:3. We used not only the purified enzyme but also the E. coli cells containing the PaGT3 gene for the synthesis of glycoconjugates. E. coli cell cultures also have other advantages, such as a shorter incubation time compared with cultured plant cells, no need for the addition of exogenous glucosyl donor compounds such as UDP-glucose, and almost complete conversion of the aglycone to the glucoside products. Furthermore, a hom...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5377597</comments>
            <pubDate>Thu, 03 Nov 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5377597</guid>        </item>
        <item>
            <title>Natural plant genetic engineer Agrobacterium rhizogenes: role of T-DNA in plant secondary metabolism.</title>
            <link>http://www.medworm.com/index.php?rid=5377596&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22048847%26dopt%3DAbstract</link>
            <description>Authors: Chandra S
    Abstract
    Agrobacterium           rhizogenes is a natural plant genetic engineer. It is a gram-negative soil bacterium that induces hairy root formation. Success has been obtained in exploring the molecular mechanisms of transferred DNA (T-DNA) transfer, interaction with host plant proteins, plant defense signaling and integration to plant genome for successful plant genetic transformation. T-DNA and corresponding expression of rol genes alter morphology and plant host secondary metabolism. During transformation, there is a differential loss of a few T-DNA genes. Loss of a few ORFs drastically affect the growth and morphological patterns of hairy roots, expression pattern of biosynthetic pathway genes and accumulation of specific secondary metabolites.
    PMID: 2...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5377596</comments>
            <pubDate>Thu, 03 Nov 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5377596</guid>        </item>
        <item>
            <title>Construction of multi-functional extracellular matrix proteins that inhibits migration and tube formation of endothelial cells.</title>
            <link>http://www.medworm.com/index.php?rid=5377595&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22048848%26dopt%3DAbstract</link>
            <description>Authors: Nakamura M, Mie M, Nakamura M, Kobatake E
    Abstract
    Artificial extracellular matrix (ECM) proteins have been designed that have strong cell-adhesive activity and active functional units that inhibit network formation among vascular endothelial cells. A laminin-derived sequence (YIGSR) that blocks migration of vascular endothelial cells was designed to incorporate into an elastin-derived structural unit. The designed ECM fusion protein also had a cell-adhesive RGDN sequence that conferred an intense migration-inhibitory effect. The resultant ECM showed cell-adhesive activity superior to that of the synthetic YIGSR peptide and it blocked the migration of vascular endothelial cells. Furthermore, the designed ECM inhibited the angiogenic activity of a collagen gel. The engineer...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5377595</comments>
            <pubDate>Thu, 03 Nov 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5377595</guid>        </item>
        <item>
            <title>Salt effect of nisin Z isolated from a marine fish on the growth inhibition of Streptococcus iniae, a pathogen of streptococcosis.</title>
            <link>http://www.medworm.com/index.php?rid=5377602&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22042302%26dopt%3DAbstract</link>
            <description>Authors: Heo WS, Kim EY, Kim YR, Hossain MT, Kong IS
    Abstract
    A bacteriocin-producing Lactococcus lactis subsp. lactis was isolated from the intestine of olive flounder. The bacteriocin was identified as nisin Z. It was active against Gram-positive bacteria. Nisin Z at 3,200 arbitrary units (AU) was more effective in seawater than in PBS; growth of Streptococcus iniae was completely inhibited within 3Â h. Nisin Z preparations with 3.5% (w/v) NaCl was the most effective against S. iniae being similar to nisin Z in seawater. Nisin Z is thus a good alternative to antibiotics to prevent streptococcosis caused by S. iniae aquaculture systems.
    PMID: 22042302 [PubMed - as supplied by publisher] (Source: Biotechnology Letters)</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5377602</comments>
            <pubDate>Tue, 01 Nov 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5377602</guid>        </item>
        <item>
            <title>Enhancement of pH stability and activity of glycerol dehydratase from Klebsiella pneumoniae by rational design.</title>
            <link>http://www.medworm.com/index.php?rid=5377599&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22042303%26dopt%3DAbstract</link>
            <description>Authors: Qi X, Guo Q, Wei Y, Xu H, Huang R
    Abstract
    Glycerol dehydratase (GDHt) is a key and rate-limiting enzyme in the pathway of 1,3-propanediol (1,3-PD) synthesis. The improvement of GDHt's stability and enzymatic activity is desirable for the biosynthesis of 1,3-PD. The gldABC gene encoding GDHt of Klebsiella pneumoniae was cloned and expressed in Escherichia coli XL10-Gold, and the mutation sites of GDHt were obtained through prediction by PoPMuSiC program. Consequently, two mutants (KpG60 and KpG525) were developed by rational design through site-mutagenesis based on 3D structure which was constructed from homology modeling. Analyses of enzymatic properties showed that pH stability of the mutants was about 1.25-2 times higher than that of the wild type, and specific activity...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5377599</comments>
            <pubDate>Tue, 01 Nov 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5377599</guid>        </item>
        <item>
            <title>Expression and purification of antimicrobial peptide buforin IIb in Escherichia coli.</title>
            <link>http://www.medworm.com/index.php?rid=5273916&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21735257%26dopt%3DAbstract</link>
            <description>Authors: Wang Q, Zhu F, Xin Y, Liu J, Luo L, Yin Z
    Abstract
    A novel production method in Escherichia coli for an antimicrobial peptide of 21 amino acids, buforin IIb, which is a synthetic analog of buforin II, has been developed. The buforin IIb gene was cloned into the vector pET32a to construct an expression vector pET32a-buforin IIb. The fusion protein Trx-buforin IIb, purified by nickel nitrilo-triacetic acid (Ni-NTA) resin chromatography, was cleaved by hydroxylamine hydrochloride to release recombinant buforin IIb. Purification of recombinant buforin IIb was achieved by HPLC: about 3.1Â mg/l active recombinant buforin IIb with purity &amp;gt;99% was obtained. The recombinant buforin IIb showed antimicrobial activities that were similar to the synthetic one.
    PMID: 21735257 [Pu...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5273916</comments>
            <pubDate>Mon, 03 Oct 2011 04:28:26 +0100</pubDate>
            <guid isPermaLink="false">5273916</guid>        </item>
        <item>
            <title>Over-expression of chloroperoxidase in Caldariomyces fumago.</title>
            <link>http://www.medworm.com/index.php?rid=5273915&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21735258%26dopt%3DAbstract</link>
            <description>Authors: Buchhaupt M, Ehrich K, HÃ¼ttmann S, Guder J, Schrader J
    Abstract
    The filamentous fungus Caldariomyces fumago secretes a chloroperoxidase (CPO). To increase its production, we integrated a CPO-expression cassette into the non-transcribed spacer regions of the rDNA in C. fumago. One strain was obtained that had twice the CPO activity when grown in shake-flask and bioreactor compared to the wild-type. The highest CPO activity from the bioreactor cultivation was 3,236Â UÂ ml(-1). This is the highest value reported so far.
    PMID: 21735258 [PubMed - in process] (Source: Biotechnology Letters)</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5273915</comments>
            <pubDate>Mon, 03 Oct 2011 04:28:16 +0100</pubDate>
            <guid isPermaLink="false">5273915</guid>        </item>
        <item>
            <title>The substrate binding cavity of particulate methane monooxygenase from Methylosinus trichosporium OB3b expresses high enantioselectivity for n-butane and n-pentane oxidation to 2-alcohol.</title>
            <link>http://www.medworm.com/index.php?rid=5273914&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21744144%26dopt%3DAbstract</link>
            <description>Authors: Miyaji A, Miyoshi T, Motokura K, Baba T
    Abstract
    The particulate methane monooxygenase (pMMO) of Methylosinus trichosporium OB3b oxidized n-butane and n-pentane and mainly produced (R)-2-butanol and (R)-2-pentanol that comprised 78 and 89% of the product, respectively, indicating that the pro-R hydrogen of the 2-position carbon of n-butane and n-pentane is oriented toward a catalytic site within the substrate binding site of pMMO. The protein cavity adjacent to the catalytic center for pMMO has optimum volume for recognizing n-butane and n-pentane for enantioselective hydroxylation.
    PMID: 21744144 [PubMed - in process] (Source: Biotechnology Letters)</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5273914</comments>
            <pubDate>Mon, 03 Oct 2011 04:28:06 +0100</pubDate>
            <guid isPermaLink="false">5273914</guid>        </item>
        <item>
            <title>Highly regioselective synthesis of undecylenic acid esters of purine nucleosides catalyzed by Candida antarctica lipase B.</title>
            <link>http://www.medworm.com/index.php?rid=5273913&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21744146%26dopt%3DAbstract</link>
            <description>Authors: Gao WL, Li N, Zong MH
    Abstract
    Regioselective undecylenoylation of purine nucleosides as potential dual prodrugs was achieved by Candida antarctica lipase B using adenosine as a model reactant. The optimum organic solvent, molar ratio of vinyl ester to nucleoside, enzyme dosage, reaction temperature and molecular sieve amount were anhydrous THF, 5:1, 20Â U/ml, 45Â°C and 75Â mg/ml, respectively. Under the optimum conditions, the initial reaction rate, yield and 5'-regioselectivity were 1.1Â mM/h, 90% andÂ &amp;gt;99%, respectively. The enzymatic acylation of various nucleosides furnished the desired 5'-ester derivatives with the yields of 60-95% and 5'-regioselectivities ofÂ &amp;gt;99%. In addition, the lipase displayed excellent operational stability in THF, and retained 96% of i...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5273913</comments>
            <pubDate>Mon, 03 Oct 2011 04:27:56 +0100</pubDate>
            <guid isPermaLink="false">5273913</guid>        </item>
        <item>
            <title>Biosynthetic substitution of tyrosine in green fluorescent protein with its surrogate fluorotyrosine in Escherichia coli.</title>
            <link>http://www.medworm.com/index.php?rid=5273912&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21744148%26dopt%3DAbstract</link>
            <description>Authors: Ayyadurai N, Prabhu NS, Deepankumar K, Kim A, Lee SG, Yun H
    Abstract
    Introduction of a fluorine moiety into green fluorescent protein offers an interesting novel spectral variant. The calculated binding energy of fluorotyrosine (F-Tyr) (-8.42Â kcal/mol) for tyrosyl tRNA synthetase was moderately higher than that of tyrosine (Tyr) (-8.36Â kcal/mol). This result directly correlated with the expression level of F-Tyr containing GFP (38Â mg/l), which was comparably higher than that of the parent GFP expression level (34Â mg/l). Finally, we generated a model structure for GFP to assess possible interaction in the chromophore of the protein structure, which plays an important role in determining the spectral and folding behaviors of the F-Tyr incorporated GFP variant.
    PMID: ...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5273912</comments>
            <pubDate>Mon, 03 Oct 2011 04:27:45 +0100</pubDate>
            <guid isPermaLink="false">5273912</guid>        </item>
        <item>
            <title>Polysaccharides purified from the submerged culture of Ganoderma formosanum stimulate macrophage activation and protect mice against Listeria monocytogenes infection.</title>
            <link>http://www.medworm.com/index.php?rid=5273911&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21744272%26dopt%3DAbstract</link>
            <description>Authors: Wang CL, Pi CC, Kuo CW, Zhuang YJ, Khoo KH, Liu WH, Chen CJ
    Abstract
    The bioactive components of Ganoderma formosanum have not yet been characterized. We investigated the immunomodulatory activities of the extracellular polysaccharides produced from a submerged mycelial culture of G. formosanum. The polysaccharides were mainly composed of D: -mannose, D: -galactose and D: -glucose. After gel filtration chromatography, three polysaccharide fractions (PS-F1, PS-F2 and PS-F3) were purified. PS-F2 stimulated mouse RAW264.7 macrophages to produce TNF-Î± and nitric oxide, and enhanced the phagocytic activity of macrophages. PS-F2 challenge in mice triggered an acute inflammatory response characterized by the recruitment of neutrophils and monocytes, which protected mice from sub...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5273911</comments>
            <pubDate>Mon, 03 Oct 2011 04:27:35 +0100</pubDate>
            <guid isPermaLink="false">5273911</guid>        </item>
        <item>
            <title>Enantioselective esterification of (R,S)-2-methylalkanoic acid with Carica papaya lipase in organic solvents.</title>
            <link>http://www.medworm.com/index.php?rid=5273910&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21744274%26dopt%3DAbstract</link>
            <description>Authors: Chang CS, Ho SC
    Abstract
    Isooctane was the best reaction medium for the enantioselective esterification of (R,S)-2-methylalkanoic acid with n-butanol using Carica papaya lipase as catalyst. Increasing linear alkyl-chain length of racemic 2-methylalkanoic acids from ethyl to hexyl increased the enantioselectivity (E) from 2.1 to 98.2 for the esterification of racemic 2-methylalkanoic acids with n-butanol at 35Â°C. Decreasing reaction temperature from 40 to 20Â°C increased the enantioselectivity (E) from 14 to 33 for the esterification of racemic 2-methylhexanoic acids with n-butanol. We obtained a maximum enantioselectivity, of EÂ =Â 24.3, for the enantioselective esterification of racemic 2-methylhexanoic acids with n-butanol in isooctane at water activity 0.33, and at 35Â...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5273910</comments>
            <pubDate>Mon, 03 Oct 2011 04:27:26 +0100</pubDate>
            <guid isPermaLink="false">5273910</guid>        </item>
        <item>
            <title>Bio-oxidation of H(2)S by Sulfolobus metallicus.</title>
            <link>http://www.medworm.com/index.php?rid=5273909&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21744275%26dopt%3DAbstract</link>
            <description>Authors: Morales M, Arancibia J, Lemus M, Silva J, Gentina JC, Aroca G
    Abstract
    Sulfolobus metallicus is a hyperthermophilic and chemolithoautotrophic archaeon that uses elemental sulfur as an energy source. Its ability to oxidize H(2)S was measured either in the presence or absence of elemental sulphur, showing its ability for using both as an energy source. A biotrickling filter was set up and a biofilm of S. metallicus was established over the support. The maximum removal capacity of the biotrickling filter reached at 55Â°C was 40 gÂ S/m(3)h for input loads higher than 70Â gÂ S/m(3)h. Thus, S. metallicus can be used in a biofiltration system for the treatment of waste gas emissions at high temperatures contaminated with H(2)S.
    PMID: 21744275 [PubMed - in process] (Source: Bi...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5273909</comments>
            <pubDate>Mon, 03 Oct 2011 04:27:16 +0100</pubDate>
            <guid isPermaLink="false">5273909</guid>        </item>
        <item>
            <title>Screening of Aspergillus-derived FAD: -glucose dehydrogenases from fungal genome database.</title>
            <link>http://www.medworm.com/index.php?rid=5273908&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21748361%26dopt%3DAbstract</link>
            <description>Authors: Mori K, Nakajima M, Kojima K, Murakami K, Ferri S, Sode K
    Abstract
    Aspergillus-derived FAD-dependent glucose dehydrogenases (FADGDHs) were screened from fungal genomic databases, primarily by searching for putative homologues of the Aspergillus niger-derived glucose oxidase (GOD). Focusing on a GOD active-site motif, putative proteins annotated as belonging to the glucose methanol choline (GMC) oxidoreductase family were selected. Phylogenetic analysis of these putative proteins produced a GOD clade, which includes the A. niger and Penicillium amagasakiens GODs, and a second clade made up of putative proteins showing 30-40% homology with GOD. The genes encoding the proteins from the second clade were functionally expressed in Escherichia coli, resulting in dye-mediated glu...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5273908</comments>
            <pubDate>Mon, 03 Oct 2011 04:27:06 +0100</pubDate>
            <guid isPermaLink="false">5273908</guid>        </item>
        <item>
            <title>Construction and validation of two metagenomic DNA libraries from Cerrado soil with high clay content.</title>
            <link>http://www.medworm.com/index.php?rid=5273907&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21748362%26dopt%3DAbstract</link>
            <description>Authors: de Castro AP, Quirino BF, Allen H, Williamson LL, Handelsman J, KrÃ¼ger RH
    Abstract
    A challenge of metagenomic studies is in the extraction and purification of DNA from environmental samples. The soils of the Cerrado region of Brazil present several technical difficulties to DNA extraction: high clay content (&amp;gt;55% w/w), low pH (4.7) and high iron levels (146Â ppm). Here we describe for the first time the efficient recovery and purification of microbial DNA associated with these unusual soil characteristics and the construction and validation of two metagenomic libraries: a 150,000 clones library with insert size of approximately 8Â kb and a 65,000 clones library with insert size of approximately 35Â kb. The construction of these metagenomic libraries will allow the biot...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5273907</comments>
            <pubDate>Mon, 03 Oct 2011 04:26:57 +0100</pubDate>
            <guid isPermaLink="false">5273907</guid>        </item>
        <item>
            <title>Applicability of thermo-alkali-stable and cellulase-free xylanase from a novel thermo-halo-alkaliphilic Bacillus halodurans in producing xylooligosaccharides.</title>
            <link>http://www.medworm.com/index.php?rid=5273906&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21750994%26dopt%3DAbstract</link>
            <description>Authors: Kumar V, Satyanarayana T
    Abstract
    An alkaliphilic, moderately thermophilic and halophilic bacterial isolate capable of producing a high titer of extracellular thermo-alkali-stable, cellulase-free endoxylanase was isolated from the paper mill effluents. It was identified as Bacillus halodurans. The purified xylanase was active from pH 7 to 12 and 30 to 100Â°C with optimal activity at pH 9.0 and 80Â°C. It had T(1/2) values of 40 and 15Â min at 70 and 80Â°C, respectively. Activity was stimulated by dithiothreitol but strongly inhibited by N-bromosuccinimide. Its action on birchwood xylan and agro-residues liberated xylooligosaccharides of 2-7 degree of polymerization, and thus, the mode of action is similar to endoxylanases of the family 10 glucoside hydrolases.
    PMID: 217...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5273906</comments>
            <pubDate>Mon, 03 Oct 2011 04:26:46 +0100</pubDate>
            <guid isPermaLink="false">5273906</guid>        </item>
        <item>
            <title>Effects of microbial species, organic loading and substrate degradation rate on the power generation capability of microbial fuel cells.</title>
            <link>http://www.medworm.com/index.php?rid=5273905&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21750995%26dopt%3DAbstract</link>
            <description>Authors: Juang DF, Yang PC, Chou HY, Chiu LJ
    Abstract
    Four microbial fuel cells (MFCs) inoculated with different bacterial species were constructed. The species were Pseudomonas putida, Comamonas testosteroni, Corynebacterium gultamicum, and Arthrobacter polychromogenes. The MFCs were operated under identical continuous flow conditions. The factors affecting the capabilities of the MFCs for treating organic matter and generating power were evaluated and compared. The factors include microbial species type, organic loading, and substrate degradation rate. For all four MFCs, power output increased with the organic loading rate. Power density also increased with the substrate degradation rate. These findings implied that more organic matter was utilized for power generation at higher ...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5273905</comments>
            <pubDate>Mon, 03 Oct 2011 04:26:36 +0100</pubDate>
            <guid isPermaLink="false">5273905</guid>        </item>
        <item>
            <title>Transgenic potato overproducing L: -ascorbic acid resisted an increase in methylglyoxal under salinity stress via maintaining higher reduced glutathione level and glyoxalase enzyme activity.</title>
            <link>http://www.medworm.com/index.php?rid=5273904&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21750996%26dopt%3DAbstract</link>
            <description>Authors: Upadhyaya CP, Venkatesh J, Gururani MA, Asnin L, Sharma K, Ajappala H, Park SW
    Abstract
    Salt-tolerance was studied in transgenic potato. It was conferred by overexpression of ascorbate pathway enzyme (D: -galacturonic acid reductase, GalUR). As genetic engineering of the GalUR gene in potato enhances its ascorbic acid content (L: -AsA), and subsequently plants suffered minimal oxidative stress-induced damage, we now report on the comprehensive aptness of this engineering approach for enhanced salt tolerance in transgenic potato (Solanum tuberosum L. cv. Taedong Valley). Potatoes overexpressing GalUR grew and tuberized in continuous presence of 200Â mM of NaCl. The transgenic plants maintained a higher reduced to oxidized glutathione (GSH:GSSG) ratio together with enhanced ...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5273904</comments>
            <pubDate>Mon, 03 Oct 2011 04:26:25 +0100</pubDate>
            <guid isPermaLink="false">5273904</guid>        </item>
        <item>
            <title>In vitro cultures of Drosera aliciae as a source of a cytotoxic naphthoquinone: ramentaceone.</title>
            <link>http://www.medworm.com/index.php?rid=5273903&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21761256%26dopt%3DAbstract</link>
            <description>Authors: Kawiak A, KrÃ³licka A, Lojkowska E
    Abstract
    A protocol for the in vitro propagation of Drosera aliciae to increase the yield of the naphthoquinone, ramentaceone, was developed. The highest micropropagation coefficient was obtained using half-strength Murashige-Skoog medium supplemented with 0.4Â Î¼M 6-benzyladenine (BA). The genetic fidelity and stability of the regenerated plants was confirmed with RAPD markers. The activity of the isolated ramentaceone was determined against four human tumor cell lines: U937, HeLa, MCF-7, HCT-116 with the highest cytotoxic activity towards the leukemic U937 cell line with an IC(50) value of 3.2Â Î¼M.
    PMID: 21761256 [PubMed - as supplied by publisher] (Source: Biotechnology Letters)</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5273903</comments>
            <pubDate>Mon, 03 Oct 2011 04:26:15 +0100</pubDate>
            <guid isPermaLink="false">5273903</guid>        </item>
        <item>
            <title>Energetic evaluation of an internally illuminated photobioreactor for algal cultivation.</title>
            <link>http://www.medworm.com/index.php?rid=5273902&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21766245%26dopt%3DAbstract</link>
            <description>Authors: Pegallapati AK, Nirmalakhandan N
    Abstract
    An annular internally illuminated photobioreatcor (IIPBR) configuration based on the airlift/bubble column principles was developed and validated at an 18Â l prototype scale using Scenedemus sp. and Nannochloropsis salina in batch and semi-continuous modes, at constant light supply and constant gas-to-culture volume ratio, but at varying CO(2)-to-air ratios. Highest biomass production was recorded at CO(2)-to-air ratio of 4% with Scenedesmus sp. and at 1% with Nannochloropsis salina. The energetic performance of this IIPBR was quantified in terms of biomass productivity per unit energy input, P/E (gÂ W(-1)Â day(-1)), considering energy input for illumination and for pneumatic mixing and circulation. Under optimal conditions, the II...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5273902</comments>
            <pubDate>Mon, 03 Oct 2011 04:26:04 +0100</pubDate>
            <guid isPermaLink="false">5273902</guid>        </item>
        <item>
            <title>Expansion of human mesenchymal stem cells on microcarriers.</title>
            <link>http://www.medworm.com/index.php?rid=5273901&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21769648%26dopt%3DAbstract</link>
            <description>Authors: Hewitt CJ, Lee K, Nienow AW, Thomas RJ, Smith M, Thomas CR
    Abstract
    The effects on human mesenchymal stem cell growth of choosing either of two spinner flask impeller geometries, two microcarrier concentrations and two cell concentrations (seeding densities) were investigated. Cytodex 3 microcarriers were not damaged when held at the minimum speed, N(JS), for their suspension, using either impeller, nor was there any observable damage to the cells. The maximum cell density was achieved after 8-10Â days of culture with up to a 20-fold expansion in terms of cells per microcarrier. An increase in microcarrier concentration or seeding density generally had a deleterious or neutral effect, as previously observed for human fibroblast cultures. The choice of impeller was signific...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5273901</comments>
            <pubDate>Mon, 03 Oct 2011 04:25:54 +0100</pubDate>
            <guid isPermaLink="false">5273901</guid>        </item>
        <item>
            <title>Identification and characterization of plastid trnF((GAA)) pseudogenes in four species of Solanum (Solanaceae).</title>
            <link>http://www.medworm.com/index.php?rid=5273900&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21833547%26dopt%3DAbstract</link>
            <description>Authors: Poczai P, HyvÃ¶nen J
    Abstract
    Non-functional trnF pseudogenes that rarely occur in embryophytes have been found in Solanaceae. We have sequenced the trnL-F intergenic spacer of four species of Solanum, and found duplicated regions of the original trnF gene. These repeats were 94-260Â bp long causing large length variation in the trnL-F intergenic spacer resulting from differences in pseudogene copy number (2-4). The duplicated trnF regions are comprised of several highly structured motifs, which were partial residues, or entire parts of the Anticodon, T- and D-domains of the original gene, but all lacked the acceptor stems at the 5'- or 3'-end. Pseudogenes included several transitions and transversions in their sequences compared to the original trnF gene. Among pseudogene...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5273900</comments>
            <pubDate>Mon, 03 Oct 2011 04:25:43 +0100</pubDate>
            <guid isPermaLink="false">5273900</guid>        </item>
        <item>
            <title>Trichoderma reesei cellobiohydrolase II is associated with the outer membrane when overexpressed in Escherichia coli.</title>
            <link>http://www.medworm.com/index.php?rid=5273898&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21956129%26dopt%3DAbstract</link>
            <description>Authors: Abdeljabbar DM, Song HJ, Link AJ
    Abstract
    Cellulose degradation is essential for the future production of many advanced biofuels. Cellulases from the filamentous fungus Trichoderma reesei are among the most efficient enzymes for the hydrolysis of cellulosic materials. One of the cellulases from T. reesei, cellobiohydrolase II (CBH2), was studied because of its industrial relevance and proven enzymatic activity. Using both crude and rigorous membrane fractionation methods we show that full length T. reesei CBH2 is exclusively localized to the outer membrane when expressed recombinantly in Escherichia coli. Even fusing signal sequence-free maltose-binding protein to the N-terminus of CBH2, which has been shown to increase solubility of other proteins, did not prevent the out...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5273898</comments>
            <pubDate>Thu, 29 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5273898</guid>        </item>
        <item>
            <title>Isolation and characterization of the citrinin biosynthetic gene cluster from Monascus aurantiacus.</title>
            <link>http://www.medworm.com/index.php?rid=5273897&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21956130%26dopt%3DAbstract</link>
            <description>Authors: Li YP, Xu Y, Huang ZB
    Abstract
    Monascus aurantiacus produces high amounts of citrinin which is a mycotoxin with nephrotoxic activity. Six putative citrinin biosynthesis genes have been discovered in M. purpureus and at least 10 genes are responsible for its biosynthesis. However, the sequence of citrinin pathway gene cluster in M. aurantiacus has not been reported. Here, the putative sequence of citrinin biosynthetic gene cluster was obtained by a PCR-based strategy for screening a genome fosmid library of M. aurantiacus. A sequence of 43Â kb revealed 16 ORFs including the six putative biosynthetic genes reported previous. The putative gene cluster consists of a polytekide synthetase encoding one PKS module, an oxidoreductase gene, three dehydrogenase genes, an acyl-coenzy...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5273897</comments>
            <pubDate>Thu, 29 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5273897</guid>        </item>
        <item>
            <title>Synthesis of encephalomyocarditis virus in a cell-free system: from DNA to RNA virus in one tube.</title>
            <link>http://www.medworm.com/index.php?rid=5273899&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21952914%26dopt%3DAbstract</link>
            <description>Authors: Kobayashi T, Nakamura Y, Mikami S, Masutani M, Machida K, Imataka H
    Abstract
    Virus particles are used in vaccination, drug delivery, and material sciences. Here we devised a system where the RNA virus encephalomyocarditis virus (EMCV) is synthesized from DNA templates in vitro. When a plasmid or a PCR product harboring the full-length cDNA of EMCV in the T7 promoter/terminator unit was incubated in a HeLa cell extract supplemented with T7 RNA polymerase, EMCV was produced within 4Â h at an efficiency of over 10-fold compared with the system programmed with the EMCV RNA. The EMCV RNA transcribed by the virally encoded RNA-dependent RNA polymerase was predominantly incorporated into the EMCV particle even in the presence of a larger amount of the EMCV RNA transcribed by T7 R...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5273899</comments>
            <pubDate>Wed, 28 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5273899</guid>        </item>
        <item>
            <title>Taxol-induced alteration of intracellular amino-acid profile related to human cervical carcinoma HeLa cell death.</title>
            <link>http://www.medworm.com/index.php?rid=5259294&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21938489%26dopt%3DAbstract</link>
            <description>Authors: Han XF, Liu YQ, Wang LX, Yang QX, Xiao HB
    Abstract
    The anti-tumor action of Taxol was investigated in the changes of amino-acids involved in tumor cell survival. By tracing the intracellular amino-acid profiles of HeLa cells treated with non-conditioned and three conditioned media (Taxol, L: -alanine, and TaxolÂ +Â L: -alanine), it was observed that an alteration of amino-acid metabolism participates in Taxol-induced death of HeLa cells. The contents of 18 out of 21 detected amino-acids are 5-95% and the ones of lysine and methionine are 158 and 117% of the corresponding contents in the control after treatment with Taxol for 24Â h, respectively. Addition of L: -alanine inhibited cell apoptosis upon Taxol treatment by partially blocking the increase of lysine and methionine...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5259294</comments>
            <pubDate>Thu, 22 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5259294</guid>        </item>
        <item>
            <title>A potential strategy for high-grade gliomas: combination treatment with lithium chloride and BmK CT.</title>
            <link>http://www.medworm.com/index.php?rid=5241966&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21932030%26dopt%3DAbstract</link>
            <description>Authors: Fu Y, Zheng S, Huang R, An N, Zheng Y, Zhang Z, Liang A
    Abstract
    Therapies for high-grade gliomas (HHG) that have strong tendency of infiltration and resistance to chemotherapies are currently unavailable. Here, we report that lower-dose combination therapy of Buthus martensii Karsch (BmK) CT, a type of scorpion toxin peptide, and LiCl, clinically used as mood stabilizer, could synergistically inhibit the migration, invasion and proliferation of C6 glioma cells. The decreased invasiveness of C6 glioma cells was accompanied by inhibited activation, catalytic activity and/or expression of matrix metalloproteinase-2. Moreover, TOPfalsh luciferase reporter and immunofluorescence staining showed altered localization pattern of Î²-catenin at the leading edge of 2D scratch. Our r...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5241966</comments>
            <pubDate>Tue, 20 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5241966</guid>        </item>
        <item>
            <title>A genome-wide association analysis of quantitative trait loci for protein fraction content in Tibetan wild barley.</title>
            <link>http://www.medworm.com/index.php?rid=5225914&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21915716%26dopt%3DAbstract</link>
            <description>Authors: Jin X, Wei K, Zhang G
    Abstract
    The genetic associations and differences of four protein fractions were investigated in Tibetan wild barley. Albumin, globulin and hordein contents were under genetic control probably via multiple genes/quantitative trait loci. A correlation analysis showed that globulin was significantly associated with albumin, glutelin and hordein, while hordein was closely correlated with glutelin. Forty-nine diversity array technology (DArT) markers, which were distributed over seven chromosomes, were associated with the protein fraction contents. Those DArT markers associated with hordein were the same as those associated with globulin and glutelin. Only five markers associated with hordein, globulin and glutelin were also associated with albumin. Most ...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5225914</comments>
            <pubDate>Wed, 14 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5225914</guid>        </item>
        <item>
            <title>Efficient expression of an alkaline pectate lyase gene from Bacillus subtilis and the characterization of the recombinant protein.</title>
            <link>http://www.medworm.com/index.php?rid=5225913&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21915717%26dopt%3DAbstract</link>
            <description>Authors: Liu Y, Chen G, Wang J, Hao Y, Li M, Li Y, Hu B, Lu F
    Abstract
    The gene encoding a novel alkaline pectate lyase (Apel) from Bacillus subtilis was cloned and expressed in B. subtilis WB600. Apel contained an ORF of 1,260Â bp, encoding a signal peptide of 21 amino acids and a mature protein of 399 amino acids with a calculated molecular mass of 45497.9Â Da. The mature Apel was structurally related to the enzymes in the polysaccharide lyase family 1. After purification, the recombinant Apel had a specific activity of 445Â UÂ mg(-1). The enzyme was optimally active at 50Â°C and pH 9.
    PMID: 21915717 [PubMed - as supplied by publisher] (Source: Biotechnology Letters)</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5225913</comments>
            <pubDate>Wed, 14 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5225913</guid>        </item>
        <item>
            <title>A high-throughput solid phase screening method for identification of lignocellulose-degrading bacteria from environmental isolates.</title>
            <link>http://www.medworm.com/index.php?rid=5216218&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21904949%26dopt%3DAbstract</link>
            <description>In this report, we describe a new, solid-phase screening system for the identification of microbes capable of lignocellulose degradation. The critical component of this screening system is the use of acrylamide, instead of agar, as the solidifying agent. Our results show that this screening method allows for the identification of Gram-positive and Gram-negative bacteria that possess cellulose and hemicellulose degrading activities from environmental isolates.
    PMID: 21904949 [PubMed - as supplied by publisher] (Source: Biotechnology Letters)</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5216218</comments>
            <pubDate>Fri, 09 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5216218</guid>        </item>
        <item>
            <title>Extracellular secretion of anticoagulant peptide hirudin in Lactococcus lactis using SP310mut2 signal peptide.</title>
            <link>http://www.medworm.com/index.php?rid=5216219&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21901343%26dopt%3DAbstract</link>
            <description>Authors: Lv J, Huang C, Zhang X, Tan S
    Abstract
    Hirudin can be used as an oral anticoagulant and antithrombotic agent. The hirudin variant III gene, derived from the medicinal leech, Hirudo medicinalis, was fused to SP310mut2 signal sequence and expressed by a nisin-controlled gene expression system in Lactococcus lactis which was then grown in a 7 l fermenter. After induction with 8Â ng nisin ml(-1), the product was secreted into the culture medium and accumulated up to ~2.7Â mg l(-1). MALDI-TOF/MS and anticoagulant activity analyses on the purified product confirmed its authenticity. This is the first demonstration that hirudin can be extracellularly secreted and correctly processed in L. lactis.
    PMID: 21901343 [PubMed - as supplied by publisher] (Source: Biotechnology Letter...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5216219</comments>
            <pubDate>Thu, 08 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5216219</guid>        </item>
        <item>
            <title>Characterization of a Î²-glucosidase from Sulfolobus solfataricus for isoflavone glycosides.</title>
            <link>http://www.medworm.com/index.php?rid=5216225&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21898127%26dopt%3DAbstract</link>
            <description>Authors: Kim BN, Yeom SJ, Kim YS, Oh DK
    Abstract
    The specific activity of a recombinant Î²-glucosidase from Sulfolobus solfataricus for isoflavones was: daidzinÂ &amp;gt;Â glycitinÂ &amp;gt;Â genistinÂ &amp;gt;Â malonyl genistinÂ &amp;gt;Â malonyl daidzinÂ &amp;gt;Â malonyl glycitin. The hydrolytic activity of this enzyme for daidzin was highest at pH 5.5 and 90Â°C with a half-life of 18Â h, a K (m) of 0.5Â mM, and a k (cat) of 2532Â s(-1). The enzyme converted 1Â mM daidzin to 1Â mM daidzein after 1Â h with a molar yield of 100% and a productivity of 1Â mMÂ h(-1). Among Î²-glucosidases, that from S. solfataricus Î² had the highest thermostability, k (cat), k (cat)/K (m), conversion yield, and productivity in the hydrolysis of daidzin.
    PMID: 21898127 [PubMed - as supplied by publisher] (Source: Bi...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5216225</comments>
            <pubDate>Tue, 06 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5216225</guid>        </item>
        <item>
            <title>Isolation, characterization and docking studies of 2,3-dihydroxybiphenyl 1,2-dioxygenase from an activated sludge metagenome.</title>
            <link>http://www.medworm.com/index.php?rid=5216224&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21898128%26dopt%3DAbstract</link>
            <description>Authors: Gou M, Qu Y, Xu B, Zhou J, Li X, Zhou H
    Abstract
    A 2,3-dihydroxybiphenyl-1,2-dioxygenase gene (designated as bphC_meta) was identified in activated sludge metagenome by PCR. This gene shared 99% sequence identity with BphC from Burkholderia xenovorans LB400. The enzyme was purified from recombinant Escherichia coli with a subunit molecular mass of 32Â Â±Â 1Â kDa. It was optimally active at pH 9.0 and 40Â°C, using 2,3-dihydroxybiphenyl as a substrate. Activity toward substituted catechols was: 2,3-dihydroxybiphenylÂ &amp;gt;Â 3-methylcatecholÂ &amp;gt;Â catecholÂ &amp;gt;Â 4-chlorocatechol (4-methylcatechol). The prediction made by molecular docking was consistent with the kinetic experimental data, and further explained the substrate preference of BphC_meta. The present study could pa...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5216224</comments>
            <pubDate>Tue, 06 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5216224</guid>        </item>
        <item>
            <title>Regioselectivity-reversal in acylation of 6-azauridine catalyzed by Burkholderia cepacia lipase.</title>
            <link>http://www.medworm.com/index.php?rid=5216223&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21898129%26dopt%3DAbstract</link>
            <description>Authors: Wang ZY, Bi YH, Zong MH
    Abstract
    3'-O-Stearoylation of 6-azauridine was achieved enzymatically for the first time. Among eight commercially available lipases, that from Burkholderia cepacia displayed a 3'-regioselectivity of 80% towards the acylation of 3-hydroxyl of 6-azauridine. Using an immobilized lipase from BurkholderiaÂ cepacia, the 3'-regioselectivities of the acylations could be reversed by lengthening the aliphatic chain of the acyl donors (C2-C18). The possible reason might be the presence of the interaction between the base moiety and the acyl group.
    PMID: 21898129 [PubMed - as supplied by publisher] (Source: Biotechnology Letters)</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5216223</comments>
            <pubDate>Tue, 06 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5216223</guid>        </item>
        <item>
            <title>Cell recycling during repeated very high gravity bio-ethanol fermentations using the industrial Saccharomyces cerevisiae strain PE-2.</title>
            <link>http://www.medworm.com/index.php?rid=5216222&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21898130%26dopt%3DAbstract</link>
            <description>This study contributes to the improvement of VHG fermentation processes by exploring an innovative operational strategy that allows attaining very high ethanol titres without a critical decrease of the viability level thus minimizing the production costs due to energy savings during the distillation process.
    PMID: 21898130 [PubMed - as supplied by publisher] (Source: Biotechnology Letters)</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5216222</comments>
            <pubDate>Tue, 06 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5216222</guid>        </item>
        <item>
            <title>Cholesterol assimilation and biotransformation by Lactobacillus helveticus.</title>
            <link>http://www.medworm.com/index.php?rid=5216221&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21898131%26dopt%3DAbstract</link>
            <description>Authors: Ahire JJ, Bhat AA, Thakare JM, Pawar PB, Zope DG, Jain RM, Chaudhari BL
    Abstract
    Lactobacillus helveticus, grown at 37Â°C in MRS medium supplemented with 3Â mM cholesterol, assimilated all the cholesterol in 42Â h having 68Â UÂ mg(-1) of intracellular cholesterol oxidase activity. The strain transformed 1Â g cholesterol to 0.05Â g of androsta-1, 4-diene-3, 17-dione and 0.04Â g of androst-4-ene-3, 17 dione within 48Â h at 37Â°C with extracellular cholesterol oxidase activity at 12Â UÂ mg(-1) and intracellular oxidase at 0.5Â UÂ mg(-1).
    PMID: 21898131 [PubMed - as supplied by publisher] (Source: Biotechnology Letters)</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5216221</comments>
            <pubDate>Tue, 06 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5216221</guid>        </item>
        <item>
            <title>H(2) production from CO, formate or starch using the hyperthermophilic archaeon, Thermococcus onnurineus.</title>
            <link>http://www.medworm.com/index.php?rid=5216220&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21898132%26dopt%3DAbstract</link>
            <description>Authors: Bae SS, Kim TW, Lee HS, Kwon KK, Kim YJ, Kim MS, Lee JH, Kang SG
    Abstract
    The hyperthermophilic archaeon, Thermococcus onnurineus, was grown in media supplemented with either CO, formate, or starch. H(2) was produced with each substrate with respective maximum rates of 1.55, 3.83 and 2.66Â mmol H(2)/lÂ h. The yields (mol H(2)/mol substrate) were 0.98, 1 and 3.13, respectively. This microbe is the first example where a single microorganism can grow and produce H(2) using CO, formate or starch as substrate.
    PMID: 21898132 [PubMed - as supplied by publisher] (Source: Biotechnology Letters)</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5216220</comments>
            <pubDate>Tue, 06 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5216220</guid>        </item>
        <item>
            <title>Erratum to: Development of a simple PCR-based assay for the identification of triazine resistance in the noxious plant common ragweed (Ambrosia artemisiifolia) and its applicability in higher plants.</title>
            <link>http://www.medworm.com/index.php?rid=5191077&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21874267%26dopt%3DAbstract</link>
            <description>Authors: MÃ¡tyÃ¡s KK, Taller J, Cseh A, Poczai P, CernÃ¡k I
    PMID: 21874267 [PubMed - as supplied by publisher] (Source: Biotechnology Letters)</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5191077</comments>
            <pubDate>Fri, 26 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5191077</guid>        </item>
        <item>
            <title>Gamma-radiation induced modifications in substrate specificity of glucose dehydrogenase and carbon source utilization pattern of phosphate-solubilizing Pantoea strains.</title>
            <link>http://www.medworm.com/index.php?rid=5173042&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21866443%26dopt%3DAbstract</link>
            <description>Authors: Lee YK, Senthilkumar M, Jeong IY, Annapurna K, Swarnalakshmi K
    Abstract
    Glucose, maltose, and mannose as sole carbon sources, induced synthesis of glucose dehydrogenase (GDH) in three strains of Pantoea with specific activities from 0.14 to 0.6Â U/mg proteins. Utilization of lactose indicated that the enzyme belongs to GDH type B isozyme. Of mutant clones, developed through radiation mutagenesis, P2-M2 utilized ribose with GDH specific activity of 0.57Â U/mg protein, P4-M3 grown on glucose gave 1.5Â U/mg protein and P4-M5 had high activities, when grown on galactose, maltose, and lactose. Clones P3-M2 and P2-M5 had versatile utilization of sugars and released higher amounts of P from tri-calcium phosphate and can be efficiently used for biofertilization.
    PMID: 21866443...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5173042</comments>
            <pubDate>Wed, 24 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5173042</guid>        </item>
        <item>
            <title>Streptomyces ghanaensis pleiotropic regulatory gene wblA ( gh ) influences morphogenesis and moenomycin production.</title>
            <link>http://www.medworm.com/index.php?rid=5148035&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21858667%26dopt%3DAbstract</link>
            <description>Authors: Rabyk M, Ostash B, Rebets Y, Walker S, Fedorenko V
    Abstract
    The wblA ( gh ) gene, encoding a homologue of the WhiB-family of proteins, was identified in the sequenced genome of moenomycin producer Streptomyces ghanaensis. Deletion of the gene blocked aerial mycelium sporulation and caused a 230% increase in moenomycins production. S. ghanaensis overexpressing SSFG-01620: a homologue of extracellular protease inhibitor SCO0762, whose expression in Streptomyces coelicolor is down-regulated by wblA: showed deficiencies in sporulation similar to that of wblA ( gh ) knockout strain. The wblA ( gh ) gene of S. ghanaensis appears to play a negative role in the control of moenomycin biosynthesis and is essential for sporulation.
    PMID: 21858667 [PubMed - as supplied by publishe...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5148035</comments>
            <pubDate>Sat, 20 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5148035</guid>        </item>
        <item>
            <title>A novel method for human hematopoietic stem/progenitor cell isolation from umbilical cord blood based on immunoaffinity aqueous two-phase partitioning.</title>
            <link>http://www.medworm.com/index.php?rid=5148034&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21858668%26dopt%3DAbstract</link>
            <description>Authors: Sousa AF, Andrade PZ, Pirzgalska RM, Galhoz TM, Azevedo AM, da Silva CL, Raquel Aires-Barros M, Cabral JM
    Abstract
    A novel cell separation process based on immunoaffinity aqueous two phase systems is presented to isolate and purify CD34(+) stem/progenitor cells directly from the whole umbilical cord blood (UCB). A system, composed of polyethylene glycol and dextran, was evaluated for the selective recovery of CD34(+) cells from UCB. A monoclonal antibody against the CD34 surface antigen was used for the direct partitioning of CD34(+) cells in UCB to the PEG-rich phase. The initial population of CD34(+) cells (0.2% of the initial sample) was enriched to values up to 42% in a single partitioning step, while the majority of contaminant cells were partitioned to the dextran-ri...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5148034</comments>
            <pubDate>Sat, 20 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5148034</guid>        </item>
        <item>
            <title>2,4,6-Trinitrophenol degradation by Bacillus cereus isolated from a firing range.</title>
            <link>http://www.medworm.com/index.php?rid=5148033&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21858669%26dopt%3DAbstract</link>
            <description>Authors: Singh B, Kaur J, Singh K
    Abstract
    Bacillus cereus strain PU, isolated from soil contaminated with explosive waste, tolerated up to 1.3Â mM 2,4,6 trinitrophenol (TNP) and utilize it aerobically as sole nitrogen and carbon source. Degradation of TNP was accompanied by stoichiometric release of 2.1Â Â±Â 0.15Â mol nitrite/mol TNP at 539Â Î¼mol/hÂ g dry cell wt. Metabolism of TNP was accompanied by transient accumulation of an orange-red metabolite, hydride meisenheimer complex (H-TNP), indicating a metabolic pathway involving complete reductive removal of the nitro group as nitrite.
    PMID: 21858669 [PubMed - as supplied by publisher] (Source: Biotechnology Letters)</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5148033</comments>
            <pubDate>Sat, 20 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5148033</guid>        </item>
        <item>
            <title>Fungal autolysate as a nutrient supplement for ethanol and chitosan production by Mucor indicus.</title>
            <link>http://www.medworm.com/index.php?rid=5140173&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21842395%26dopt%3DAbstract</link>
            <description>Authors: Asachi R, Karimi K, Taherzadeh MJ
    Abstract
    Mucor indicus can be used to produce ethanol from a variety of sugars, including pentose's. An extract of it, produced by autolysis, could replace yeast extract in culture medium with improved production of ethanol. At 10Â gÂ l(-1), the extract gave a higher ethanol yield (0.47Â gÂ g(-1)) and productivity (0.71Â gÂ l(-1)Â h(-1)) compared to medium containing yeast extract (yield 0.45Â gÂ g(-1); productivity 0.67Â gÂ l(-1)Â h(-1)).
    PMID: 21842395 [PubMed - as supplied by publisher] (Source: Biotechnology Letters)</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5140173</comments>
            <pubDate>Sat, 13 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5140173</guid>        </item>
        <item>
            <title>Expression of a secretory Î²-glucosidase from Trichoderma reesei in Pichia pastoris and its characterization.</title>
            <link>http://www.medworm.com/index.php?rid=5140189&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21826396%26dopt%3DAbstract</link>
            <description>Authors: Chen P, Fu X, Ng TB, Ye XY
    Abstract
    A Î²-glucosidase gene (bglI) from Trichoderma reesei was cloned into the pPIC9 vector and integrated into the genome of Pichia pastoris GS115. Under the control of the methanol-inducible alcohol oxidase (AOX) promoter and using Saccharomyces cerevisiae secretory signal peptide (Î±-factor), the recombinant Î²-glucosidase was expressed and secreted into the culture medium. The maximum recombinant Î²-glucosidase activity achieved was 60Â U/ml, and Î²-glucosidase expression reached 0.3Â mg/ml. The recombinant 76Â kDa Î²-glucosidase was purified 1.8-fold with 26% yield and a specific activity of 197Â U/mg. It was optimally active at 70Â°C and pH 5.0.
    PMID: 21826396 [PubMed - as supplied by publisher] (Source: Biotechnology Letters)</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5140189</comments>
            <pubDate>Mon, 08 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5140189</guid>        </item>
        <item>
            <title>Synthesis of Î³-aminobutyric acid by expressing Lactobacillus brevis-derived glutamate decarboxylase in the Corynebacterium glutamicum strain ATCC 13032.</title>
            <link>http://www.medworm.com/index.php?rid=5140180&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21826397%26dopt%3DAbstract</link>
            <description>Authors: Shi F, Li Y
    Abstract
    PURPOSE OF WORK: Purpose of this work is to synthesize Î³-aminobutyric acid by glutamate-producing species expressing Lactobacillus brevis-derived glutamate decarboxylase genes, i.e. recombinant Corynebacterium glutamicum strains, which directly convert endogenous L: -glutamate precursor into Î³-aminobutyric acid (GABA) through single-step fermentation. To express exogenous glutamate decarboxylase (GAD) in an L: -glutamate-producing strain, Lactobacillus brevis Lb85, which can produce GABA, was used. Two Lb85 GAD genes, gadB1 and gadB2, and the ancillary genes, gadC-gadB2 and gadR-gadC-gadB2, were cloned separately into pDXW-8 and transformed into C. glutamicum. All four recombinant strains produced GABA whereas the wild-type strain did not. GABA produ...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5140180</comments>
            <pubDate>Mon, 08 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5140180</guid>        </item>
        <item>
            <title>Effects of temperature during soybean seed development on defense-related gene expression and fungal pathogen accumulation.</title>
            <link>http://www.medworm.com/index.php?rid=5140179&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21826398%26dopt%3DAbstract</link>
            <description>Authors: Upchurch RG, Ramirez ME
    Abstract
    Soybean [Glycine max (L.) Merr] plants were exposed to three temperature regimens during seed development to investigate the effect of temperature on the expression of eight defense-related genes and the accumulation of two fungal pathogens in inoculated seeds. In seeds prior to inoculation, either a day/night warm (34/26Â°C) or a cool temperature (22/18Â°C) relative to normal (26/22Â°C) resulted in altered patterns of gene expression including substantially lower expression of PR1, PR3 and PR10. After seed inoculation with Cercospora kikuchii, pathogen accumulation was lowest in seeds produced at 22/18Â°C in which of all defense genes, MMP2 was uniquely most highly induced. For seeds inoculated with Diaporthe phaseolorum, pathogen accumula...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5140179</comments>
            <pubDate>Mon, 08 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5140179</guid>        </item>
        <item>
            <title>Inducible protein expression in Drosophila Schneider 2 cells using the lac operator-repressor system.</title>
            <link>http://www.medworm.com/index.php?rid=5140178&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21826399%26dopt%3DAbstract</link>
            <description>Authors: Wakiyama M, Muramatsu R, Kaitsu Y, Ikeda M, Yokoyama S
    Abstract
    Schneider line 2 cells, derived from Drosophila melanogaster, can be used as a highly versatile gene expression system. Two powerful promoters derived from the actin5C (Ac5) and metallothionein (Mtn) genes are available. The Mtn promoter can be used for the inducible expression of heterologous proteins unsuitable for constitutive expression. However, to circumvent using CuSO(4) or CdCl(2) as inducers of the Mtn promoter, we created a modified Ac5 promoter, Ac5LacO, in which two short lac operator sequences are embedded. Expression from the Ac5LacO promoter was regulated with co-expression of the lac repressor and IPTG. More than 25-fold induction of firefly luciferase expression was achieved in transient trans...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5140178</comments>
            <pubDate>Mon, 08 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5140178</guid>        </item>
        <item>
            <title>Malic acid production from thin stillage by Aspergillus species.</title>
            <link>http://www.medworm.com/index.php?rid=5140177&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21826400%26dopt%3DAbstract</link>
            <description>Authors: West TP
    Abstract
    The ability of Aspergillus strains to utilize thin stillage to produce malic acid was compared. The highest malic acid was produced by Aspergillus niger ATCC 9142 at 17Â gÂ l(-1). Biomass production from thin stillage was similar with all strains but ATCC 10577 was the highest at 19Â gÂ l(-1). The highest malic acid yield (0.8Â gÂ g(-1)) was with A. niger ATCC 9142 and ATCC 10577 on the stillage. Thus, thin stillage has the potential to act as a substrate for the commercial production of food-grade malic acid by the A. niger strains.
    PMID: 21826400 [PubMed - as supplied by publisher] (Source: Biotechnology Letters)</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5140177</comments>
            <pubDate>Mon, 08 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5140177</guid>        </item>
        <item>
            <title>Ginsenoside F(1) production from ginsenoside Rg(1) by a purified Î²-glucosidase from Fusarium moniliforme var. subglutinans.</title>
            <link>http://www.medworm.com/index.php?rid=5140175&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21826401%26dopt%3DAbstract</link>
            <description>Authors: Kim YS, Yoo MH, Lee GW, Choi JG, Kim KR, Oh DK
    Abstract
    Fusarium moniliforme var. subglutinans was selected from among 100 strains of fungi for producing ginsenoside F(1) from ginsenoside Rg(1). The enzyme responsible was purified as a single 85Â kDa band with a specific activity of 136Â UÂ mg(-1). It hydrolysed glucose-linked ginsenosides Rb(1), Rd and Rg(1) but not for other monosaccharide-linked ginsenosides, Rb(2), Rc, R(1), and Re. Under the optimum conditions of pH 6.0, 50Â°C, 30Â UÂ l(-1) of enzyme, and 5Â mg Rg(1)Â ml(-1), 4Â mg F(1)Â ml(-1) was produced after 4Â h, with a molar yield of 100% and a productivity of 1Â gÂ l(-1)Â h(-1). This represents the highest productivity and conversion yield of F(1) yet reported.
    PMID: 21826401 [PubMed - as supplied by publi...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5140175</comments>
            <pubDate>Mon, 08 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5140175</guid>        </item>
        <item>
            <title>Micropropagation and hairy root culture of Ophiorrhiza alata Craib for camptothecin production.</title>
            <link>http://www.medworm.com/index.php?rid=5140174&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21826402%26dopt%3DAbstract</link>
            <description>Authors: Ya-Ut P, Chareonsap P, Sukrong S
    Abstract
    An efficient system was developed for the in vitro micropropagation and hairy root culture of Ophiorrhiza alata Craib for camptothecin (CPT) production. Shoot multiplication on leaf and node explants from germinated seeds of O. alata was successful on half-strength Murashige and Skoog medium supplemented with varying amounts of kinetin and Î±-naphthaleneacetic acid. Node explants grown in vitro were successfully infected by Agrobacterium rhizogenes TISTR 1450 for the establishment of hairy root culture. The amount of CPT in various parts of O. alata was analyzed by HPLC. The accumulation of CPT in transformed hairy roots was twice that in soil-grown plants (785Â Â±Â 52 and 388Â Â±Â 32Â Î¼g/g dry wt, respectively). In the presence o...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5140174</comments>
            <pubDate>Mon, 08 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5140174</guid>        </item>
        <item>
            <title>Development of a simple PCR-based assay for the identification of triazine resistance in the noxious plant common ragweed (Ambrosia artemisiifolia) and its applicability in higher plants.</title>
            <link>http://www.medworm.com/index.php?rid=5092906&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21809088%26dopt%3DAbstract</link>
            <description>Authors: MÃ¡tyÃ¡s KK, Taller J, Cseh A, Poczai P, CernÃ¡k I
    Bidirectional allele-specific PCR (Bi-PASA) was used to detect a point mutation causing triazine resistance in common ragweed (Ambrosia artemisiifolia). The external primers amplified a 278Â bp standard DNA fragment in all genotypes. In the susceptible S264S genotypes, a 208Â bp fragment was expected while in resistant S264G common ragweed genotypes a 109Â bp band was expected. In resistant plants, both the wild and mutant type fragments were detected, indicating that the original triazine sensitive cpDNA is maintained in a heteroplasmic state in the resistant S264G genotypes. Additionally, in silico analysis confirmed the potential applicability of our diagnostic assay for other plant species. In 24 out of 74 taxa (32%), the ...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5092906</comments>
            <pubDate>Mon, 01 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5092906</guid>        </item>
        <item>
            <title>Combination of site-directed mutagenesis and yeast surface display enhances Rhizomucor miehei lipase esterification activity in organic solvent.</title>
            <link>http://www.medworm.com/index.php?rid=5092900&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21809089%26dopt%3DAbstract</link>
            <description>In conclusion, this method demonstrated that multiple sequence alignments and rational site-directed mutagenesis combined with yeast display technology is a faster and more effective means of obtaining high-efficiency esterification lipase variants compared with previous similar methods.
    PMID: 21809089 [PubMed - as supplied by publisher] (Source: Biotechnology Letters)</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5092900</comments>
            <pubDate>Mon, 01 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5092900</guid>        </item>
        <item>
            <title>Shear stress magnitude is critical in regulating the differentiation of mesenchymal stem cells even with endothelial growth medium.</title>
            <link>http://www.medworm.com/index.php?rid=5092910&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21805363%26dopt%3DAbstract</link>
            <description>Authors: Kim DH, Heo SJ, Kim SH, Shin JW, Park SH, Shin JW
    Human mesenchymal stem cells (MSC) were seeded onto the inner surface of a tubular silicon construct and, after 24Â h, were exposed to a shearing stress of either 2.5 or 10 dyne/cm(2) for 1Â day. The fluid contained endothelial growth factors in both cases. Morphological changes and cytoskeletal rearrangements were observed in the stimulated cells. Immunofluorescence staining showed that low (2.5 dyne/cm(2)) and high shear stress (10 dyne/cm(2)) resulted in the expression of von Willebrand factor (vWF) and calponin, respectively. At low shear stress, CD31 (PECAM-1) was significantly expressed whereas vWF and KDR expression was only slightly higher than those under 10 dyne/cm(2). All three markers related to smooth muscle cells ...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5092910</comments>
            <pubDate>Sat, 30 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5092910</guid>        </item>
        <item>
            <title>Construction of a Bacillus thuringiensis genetically-engineered strain harbouring the secreted Cry1Ia delta-endotoxin in its crystal.</title>
            <link>http://www.medworm.com/index.php?rid=5092935&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21805183%26dopt%3DAbstract</link>
            <description>Authors: Dammak M, Jaoua S, Tounsi S
    Unlike other Bacillus thuringiensis Cry proteins, Cry1Ia does not form a crystal since it is a secreted delta-endotoxin. We have engineered a Cry1Iac chimeric protein by substituting the C-terminal part of Cry1Ia by the corresponding Cry1Ac part. When expressed in an acrystalliferous B. thuringiensis strain, Cry1Iac did not crystallize, but when expressed in the crystalliferous strain BNS3, the chimeric protein co-crystallized with the endogenous Cry1A delta-endotoxins forming a typical bipyramidal crystal. The integration of Cry1Ia in the composition of the crystal of BNS3 led to an increase of its delta-endotoxin production (13%) and to an improvement (60%) of its toxicity against Agrotis ipsilon.
    PMID: 21805183 [PubMed - as supplied by publis...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5092935</comments>
            <pubDate>Fri, 29 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5092935</guid>        </item>
        <item>
            <title>Synthesis of sugar fatty acid esters using a Î²-xylosidase from Aspergillus awamori for transxylosylation.</title>
            <link>http://www.medworm.com/index.php?rid=5092928&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21805184%26dopt%3DAbstract</link>
            <description>Authors: Kurakake M, Ito Y, Komaki T
    Aspergillus awamori K4 Î²-xylosidase has broad acceptor specificity. It has been used to synthesize a sugar fatty acid ester via its transxylosylation activity. One xylosyl residue was initially transferred to hexamethylene glycol as a linker with a yield of 0.36Â g/g xylobiose. Linoleic acid was subsequently linked to one terminal hydroxyl side of the transfer product hydroxyhexyl xyloside through an esterification reaction catalyzed by a lipase. The synthesis of hexyl linoleoyl xyloside was confirmed by TOF-MS analysis. The binding with a linker improved the esterification reaction because of the hydrophobic hexamethylene chain and also prevented steric hindrance by the xylosyl residue. This sugar fatty acid ester synthesis method using transglyco...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5092928</comments>
            <pubDate>Fri, 29 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5092928</guid>        </item>
        <item>
            <title>Current perspectives of the Escherichia coli RNA degradosome.</title>
            <link>http://www.medworm.com/index.php?rid=5092921&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21805185%26dopt%3DAbstract</link>
            <description>Authors: Burger A, Whiteley C, Boshoff A
    Many biological processes in the cell are linked to RNA metabolism and therefore have implications for a wide range of biotechnological applications. The processing and degradation of RNA plays an important role in RNA metabolism with often the same enzymes being involved in both processes. In this review, we highlight the dynamic nature of the structural components of the Escherichia coli RNA degradosome which is a large multiprotein complex that plays an important role in RNA degradation. The activities of the individual components of the degradosome are also discussed. The RNA degradosome forms part of the bacterial cytoskeleton and associated proteins, such as molecular chaperones, may aid in the compartmentalization of enzymatic activities ...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5092921</comments>
            <pubDate>Fri, 29 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5092921</guid>        </item>
        <item>
            <title>Molecular analysis of genetic fidelity in Cannabis sativa L. plants grown from synthetic (encapsulated) seeds following in vitro storage.</title>
            <link>http://www.medworm.com/index.php?rid=5092917&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21805186%26dopt%3DAbstract</link>
            <description>Authors: Lata H, Chandra S, Techen N, Khan IA, Elsohly MA
    The increasing utilization of synthetic (encapsulated) seeds for germplasm conservation and propagation necessitates the assessment of genetic stability of conserved propagules following their plantlet conversion. We have assessed the genetic stability of synthetic seeds of Cannabis sativa L. during in vitro multiplication and storage for 6Â months at different growth conditions using inter simple sequence repeat (ISSR) DNA fingerprinting. Molecular analysis of randomly selected plants from each batch was conducted using 14 ISSR markers. Of the 14 primers tested, nine produced 40 distinct and reproducible bands. All the ISSR profiles from in vitro stored plants were monomorphic and comparable to the mother plant which confirms t...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5092917</comments>
            <pubDate>Fri, 29 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5092917</guid>        </item>
        <item>
            <title>Cloning, expression and characterization of a new lipase from Yarrowia lipolytica.</title>
            <link>http://www.medworm.com/index.php?rid=5092913&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21805187%26dopt%3DAbstract</link>
            <description>Authors: Zhao H, Zheng L, Wang X, Liu Y, Xu L, Yan Y
    Bioinformatic analysis of the Yarrowia lipolytica CLIB122 genome has revealed 18 putative lipase genes all of which were expressed in Escherichia coli and screened for hydrolyzing activities against p-nitrophenyl-palmitate. One positive transformant containing an ORF of 1,098Â bp encoding a protein of 365 amino acids was obtained. To characterize its enzymatic properties, the lipase gene was functionally expressed in Pichia pastoris. The resulting lipase exhibited the highest activity towards p-NP-decanoate at pH 7 and 35Â°C. In addition, the new lipase had a lower optimal temperature and pH compared to other Y. lipolytica lipases. It was noticeably enhanced by Ca(2+), but was inhibited by PMSF, Hg(2+) and Ni(2+). The new lipase disp...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5092913</comments>
            <pubDate>Fri, 29 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5092913</guid>        </item>
        <item>
            <title>Functional characterization of a putative Î²-lactamase gene in the genome of Zymomonas mobilis.</title>
            <link>http://www.medworm.com/index.php?rid=5092939&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21796435%26dopt%3DAbstract</link>
            <description>Authors: Rajnish KN, Asraf SA, Manju N, Gunasekaran P
    Zymomonas mobilis ZM4 is resistant to Î²-lactam antibiotics but there are no reports of a Î²-lactam resistance gene and its regulation. A putative Î²-lactamase gene sequence (ZMO0103) in the genome of Z. mobilis showed a 55% amino acid sequence identity with class C Î²-lactamase genes. qPCR analysis of the Î²-lactamase transcript indicated a higher level expression of the Î²-lactamase compared to the relative transcript quantities in antibiotic-susceptible bacteria. The putative Î²-lactamase gene was cloned, expressed in Escherichia coli BL21 and the product, AmpC, was purified to homogeneity. Its optimal activity was at pH 6 and 30Â°C. Further, the Î²-lactamase had a higher affinity towards penicillins than cephalosporin antibiotic...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5092939</comments>
            <pubDate>Wed, 27 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5092939</guid>        </item>
        <item>
            <title>Increased production of succinic acid in Escherichia coli by overexpression of malate dehydrogenase.</title>
            <link>http://www.medworm.com/index.php?rid=5092942&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21792684%26dopt%3DAbstract</link>
            <description>Authors: Liang LY, Liu RM, Ma JF, Chen KQ, Jiang M, Wei P
    Escherichia coli NZN111 is a double mutant with inactivated lactate dehydrogenase and pyruvate formate-lyase. It cannot utilize glucose anaerobically because of its unusually high intracellular NADH/NAD(+) ratio. We have now constructed a recombinant strain, E. coli NZN111/pTrc99a-mdh, which, during anaerobic fermentation, produced 4.3Â g succinic acidÂ l(-1) from 13.5Â gÂ glucoseÂ l(-1). The NADH/NAD(+) ratio decreased from 0.64 to 0.26. Furthermore, dual-phase fermentation (aerobic growth followed by anaerobic phase) resulted in enhanced succinic acid production and reduced byproduct formation. The yield of succinic acid from glucose during the anaerobic phase was 0.72Â gÂ g(-1), and the productivity was 1.01Â gÂ l(-1)Â h(-1)....</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5092942</comments>
            <pubDate>Tue, 26 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5092942</guid>        </item>
        <item>
            <title>Hairy roots cultures from different Solanaceous species have varying capacities to produce E. coli B-subunit heat-labile toxin antigen.</title>
            <link>http://www.medworm.com/index.php?rid=5092945&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21786173%26dopt%3DAbstract</link>
            <description>Authors: De Guzman G, Walmsley AM, Webster DE, Hamill JD
    The gene encoding enterotoxigenic Escherichia coli B-subunit heat-labile toxin (LTB) antigen was co-transformed into hairy root cultures of Nicotiana tabacum (tobacco), Solanum lycopersicum (tomato) and Petunia parodii (petunia) under the CaMV35S promoter. Tobacco and petunia roots containedÂ ~65-70Â Î¼g LTBÂ g(-1) tissue whilst hairy roots of tomato containedÂ ~10Â Î¼g LTBÂ g(-1). Antigen atÂ ~600Â ngÂ ml(-1) was detected in growth medium of tobacco and petunia. Tobacco roots with higher LTB levels showed growth retardation of ~80% whereas petunia hairy roots with similar levels of LTB showed only ~35% growth retardation, relative to vector controls. Regeneration of plants from LTB-containing tobacco hairy roots was readily achi...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5092945</comments>
            <pubDate>Sat, 23 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5092945</guid>        </item>
        <item>
            <title>Transformation of alfalfa chloroplasts and expression of green fluorescent protein in a forage crop.</title>
            <link>http://www.medworm.com/index.php?rid=5092952&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21785988%26dopt%3DAbstract</link>
            <description>Authors: Wei Z, Liu Y, Lin C, Wang Y, Cai Q, Dong Y, Xing S
    The ability to transform chloroplasts in multiple species is important for improving agricultural traits. Chloroplast transformation of alfalfa (Medicago sativa L.), a useful forage plant with high market value, was achieved using a vector carrying aadA and gfp genes being introduced into the chloroplasts of alfalfa via particle bombardment using leaves and calli as explants. Resistant somatic embryos were generated and developed into plantlets from explants. The transformation efficiency was 1.3% for callus explants and 2.7% for leaf explants. PCR and Southern blotting analyses revealed that the foreign genes were integrated into the transformed chloroplast genome. The occurrence of GFP was further confirmed by fluorescence m...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5092952</comments>
            <pubDate>Fri, 22 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5092952</guid>        </item>
        <item>
            <title>Use of Pichia fermentans and Candida sp. strains for the biological treatment of stored olive mill wastewater.</title>
            <link>http://www.medworm.com/index.php?rid=5092949&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21785989%26dopt%3DAbstract</link>
            <description>Authors: Taccari M, Ciani M
    Of 105 isolates screened for growth on plates containing olive mill wastewater (OMW), five were selected and identified as Pichia fermentans (Y1, Y4) and Candida sp. (Y2, Y11, and Y18). On the basis of their ability to use phenol at 716Â mgÂ l(-1), strains Y2 (15% reduction) and Y4 (18% reduction) were then used to detoxify stored OMW under various operational conditions. Yeast treatment of OMW increased the pH and, in the best conditions (aeration and no glucose addition), the COD decreased (47%) and phytotoxicity was also decreased (56%) probably due to the changes in the composition of phenolic compounds.
    PMID: 21785989 [PubMed - as supplied by publisher] (Source: Biotechnology Letters)</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5092949</comments>
            <pubDate>Fri, 22 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5092949</guid>        </item>
        <item>
            <title>Site-directed mutagenesis of aromatic residues in the carbohydrate-binding module of Bacillus endoglucanase EGA decreases enzyme thermostability.</title>
            <link>http://www.medworm.com/index.php?rid=4998107&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21720844%26dopt%3DAbstract</link>
            <description>Authors: Yin Q, Teng Y, Ding M, Zhao F
    The endoglucanase, EGA, from Bacillus sp. AC-1 comprises a glycosyl hydrolase family-9 catalytic module (CM9) and a family-3 carbohydrate-binding module (CBM3). Seven aromatic residues were subjected to site-directed mutagenesis in both CBM3 and EGA to investigate their roles in enzyme thermostability. The complexes generated by mixing CBMY527G, CBMW532A, or CBMF592G with CM9 each lost their activities after 15Â min at 45Â°C, while the wild-type complex retained &amp;gt;70% activity after 2Â h. The mutants EGAY527G, EGAW532A, and EGAF592G showed little activity after 15Â min at 60Â°C, whereas EGA remained 70% active after 2Â h. Thus the residues Tyr(527), Trp(532), and Phe(592) contribute not only to CBM3-mediated stability of CM9 but also to EGA ther...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4998107</comments>
            <pubDate>Thu, 30 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4998107</guid>        </item>
        <item>
            <title>Use of chemometrics in the selection of a Saccharomyces cerevisiae expression system for recombinant cyprosin B production.</title>
            <link>http://www.medworm.com/index.php?rid=4998106&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21720845%26dopt%3DAbstract</link>
            <description>Authors: Sampaio PN, Sousa L, Calado CR, Pais MS, Fonseca LP
    Two multivariate statistical methods, factor analysis (FA) and hierarchical cluster analysis (HCA), were applied to experimental data set to evaluate their usefulness in selecting the adequate expression system and optimal growth parameters for recombinant cyprosin B production. Using FA, the large data set was reduced to two factors representing 73.4% of variability. Factor 1, with 53.5% of variability, corresponds to recombinant cyprosin B expression and efficient secretion, while factor 2, accounting for 19.9% of variability, represents cell growth and physiological characteristics. FA and HCA allowed the establishment of correlations among different variables and the clusters obtained providing clear identification of the...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4998106</comments>
            <pubDate>Thu, 30 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4998106</guid>        </item>
        <item>
            <title>Discovery and characterization of a xylose reductase from Zymomonas mobilis ZM4.</title>
            <link>http://www.medworm.com/index.php?rid=4998105&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21720846%26dopt%3DAbstract</link>
            <description>We report here the discovery of xylose reductase in Zymomonas mobilis and, for the first time, to associate the enzyme function with its gene. Besides xylose and xylulose, the enzyme was active towards benzaldehyde, furfural, 5-hydroxymethyl furfural, and acetaldehyde, exhibiting nearly 150-times higher affinity with benzaldehyde than xylose. The discovery of xylose reductase paves the way for further improvement of xylose fermentation in Z. mobilis. The enzyme may also be used to mitigate toxicity of furfural and other inhibitors from plant biomass.
    PMID: 21720846 [PubMed - as supplied by publisher] (Source: Biotechnology Letters)</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4998105</comments>
            <pubDate>Thu, 30 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4998105</guid>        </item>
        <item>
            <title>Killer phenotype of indigenous yeasts isolated from Argentinian wine cellars and their potential starter cultures for winemaking.</title>
            <link>http://www.medworm.com/index.php?rid=4998104&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21720847%26dopt%3DAbstract</link>
            <description>Authors: de Ullivarri MF, Mendoza LM, Raya RR, FarÃ­as ME
    Of 31 yeasts, from different surfaces of two cellars from the northwest region of Argentina, 11 expressed killer activity against the sensitive strain Saccharomyces cerevisiae P351. Five of these killer yeasts were identified as S. cerevisiae by phenotypic tests and PCR-RFLP analysis. Two S. cerevisiae killer strains, Cf5 and Cf8, were selected based on their excellent kinetic and enological properties as potential autochthonous mixed starter cultures to be used during wine fermentation. They could dominate the natural microbiota in fermentation vats and keep the typical sensorial characteristics of the wine of this region.
    PMID: 21720847 [PubMed - as supplied by publisher] (Source: Biotechnology Letters)</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4998104</comments>
            <pubDate>Thu, 30 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4998104</guid>        </item>
        <item>
            <title>Improvement of the thermostability and enzymatic activity of cholesterol oxidase by site-directed mutagenesis.</title>
            <link>http://www.medworm.com/index.php?rid=4998108&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21701916%26dopt%3DAbstract</link>
            <description>Authors: Sun Y, Yang H, Wang W
    Site-directed mutagenesis was applied to enhance the thermostability and enzymatic activity of cholesterol oxidase (ChOx) isolated from Brevibacterium sp. Three amino acid residues (Q153E, F128L, and S143H) located near the FAD-binding site of the enzyme were substituted based on structural analysis. The specific activity of the two-sites mutant Q153E/F128L increased by 11.6% and the relative activity increased by 47% when grown for 2Â h at 50Â°C. This mutant is a potential industrial strain for producing ChOx.
    PMID: 21701916 [PubMed - as supplied by publisher] (Source: Biotechnology Letters)</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4998108</comments>
            <pubDate>Thu, 23 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4998108</guid>        </item>
        <item>
            <title>Homologous overexpression of omcZ, a gene for an outer surface c-type cytochrome of Geobacter sulfurreducens by single-step gene replacement.</title>
            <link>http://www.medworm.com/index.php?rid=4998110&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21698445%26dopt%3DAbstract</link>
            <description>Authors: Park I, Kim BC
    The electron transfer pathway of Geobacter sulfurreducens has been intensively studied because of its ability of electron transfer to extracellular electron acceptors, such as Fe(III) and on electrode. However, the absence of overexpression system of G. sulfurreducens is one of the main obstacles for studying the physiology of G. sulfurreducens. OmcZ, an outer membrane-related c-type cytochrome of G. sulfurrducens, was homologously overexpressed via genomic integration. Quantitative RT-PCR analysis showed that the omcZ transcript in the knock-in strain was sixfold more abundant than in the wild type. Notably, omcZ expression appears to downregulate the expression level of OmcS, another outer membrane-related c-type cytochrome of G. sulfurreducens, based on the c...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4998110</comments>
            <pubDate>Wed, 22 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4998110</guid>        </item>
        <item>
            <title>Sleeping Beauty-mediated knockdown of sheep myostatin by RNA interference.</title>
            <link>http://www.medworm.com/index.php?rid=4998109&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21698446%26dopt%3DAbstract</link>
            <description>Authors: Hu S, Ni W, Sai W, Zhang H, Cao X, Qiao J, Sheng J, Guo F, Chen C
    Myostatin is a negative regulator of skeletal muscle growth. Myostatin dysfunction therefore offers a strategy for promoting animal muscle growth in livestock production. Knockdown of myostatin was achieved by combining RNA interference and the Sleeping Beauty (SB) transposon system in sheep cells. Four targeting sites of sheep myostatin were designed and measured for myostatin silencing in sheep fetal fibroblasts by real-time PCR. The sh3 construct induced significant decrease of myostatin gene expression by 90% (PÂ &amp;lt;Â 0.05). Myostatin silencing induced by SB-mediated sh3 was further tested in stably transfected cells. SB transposition increased the integration frequency of genes into sheep genomes and media...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4998109</comments>
            <pubDate>Wed, 22 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4998109</guid>        </item>
        <item>
            <title>Enhancement of activity and selectivity of Candida rugosa lipase and Candida antarctica lipase A by bioimprinting and/or immobilization for application in the selective ethanolysis of fish oil.</title>
            <link>http://www.medworm.com/index.php?rid=4998112&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21695486%26dopt%3DAbstract</link>
            <description>Authors: Kahveci D, Xu X
    Candida rugosa lipase (CRL) and Candida antarctica lipase A (CALA) with improved activity and selectivity were prepared for use in organic solvent media. CRL bioimprinted with fatty acids exhibited eightfold enhanced transesterification activity in hexane. Combination of bioimprinting and coating with lecithin or with immobilization did not improve the activity further. CALA was immobilized with and without bioimprinting, none of which improved the activity. All modified lipases were tested for selective ethanolysis of fish oil to concentrate omega-3 polyunsaturated fatty acids (PUFA). None of the preparations, except the immobilized ones catalysed ethanolysis. Immobilized CRL-catalyzed ethanolysis giving 27% (v/v) ethyl esters (EE) in 48Â h, of which 43Â mol% ...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4998112</comments>
            <pubDate>Tue, 21 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4998112</guid>        </item>
        <item>
            <title>A highly stable Cu/Zn superoxide dismutase from Withania somnifera plant: gene cloning, expression and characterization of the recombinant protein.</title>
            <link>http://www.medworm.com/index.php?rid=4998111&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21695487%26dopt%3DAbstract</link>
            <description>Authors: Madanala R, Gupta V, Deeba F, Upadhyay SK, Pandey V, Singh PK, Tuli R
    A gene from Withania somnifera (winter cherry), encoding a highly stable chloroplastic Cu/Zn superoxide dismutase (SOD), was cloned and expressed in Escherichia coli. The recombinant enzyme (specific activity ofÂ ~4,200 U mg(-1)) was purified and characterized. It retainedÂ ~90 andÂ ~70% residual activities after 1Â h at 80 and 95Â°C, respectively. At 95Â°C, thermal inactivation rate constant (K (d)) of the enzyme was 2.46Â Ã—Â 10(-3) min(-1) and half-life of heat inactivation was 4.68Â h. The enzyme was stable against a broad pH range (2.5-11.0). It also showed a high degree of resistance to detergent, ethanol and protease digestion. This recombinant Cu/Zn SOD could therefore have useful applications.
    P...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4998111</comments>
            <pubDate>Tue, 21 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4998111</guid>        </item>
        <item>
            <title>Inactivation of the extracytoplasmic function sigma factor Sig6 stimulates avermectin production in Streptomyces avermitilis.</title>
            <link>http://www.medworm.com/index.php?rid=4998115&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21691838%26dopt%3DAbstract</link>
            <description>Authors: Jiang L, Liu Y, Wang P, Wen Y, Song Y, Chen Z, Li J
    The role of the extracytoplasmic function (ECF) Ïƒ factor Sig6 (SAV663) in avermectin production by Streptomyces avermitilis was investigated by gene-deletion, complementation and over-expression experiments. Inactivation of Sig6 had no major effect on growth, stress responses, or morphology. Avermectin yield was increased 2- to 2.7-fold (~680Â Î¼g/ml) relative to the wild-type strain by deletion of the sig6 gene, and was restored to the wild-type level by introduction of a single copy of sig6. Introduction of extra multi-copy or integrative sig6 vectors into the wild-type decreased avermectin yield by 56-63%. Taken together, these findings indicate that Sig6 plays a negative regulatory role in avermectin production in S. ave...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4998115</comments>
            <pubDate>Mon, 20 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4998115</guid>        </item>
        <item>
            <title>Biomass and lipid production of heterotrophic microalgae Chlorella protothecoides by using biodiesel-derived crude glycerol.</title>
            <link>http://www.medworm.com/index.php?rid=4998114&amp;cid=s_37625_70_f&amp;fid=37625&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21691839%26dopt%3DAbstract</link>
            <description>Authors: Chen YH, Walker TH
    Microalgal lipids may be a more sustainable biodiesel feedstock than crop oils. We have investigated the potential for using the crude glycerol as a carbon substrate. In batch mode, the biomass and lipid concentration of Chlorella protothecoides cultivated in a crude glycerol medium were, respectively, 23.5 and 14.6Â g/l in a 6-day cultivation. In the fed-batch mode, the biomass and lipid concentration improved to 45.2 and 24.6Â g/l after 8.2Â days of cultivation, respectively. The maximum lipid productivity of 3Â g/lÂ day in the fed-batch mode was higher than that produced by batch cultivation. This work demonstrates the feasibility of crude biodiesel glycerol as an alternative carbon substrate to glucose for microalgal cultivation and a cost reduction of c...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4998114</comments>
            <pubDate>Mon, 20 Jun 2011 23:00:00 +0100</pubDate>
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