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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>Sun, 21 Mar 2010 17:09:03 +0100</lastBuildDate>
        <item>
            <title>Production of ethanol by the white-rot basidiomycetes Peniophora cinerea and Trametes suaveolens.</title>
            <link>http://www.medworm.com/index.php?rid=3386060&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%3D20238143%26dopt%3DAbstract</link>
            <description>Authors: Okamoto K, Imashiro K, Akizawa Y, Onimura A, Yoneda M, Nitta Y, Maekawa N, Yanase H
    The white-rot basidiomycetes, Peniophora cinerea and Trametes suaveolens, can produce ethanol from hexoses. Although T. suaveolens produced negligible amounts of ethanol under aerobic conditions, P. cinerea produced ethanol under both aerobic and semi-aerobic conditions and assimilated glucose, mannose, fructose, galactose, sucrose, maltose and cellobiose with yields of ethanol of 0.41, 0.45, 0.44, 0.19, 0.41, 0.44 and 0.45 g per g hexose, respectively. The corresponding results for T. suaveolens were 0.39, 0.3, 0.13, 0.2, 0.37, 0.35 and 0.31 g ethanol/g hexose. Furthermore, P. cinerea exhibited simultaneous saccharification and fermentation of amorphous cellulose.
    PMID: 20238143 [PubMed - ...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3386060</comments>
            <pubDate>Thu, 18 Mar 2010 00:00:00 +0100</pubDate>
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            <title>PEGylation of alpha-momorcharin: synthesis and characterization of novel anti-tumor conjugates with therapeutic potential.</title>
            <link>http://www.medworm.com/index.php?rid=3386059&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%3D20238144%26dopt%3DAbstract</link>
            <description>Authors: Bian X, Shen F, Chen Y, Wang B, Deng M, Meng Y
    Alpha-momorcharin (alpha-MMC) is a ribosome-inactivating protein (RIP) with excellent cytotoxicity to tumor cells. However, its strong immunogenicity and short plasma half-life limit its clinical applications. To overcome this, we have to PEGylated alpha-MMC using a branched 20 kDa (mPEG) (2)-Lys-NHS. Homogeneous mono-, di- and tri-PEGylated alpha-MMCs were synthesized, purified and characterized. In vitro and in vivo analysis indicated that the serial PEG-conjugates preserved moderate anti-tumor activity with 36% acute toxicity and at most 66% immunogenicity decrease. These results suggested the potential application of alpha-MMC-PEG conjugates as an anti-tumor agent.
    PMID: 20238144 [PubMed - as supplied by publisher] (Source...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3386059</comments>
            <pubDate>Thu, 18 Mar 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3386059</guid>        </item>
        <item>
            <title>Effect of the C-terminal domains and terminal residues of catalytic domain on enzymatic activity and thermostability of lichenase from Clostridium thermocellum.</title>
            <link>http://www.medworm.com/index.php?rid=3371138&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%3D20229062%26dopt%3DAbstract</link>
            <description>Authors: Niu D, Zhou XX, Yuan TY, Lin ZW, Ruan H, Li WF
    To elucidate the effects of C-terminal domains of LicMB (mature lichenase from Clostridium thermocellum) and terminal residues of LicMB-CD (catalytic domain of LicMB) on the properties of lichenase, a series of truncated genes were constructed and expressed in E. coli. The Thr-Pro box had a positive effect while the dockerin domain had a negative impact on the properties of LicMB. The N-terminal 10-25th and C-terminal 1-9th residues of LicMB-CD were necessary to retain high thermostability while the N-terminal 1-7th and C-terminal 1-3rd residues were not necessary to maintain enzymatic activity.
    PMID: 20229062 [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=3371138</comments>
            <pubDate>Sat, 13 Mar 2010 00:00:00 +0100</pubDate>
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        <item>
            <title>Functional characterization of AtHsp90.3 in Saccharomyces cerevisiae and Arabidopsis thaliana under heat stress.</title>
            <link>http://www.medworm.com/index.php?rid=3371137&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%3D20229063%26dopt%3DAbstract</link>
            <description>Authors: Xu X, Song H, Zhou Z, Shi N, Ying Q, Wang H
    The function of cytosolic AtHsp90.3 was characterized by complementing the Saccharomyces cerevisiae endogenous Hsp90 genes and overexpressing it in Arabidopsis thaliana. Though AtHsp90.3 supported the yeast growth under heat stress, in Arabidopsis, compared to the wild type, the transgenic plants overexpressing cytosolic AtHsp90.3 were more sensitive to heat stress with a lower germination rate and higher mortality but and more tolerant to high Ca(2+). Transcriptional expression of heat stress transcription factors, AtHsfA1d, AtHsfA7a and AtHsfB1, and two Hsps, AtHsp101 and AtHsp17, was delayed by constitutive overexpression of cytosolic AtHsp90.3 under heat stress. These results indicate that overexpressing AtHsp90.3 impaired plant ...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3371137</comments>
            <pubDate>Sat, 13 Mar 2010 00:00:00 +0100</pubDate>
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        <item>
            <title>Retinal production from beta-carotene by beta-carotene 15,15'-dioxygenase from an unculturable marine bacterium.</title>
            <link>http://www.medworm.com/index.php?rid=3371136&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%3D20229064%26dopt%3DAbstract</link>
            <description>Authors: Kim YS, Park CS, Oh DK
    The conversion of beta-carotene to retinal by a recombinant beta-carotene 15,15'-dioxygenase (Blh protein) from an unculturable marine bacterium was optimized in aqueous solution. Toluene was optimal solvent for the dissolution of beta-carotene and the optimal solution for the conversion reaction contained 2.4% (w/v) Tween 20, 0.15 U enzyme/ml, and 350 mg beta-carotene/l. Under these conditions, the enzyme produced 181 mg retinal/l after 20 h. This is the highest reported value for the retinal concentration from beta-carotene.
    PMID: 20229064 [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=3371136</comments>
            <pubDate>Sat, 13 Mar 2010 00:00:00 +0100</pubDate>
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        <item>
            <title>Metabolic analysis of elicited cell suspension cultures of Cannabis sativa L. by (1)H-NMR spectroscopy.</title>
            <link>http://www.medworm.com/index.php?rid=3371135&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%3D20229065%26dopt%3DAbstract</link>
            <description>Authors: Pe&amp;#x10D; J, Flores-Sanchez IJ, Choi YH, Verpoorte R
    Cannabis sativa L. plants produce a diverse array of secondary metabolites. Cannabis cell cultures were treated with jasmonic acid (JA) and pectin as elicitors to evaluate their effect on metabolism from two cell lines using NMR spectroscopy and multivariate data analysis. According to principal component analysis (PCA) and partial least square-discriminant analysis (PLS-DA), the chloroform extract of the pectin-treated cultures were more different than control and JA-treated cultures; but in the methanol/water extract the metabolome of the JA-treated cells showed clear differences with control and pectin-treated cultures. Tyrosol, an antioxidant metabolite, was detected in cannabis cell cultures. The tyrosol content increas...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3371135</comments>
            <pubDate>Sat, 13 Mar 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3371135</guid>        </item>
        <item>
            <title>Hydrophobicity of residue 108 specifically affects the affinity of human beta-carotene 15,15'-monooxygenase for substrates with two ionone rings.</title>
            <link>http://www.medworm.com/index.php?rid=3362624&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%3D20221844%26dopt%3DAbstract</link>
            <description>Authors: Kim YS, Park CS, Oh DK
    The Lys residue at position 108 of human beta-carotene 15,15'-monooxygenase is located on the outside surface of the active tunnel of the enzyme. Hydrophobic mutations (K108F and K108L) at this position substantially decreased the affinity of the enzyme for substrates with ionone rings at both ends, such as alpha-carotene, beta-carotene, and beta-cryptoxanthine. In contrast, these mutations had little effect on the affinity of the enzyme for substrates with one ionone ring and one open-chain end, such as beta-apo-4'-carotenal and beta-apo-8'-carotenal. The residue 108 may be related to the indirect interaction with the second ionone ring of the substrates with two ionone rings.
    PMID: 20221844 [PubMed - as supplied by publisher] (Source: Biotechnology...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3362624</comments>
            <pubDate>Thu, 11 Mar 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3362624</guid>        </item>
        <item>
            <title>Kinetic and thermodynamic analyses of adhesion of a peptide, Trp-Lys-Tyr-Met-Val-D-Met (WKYMVm), and human formyl peptide receptor (hFPR).</title>
            <link>http://www.medworm.com/index.php?rid=3362623&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%3D20221845%26dopt%3DAbstract</link>
            <description>Authors: Cho JH, Cho K, Shin HS
    The kinetic and thermodynamic properties of a peptide-receptor interaction was investigated by measuring the adhesion force in the reaction via atomic force microscopy (AFM). Trp-Lys-Tyr-Met-Val-D-Met (WKYMVm), considered as a model system in the present study, is a potent neutrophil chemo-attractant. Since being identified as an agonist for formyl peptide receptor (FPR), WKYMVm's high affinity to FPR has been verified through investigation of its kinetic and physiological behaviors via conventional methods. However, there have been no reports on the adhesion force of WKYMVm-FPR. In this research, we measured the adhesion force of WKYMVm-FPR using AFM. Kinetic parameters obtained from the relationship between the adhesion force and loading rate were used...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3362623</comments>
            <pubDate>Thu, 11 Mar 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3362623</guid>        </item>
        <item>
            <title>lip2, a novel lipase gene cloned from Aspergillus niger exhibits enzymatic characteristics distinct from its previously identified family member.</title>
            <link>http://www.medworm.com/index.php?rid=3354776&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%3D20213520%26dopt%3DAbstract</link>
            <description>Authors: Yang J, Sun J, Yan Y
    We have cloned a novel lipase gene, lip2, from Aspergillus niger and expressed it in Escherichia coli. Upon purification of the recombinant Lip2 protein, its properties were characterized. In comparison with a previously identified lipase Lip1, both enzymes are acid lipases (optimal pH &amp;lt;6.5), Ca(2+)-dependent and PMSF-sensitive, but have different molecular weights (35 and 43 kDa), optimal substrate spectra (C10 and C8), optimal reaction temperatures (45 and 50 degrees C) and thermal stability. Circular dichroism spectroscopy revealed that Lip2 contains a typical Ca(2+)-active site. This first report on the cloning of the Lip2 gene and its enzymatic characteristics may greatly facilitate its potential industrial application.
    PMID: 20213520 [PubMed -...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3354776</comments>
            <pubDate>Mon, 08 Mar 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3354776</guid>        </item>
        <item>
            <title>Enhancement of the thermostability of a recombinant beta-agarase, AgaB, from Zobellia galactanivorans by random mutagenesis.</title>
            <link>http://www.medworm.com/index.php?rid=3354775&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%3D20213521%26dopt%3DAbstract</link>
            <description>Authors: Jang MK, Lee SW, Lee DG, Kim NY, Yu KH, Jang HJ, Kim S, Kim A, Lee SH
    Random mutagenesis was performed on beta-agarase, AgaB, from Zobellia galactanivorans to improve its catalytic activity and thermostability. The activities of three mutants E99K, T307I and E99K-T307I were approx. 140, 190 and 200%, respectively, of wild type beta-agarase (661 U/mg) at 40 degrees C. All three mutant enzymes were stable up to 50 degrees C and E99K-T307I had the highest thermostability. The melting temperature (T (m)) of E99K-T307I, determined by CD spectra, was increased by 5.2 degrees C over that of the wild-type enzyme (54.6 degrees C). Activities of both the wild-type and E99K-T307I enzymes, as well as their overall thermostabilities, increased in 1 mM CaCl(2). The E99K-T307I enzyme was sta...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3354775</comments>
            <pubDate>Mon, 08 Mar 2010 00:00:00 +0100</pubDate>
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        <item>
            <title>Development of 3-D poly(trimethylenecarbonate-co-epsilon-caprolactone)-block-poly(p-dioxanone) scaffold for bone regeneration with high porosity using a wet electrospinning method.</title>
            <link>http://www.medworm.com/index.php?rid=3354773&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%3D20213523%26dopt%3DAbstract</link>
            <description>Authors: Shin TJ, Park SY, Kim HJ, Lee HJ, Youk JH
    The three dimensional (3-D) poly(trimethylenecarbonate-co-epsilon-caprolactone)-block-poly(p-dioxanone) scaffold was made using a wet electrospinning method and its application as a tissue engineered matrix was evaluated for bone regeneration. The scaffold was highly porous (90%) and interconnected among pores. Under scanning electron microscopy, the cells of the center of the scaffold showed healthy well attached shape even at 4 days after seeding. The osteoblastic MC3T3-E1 cells proliferated 1.2 times faster at 4 day, 1.5 times faster at 7 days after seeding as compared with the control in the scaffold (P &amp;lt; 0.05). The activity of alkaline phosphatase, a bone formation marker, of cells seeded in the scaffold was nearly four times f...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3354773</comments>
            <pubDate>Mon, 08 Mar 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3354773</guid>        </item>
        <item>
            <title>Exploring different strategies to express Dengue virus envelope protein in a plant system.</title>
            <link>http://www.medworm.com/index.php?rid=3354774&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%3D20213522%26dopt%3DAbstract</link>
            <description>Authors: Mart&amp;#xED;nez CA, Topal E, Giulietti AM, Talou JR, Mason H
    Dengue virus envelope glycoprotein (E-protein) is the main protein associated with immunity induction. To produce a candidate for subunit vaccines and to provide an antigen for diagnostic kits, it was expressed in a novel plant system using deconstructed viral modules. A truncated version of the E-protein was designed to be expressed alone and co-expressed with Dengue virus structural proteins. As well, the critical domain III of E-protein was fused to hepatitis B core antigen (HBcore). The recombinant proteins were produced in Nicotiana benthamiana plants and were reactive with the anti-E antibody. The fusion was reactive with both anti-E and anti-HBcore antibodies.
    PMID: 20213522 [PubMed - as supplied by publishe...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3354774</comments>
            <pubDate>Sun, 07 Mar 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3354774</guid>        </item>
        <item>
            <title>Engineering cytochrome P450 monooxygenase CYP 116B3 for high dealkylation activity.</title>
            <link>http://www.medworm.com/index.php?rid=3354772&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%3D20213524%26dopt%3DAbstract</link>
            <description>Authors: Liu L, Schmid RD, Urlacher VB
    Cytochrome P450 monooxygenase CYP116B3 from Rhodococcus ruber catalyzes the dealkylation of 7-ethoxycoumarin and the hydroxylation of substituted and unsubstituted aromatics. However, since activities were quite low, a combination of site-specific mutagenesis and directed evolution was applied to produce 7800 variants of CYP116B3, which were screened via a newly developed high-throughput screening system based on the dealkylation of 7-ethoxycoumarin catalyzed by recombinant E. coli. The best mutant was found after four rounds of directed evolution and had a 240-fold increased deethylation activity toward 7-ethoxycoumarin (223 nmol product/nmol P450.min) and a 10-fold increased demethylation activity toward 7-methoxycoumarin (9 nmol product/nmol P4...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3354772</comments>
            <pubDate>Sun, 07 Mar 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3354772</guid>        </item>
        <item>
            <title>Bovine prolactin promotes the expression of human transferrin in the milk of transgenic mice.</title>
            <link>http://www.medworm.com/index.php?rid=3354771&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%3D20213525%26dopt%3DAbstract</link>
            <description>Authors: Li S, Guo X, Gong X, Xu M, Yan J, Huang Y, Ren Z
    The bovine prolactin vector was injected directly into the mammary glands of mice carrying the human transferrin transgene to investigate its effect on the production of human transferrin in milk. The mean levels of human transferrin in two experimental groups were increased by approx. 60% compared with the control group: 1143 +/- 196 ng/ml (experimental group 1; two injections) and 1160 +/- 189 ng/ml (experimental group 2; three injections) versus 714 +/- 75 ng/ml (control group). These findings suggest the potential utility of the prolactin vector for efficient expression of valuable pharmaceutical proteins in transgenic animal mammary glands.
    PMID: 20213525 [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=3354771</comments>
            <pubDate>Sun, 07 Mar 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3354771</guid>        </item>
        <item>
            <title>Fructooligosaccharide production by Penicillium expansum.</title>
            <link>http://www.medworm.com/index.php?rid=3354770&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%3D20213526%26dopt%3DAbstract</link>
            <description>Authors: Prata MB, Mussatto SI, Rodrigues LR, Teixeira JA
    Fructooligosaccharides (FOS) production by Penicillium expansum was evaluated. In a first stage, the best conditions for P. expansum growth and sporulation were established with potato/dextrose/agar being the most suitable medium at between 22 and 25 degrees C, giving good growth and good sporulation. The inocula from this medium were used for FOS production using shake-flask cultures, and yielded 0.58 g FOS/g sucrose (3.25 g FOS/l.h), demonstrating the potential of this strain for sucrose conversion to FOS.
    PMID: 20213526 [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=3354770</comments>
            <pubDate>Sun, 07 Mar 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3354770</guid>        </item>
        <item>
            <title>Novel method to obtain highly enriched cultures of adult rat Schwann cells.</title>
            <link>http://www.medworm.com/index.php?rid=3354769&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%3D20213527%26dopt%3DAbstract</link>
            <description>This study describes a novel and efficient method to enrich SCs by utilizing the differential detachment properties of the two cell types. In culture, cells were treated with two different media and the chelator, EGTA, which detached SCs faster than fibroblasts and allowed for easy isolation of SCs. Within seven days, high yields of SCs with a purity of greater than 99% were achieved. This was confirmed by immunostaining characterization and flow-cytometric analyses using an antibody against the p75 low affinity nerve growth factor receptor (p75LNGFR). The entire procedure was completed in approximately 21 days. This method has the advantage of being technically easier, faster, and more efficient than other previously described methods. An SC culture that was about 99% homogenous was achie...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3354769</comments>
            <pubDate>Sun, 07 Mar 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3354769</guid>        </item>
        <item>
            <title>Reconstruction and expression of the MRI-contrast protein, ferritin, with recombinant rabies vectors.</title>
            <link>http://www.medworm.com/index.php?rid=3354768&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%3D20213528%26dopt%3DAbstract</link>
            <description>In this study, the gene of a biomolecular contrast agent, ferritin, was successfully cloned into two rabies virus vectors, vaccine-based pCTN and street strain-based pNH. Recombinant virus granules were obtained and proved to express ferritin by RT-PCR after transfection of CTN-ferritin and NH-ferritin vector systems in BHK-21 cells. The recovered rabies virus-rCTN-ferritin was of similar ability to rNH-ferritin, which suggests the possibility of application of this safe and effective rabies vector system in delivery of diagnostic or therapeutic genes into the brain.
    PMID: 20213528 [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=3354768</comments>
            <pubDate>Sun, 07 Mar 2010 00:00:00 +0100</pubDate>
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        <item>
            <title>Cryopreservation of primary porcine liver cells in an organotypical sandwich model in a clinically relevant flat membrane bioreactor.</title>
            <link>http://www.medworm.com/index.php?rid=3354767&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%3D20213529%26dopt%3DAbstract</link>
            <description>This study showed that cryopreserved cells can recover liver-specific functions. This result has the potential to dramatically expand the clinical application of bioartificial liver supports.
    PMID: 20213529 [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=3354767</comments>
            <pubDate>Sun, 07 Mar 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3354767</guid>        </item>
        <item>
            <title>High-level expression of functional recombinant human coagulation factor VII in insect cells.</title>
            <link>http://www.medworm.com/index.php?rid=3354766&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%3D20213530%26dopt%3DAbstract</link>
            <description>Authors: Masroori N, Halabian R, Mohammadipour M, Roushandeh AM, Rouhbakhsh M, Najafabadi AJ, Fathabad ME, Salimi M, Shokrgozar MA, Roudkenar MH
    Recombinant coagulation factor VII (FVII) is used as a potential therapeutic intervention in hemophilia patients who produce antibodies against the coagulation factors. Mammalian cell lines provide low levels of expression, however, the Spodoptera frugiperda Sf9 cell line and baculovirus expression system are powerful systems for high-level expression of recombinant proteins, but due to the lack of endogenous vitamin K-dependent carboxylase, expression of functional FVII using this system is impossible. In the present study, we report a simple but versatile method to overcome the defect for high-level expression of the functional recombinant c...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3354766</comments>
            <pubDate>Sun, 07 Mar 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3354766</guid>        </item>
        <item>
            <title>Substrate specificity of ribose-5-phosphate isomerases from Clostridium difficile and Thermotoga maritima.</title>
            <link>http://www.medworm.com/index.php?rid=3276819&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%3D20155483%26dopt%3DAbstract</link>
            <description>Authors: Yeom SJ, Kim BN, Park CS, Oh DK
    The activity of ribose-5-phosphate isomerases (RpiB) from Clostridium difficile for D: -ribose isomerization was optimal at pH 7.5 and 40 degrees C, while that from Thermotoga maritima for L: -talose isomerization was optimal at pH 8.0 and 70 degrees C. C. difficile RpiB exhibited activity only with aldose substrates possessing hydroxyl groups oriented in the right-handed configuration (Fischer projections) at the C2 and C3 positions, such as D: -ribose, D: -allose, L: -talose, L: -lyxose, D: -gulose, and L: -mannose. In contrast, T. maritima RpiB displayed activity only with aldose substrates possessing hydroxyl groups configured the same direction at the C2, C3, and C4 positions, such as the D: - and L: -forms of ribose, talose, and allose.
  ...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3276819</comments>
            <pubDate>Sun, 14 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3276819</guid>        </item>
        <item>
            <title>pHsh vectors, a novel expression system of Escherichia coli for the large-scale production of recombinant enzymes.</title>
            <link>http://www.medworm.com/index.php?rid=3276818&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%3D20155484%26dopt%3DAbstract</link>
            <description>Authors: Wu H, Pei J, Jiang Y, Song X, Shao W
    Gene expression system Hsh is developed to increase enzyme production and to decrease the cost in the induction of gene expression in Escherichia coli. The vectors of Hsh system were constructed by combining a synthesized heat-shock promoter with a synthesized terminator and an origin of replication derived from pUC19 in which the expression of foreign genes was regulated by an alternative sigma factor, sigma(32) of E. coli. In comparison, the Hsh promoter gave a 2.4-fold higher production for xynIII gene encoding a xylanase than existing heat-shock inducible promoter p (L), 1.2-fold and 3-fold production for xar gene encoding a arabinosidase than trc and T(7) promoter, respectively. The flow-in-heat technique created a rapid rise in temper...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3276818</comments>
            <pubDate>Sun, 14 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3276818</guid>        </item>
        <item>
            <title>Fermentation of corn fiber hydrolysate to lactic acid by the moderate thermophile Bacillus coagulans.</title>
            <link>http://www.medworm.com/index.php?rid=3276817&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%3D20155485%26dopt%3DAbstract</link>
            <description>Authors: Bischoff KM, Liu S, Hughes SR, Rich JO
    A strain of Bacillus coagulans that converted mixed sugars of glucose, xylose, and arabinose to L: -lactic acid with 85% yield at 50 degrees C was isolated from composted dairy manure. The strain was tolerant to aldehyde growth inhibitors at 2.5 g furfural/l, 2.5 g 5-hydroxymethylfurfural/l, 2.5 g vanillin/l, and 1.2 g p-hydroxybenzaldehyde/l. In a simultaneous saccharification and fermentation process, the strain converted a dilute-acid hydrolysate of 100 g corn fiber/l to 39 g lactic acid/l in 72 h at 50 degrees C. Because of its inhibitor tolerance and ability to fully utilize pentose sugars, this strain has potential to be developed as a biocatalyst for the conversion of agricultural residues into valuable chemicals.
    PMID: 2015548...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3276817</comments>
            <pubDate>Sun, 14 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3276817</guid>        </item>
        <item>
            <title>Immobilization of glucose oxidase on Fe(3)O (4)/SiO (2) magnetic nanoparticles.</title>
            <link>http://www.medworm.com/index.php?rid=3276816&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%3D20155486%26dopt%3DAbstract</link>
            <description>Authors: Huang J, Zhao R, Wang H, Zhao W, Ding L
    Glucose oxidase (GOD) was covalently immobilized onto Fe(3)O(4)/SiO(2) magnetic nanoparticles (FSMNs) using glutaraldehyde (GA). Optimal immobilization was at pH 6 with 3-aminopropyltriethoxysilane at 2% (v/v), GA at 3% (v/v) and 0.143 g GOD per g carrier. The activity of immobilized GOD was 4,570 U/g at pH 7 and 50 degrees C. The immobilized GOD retained 80% of its initial activity after 6 h at 45 degrees C while free enzyme retained only 20% activity. The immobilized GOD maintained 60% of its initial activity after 6 cycles of repeated use and retained 75% of its initial activity after 1 month at 4 degrees C whereas free enzymes retained 62% of its activity.
    PMID: 20155486 [PubMed - as supplied by publisher] (Source: Biotechnology ...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3276816</comments>
            <pubDate>Sun, 14 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3276816</guid>        </item>
        <item>
            <title>Cell encapsulation using biopolymer gels for regenerative medicine.</title>
            <link>http://www.medworm.com/index.php?rid=3276824&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%3D20155383%26dopt%3DAbstract</link>
            <description>Authors: Hunt NC, Grover LM
    There has been a consistent increase in the mean life expectancy of the population of the developed world over the past century. Healthy life expectancy, however, has not increased concurrently. As a result we are living a larger proportion of our lives in poor health and there is a growing demand for the replacement of diseased and damaged tissues. While traditionally tissue grafts have functioned well for this purpose, the demand for tissue grafts now exceeds the supply. For this reason, research in regenerative medicine is rapidly expanding to cope with this new demand. There is now a trend towards supplying cells with a material in order to expedite the tissue healing process. Hydrogel encapsulation provides cells with a three dimensional environment sim...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3276824</comments>
            <pubDate>Sat, 13 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3276824</guid>        </item>
        <item>
            <title>Isolation and characterization of a novel glycogen synthase kinase-3 gene, GmGSK, in Glycine max L. that enhances abiotic stress tolerance in Saccharomyces cerevisiae.</title>
            <link>http://www.medworm.com/index.php?rid=3276823&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%3D20155384%26dopt%3DAbstract</link>
            <description>Authors: Zhang C, Zhao H, Liu Y, Li Q, Liu X, Tan H, Yuan C, Dong Y
    A novel glycogen synthase kinase-3 gene, GmGSK, was isolated from Glycine max. It is 1,596 bp in length with one ORF of 410 amino acids. Southern blot analysis revealed that it has at least two copies in the G. max genome. GmGSK, when transiently expressed in Nicotiana tabacum leaves, was localized in both cell membrane and cytoplasm. Northern blot analysis indicated that GmGSK is expressed in all tissues, with highest expression in the root. GmGSK can be induced by various abiotic stresses. When transformed with GmGSK, Saccharomyces cerevisiae exhibited enhanced resistance to salt and drought stress.
    PMID: 20155384 [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=3276823</comments>
            <pubDate>Sat, 13 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3276823</guid>        </item>
        <item>
            <title>Dual bio-responsive gene delivery via reducible poly(amido amine) and survivin-inducible plasmid DNA.</title>
            <link>http://www.medworm.com/index.php?rid=3276822&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%3D20155385%26dopt%3DAbstract</link>
            <description>Authors: Namgung R, Brumbach JH, Jeong JH, Yockman JW, Kim SW, Lin C, Zhong Z, Feijen J, Engbersen JF, Kim WJ
    A bioreducible poly(amido amine) (SS-PAA) gene carrier, known as poly (amido-butanol) (pABOL), was used to transfect a variety of cancer and non-cancer cell lines. To obtain cancer-specific transgene expression for therapeutic efficiency in cancer treatment, we constructed survivin-inducible plasmid DNA expressing the soluble VEGF receptor, sFlt-1, downstream of the survivin promoter (pSUR-sFlt-1). Cancer-specific expression of sFlt-1 was observed in the mouse renal carcinoma (RENCA) cell line. pABOL enhanced the efficiency of gene delivery compared to traditional carriers used in the past. Thus, a dual bio-responsive gene delivery system was developed by using bioreducible p(A...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3276822</comments>
            <pubDate>Sat, 13 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3276822</guid>        </item>
        <item>
            <title>A potentially immunologically inert derivative of the reverse tetracycline-controlled transactivator.</title>
            <link>http://www.medworm.com/index.php?rid=3276821&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%3D20155386%26dopt%3DAbstract</link>
            <description>Authors: Zaldumbide A, Weening S, Cramer SJ, Rabelink MJ, Verhaagen J, Hoeben RC
    The archetypical system for regulating heterologous gene expression in mammalian cells involves tetracycline-activated transactivators (rtTA). Binding of such transactivators to tet-operator-controlled promoters induces transcription. Immune responses directed against the transactivator proteins may limit the applicability of this system in immune-competent hosts. To circumvent such immune responses the immune evasion mechanism of the Epstein-Barr virus Nuclear-Antigen 1 was exploited. Our data show that fusion of the rtTA with the EBNA-1 derived Gly-Ala repeat yielded an efficient transactivator with no detectable activity in absence of inducer. Antigenic peptides of the fusion protein were not presented ...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3276821</comments>
            <pubDate>Sat, 13 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3276821</guid>        </item>
        <item>
            <title>Surface properties and sub-surface aggregate assimilation of rhamnolipid surfactants in different aqueous systems.</title>
            <link>http://www.medworm.com/index.php?rid=3276820&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%3D20155387%26dopt%3DAbstract</link>
            <description>Authors: Raza ZA, Khalid ZM, Khan MS, Banat IM, Rehman A, Naeem A, Saddique MT
    Tensioactive properties of rhamnolipids produced by a Pseudomonas aeruginosa strain were investigated in the presence or absence of Sr(2+) or Pb(2+). Surface and interfacial properties, and aggregate forming properties and morphologies were studied by various techniques including scanning electron microscopy. When the pH of a rhamnolipid aqueous solution (40 mg/l) was increased from 5 to 8, irregular vesicles gradually took the shape of oligo-vesicles, then regular vesicles and finally smaller spherical vesicles. Addition of metal ions controlled the aggregates' morphology and stability, and influenced the surface and interfacial behavior of rhamnolipid solutions.
    PMID: 20155387 [PubMed - as supplied by ...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3276820</comments>
            <pubDate>Sat, 13 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3276820</guid>        </item>
        <item>
            <title>Functional expression of Phanerochaete chrysosporium cellobiose dehydrogenase flavin domain in Escherichia coli.</title>
            <link>http://www.medworm.com/index.php?rid=3255128&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%3D20140751%26dopt%3DAbstract</link>
            <description>Authors: Desriani , Ferri S, Sode K
    Cellobiose dehydrogenase (CDH; EC 1.1.99.18) is an extracellular glycosylated protein composed of two distinct domains, a C-terminal catalytic flavin domain and an N-terminal cytochrome-b-type heme domain, which transfers electrons from the flavin domain to external electron acceptors. The soluble flavin domain of the Phanerochaete chrysosporium CDH was successfully expressed in Escherichia coli. The enzyme showed dye-mediated CDH activity higher than that of the complete CDH, composed of flavin domain and heme domain, prepared using Pichia pastoris as the host microorganism. The ability to conveniently express the recombinant CDH flavin domain in E. coli provides great opportunities for the molecular engineering of the catalytic properties of CDH.
 ...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3255128</comments>
            <pubDate>Sun, 07 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3255128</guid>        </item>
        <item>
            <title>Quick PCR based diagnosis of typhoid using specific genetic markers.</title>
            <link>http://www.medworm.com/index.php?rid=3255129&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%3D20140635%26dopt%3DAbstract</link>
            <description>Authors: Kumar A, Balachandran Y, Gupta S, Khare S, Suman 
    A quick multiplex PCR based detection method was developed for early diagnosis of typhoid using specific genetic markers of S. typhi. Primers of tyv gene, flag gene, viaB gene and ratA gene confirmed the specificity and sensitivity of the PCR. The serum samples of the suspected typhoid patients were taken directly for PCR without culturing and isolating genomic DNA. Overall diagnosis required 2 h which is the least time ever reported for a PCR based methods. The sensitivity of the method is up to 5 fg genomic DNA. The genetic markers are specific and the four pairs of primers give selective amplification and differentiate S. typhi from closely related S. typhimurium.
    PMID: 20140635 [PubMed - as supplied by publisher] (Sourc...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3255129</comments>
            <pubDate>Sat, 06 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3255129</guid>        </item>
        <item>
            <title>Modulating the pharmacokinetics of therapeutic antibodies.</title>
            <link>http://www.medworm.com/index.php?rid=3244691&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%3D20131077%26dopt%3DAbstract</link>
            <description>This article reviews the main strategies for pharmacokinetic enhancement, primarily chemical conjugates and recombinant fusions that increase apparent molecular weight or hydrodynamic radius or interact with serum albumin which itself has a long plasma half-life. We highlight the key chemical linkage methods that preserve antibody function and retain stability and look forward to the next generation of technologies which promise to make better quality pharmaceuticals with lower side effects. Although restricted to antibodies, all of the approaches covered can be applied to other biotherapeutics.
    PMID: 20131077 [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=3244691</comments>
            <pubDate>Thu, 04 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3244691</guid>        </item>
        <item>
            <title>Studies supporting the use of mechanical mixing in large scale beer fermentations.</title>
            <link>http://www.medworm.com/index.php?rid=3244690&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%3D20131078%26dopt%3DAbstract</link>
            <description>Authors: Nienow AW, McLeod G, Hewitt CJ
    Brewing fermentations have traditionally been undertaken without the use of mechanical agitation, with mixing being provided only by the fluid motion induced by the CO(2) evolved during the batch process. This approach has largely been maintained because of the belief in industry that rotating agitators would damage the yeast. Recent studies have questioned this view. At the bench scale, brewer's yeast is very robust and withstands intense mechanical agitation under aerobic conditions without observable damage as measured by flow cytometry and other parameters. Much less intense mechanical agitation also decreases batch fermentation time for anaerobic beer production by about 25% compared to mixing by CO(2) evolution alone with a small change in ...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3244690</comments>
            <pubDate>Thu, 04 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3244690</guid>        </item>
        <item>
            <title>Construction of a direct starch-fermenting industrial strain of Saccharomyces cerevisiae producing glucoamylase, alpha-amylase and debranching enzyme.</title>
            <link>http://www.medworm.com/index.php?rid=3244689&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%3D20131079%26dopt%3DAbstract</link>
            <description>Authors: Kim JH, Kim HR, Lim MH, Ko HM, Chin JE, Lee HB, Kim IC, Bai S
    To develop a strain of Saccharomyces cerevisiae that produces ethanol directly from starch, two integrative vectors were constructed to allow the simultaneous multiple integration of the Aspergillus awamori glucoamylase gene (GA1) and the Debaryomyces occidentalis alpha-amylase gene (AMY) and glucoamylase with debranching activity gene (GAM1) into the chromosomes of an industrial strain of S. cerevisiae. The GA1 and AMY genes were constitutively expressed under the ADC1 promoter in S. cerevisiae using the double delta-integration system. The GAM1 gene was constitutively expressed under the corresponding promoter using the double 18S rDNA-integration system. The recombinant industrial strain secreting biologically ac...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3244689</comments>
            <pubDate>Thu, 04 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3244689</guid>        </item>
        <item>
            <title>Regioselective carboxylation of catechol by 3,4-dihydroxybenzoate decarboxylase of Enterobacter cloacae P.</title>
            <link>http://www.medworm.com/index.php?rid=3244688&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%3D20131080%26dopt%3DAbstract</link>
            <description>Authors: Yoshida T, Inami Y, Matsui T, Nagasawa T
    3,4-Dihydroxybenzoate decarboxylase in Enterobacter cloacae P241 was induced by adding 3,4-dihydroxybenzoic acid, 3-hydroxybenzoic acid, 3,4,5-trihydroxybenzoic acid or 4-acetamidobenzoic acid to the culture medium. After stabilizing the enzyme activity by adding 5 mM dithiothreitol and 20 mM Na(2)S(2)O(3) to a cell-free extract, catechol at 50 mM was carboxylated in the presence of 3 M KHCO(3) to 3,4-dihydroxybenzoic acid with a molar conversion ratio of 28% after 14 h at 30 degrees C.
    PMID: 20131080 [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=3244688</comments>
            <pubDate>Thu, 04 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3244688</guid>        </item>
        <item>
            <title>Genetic changes that increase 5-hydroxymethyl furfural resistance in ethanol-producing Escherichia coli LY180.</title>
            <link>http://www.medworm.com/index.php?rid=3244687&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%3D20131081%26dopt%3DAbstract</link>
            <description>This study shows EMFR9, a furfural-tolerant mutant of ethanologenic E. coli LY180, has also acquired tolerance to 5-hydroxymethyl furfural (5-HMF). The mechanism of action of 5-HMF and furfural appear similar. Furan tolerance results primarily from lower expression of yqhD and dkgA, two furan reductases with a low K(m) for NADPH. Furan tolerance was also increased by adding plasmids encoding a NADPH/NADH transhydrogenase (pntAB). Together, these results support the hypothesis that the NADPH-dependent reduction of furans by YqhD and DkgA inhibits growth by competing with biosynthesis for this limiting cofactor.
    PMID: 20131081 [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=3244687</comments>
            <pubDate>Thu, 04 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3244687</guid>        </item>
        <item>
            <title>In vitro release behavior and cytotoxicity of doxorubicin-loaded gold nanoparticles in cancerous cells.</title>
            <link>http://www.medworm.com/index.php?rid=3244686&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%3D20131082%26dopt%3DAbstract</link>
            <description>Authors: Asadishad B, Vossoughi M, Alamzadeh I
    Doxorubicin (DOX), a common cancer chemotherapeutics, was conjugated to folate-modified thiolated-polyethylene glycol-functionalized gold nanoparticles. The in vitro, controlled release behavior of DOX-loaded gold nanoparticles was observed using porous dialysis membranes (cut-off = 2 kDa). DOX-loaded gold nanoparticles had higher cytotoxicity for folate-receptor-positive cells (KB cells) compared to folate-receptor-negative cells (A549 cells) which were 48 and 62% viable for 10 muM doxorubicin, respectively. This indicates the potential of these nano-carriers for targeted-delivery. In addition, healthy cell viability was 69% for 10 muM free doxorubicin whereas for the same content of drug in DOX-loaded nanoparticles healthy cell viability...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3244686</comments>
            <pubDate>Thu, 04 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3244686</guid>        </item>
        <item>
            <title>Mesenchymal stem cells derived from human umbilical cord ameliorate ischemia/reperfusion-induced acute renal failure in rats.</title>
            <link>http://www.medworm.com/index.php?rid=3244685&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%3D20131083%26dopt%3DAbstract</link>
            <description>Authors: Cao H, Qian H, Xu W, Zhu W, Zhang X, Chen Y, Wang M, Yan Y, Xie Y
    Mesenchymal stem cells (MSCs) are candidates for cell therapy of kidney diseases. However, the application of MSC derived from human umbilical cord (UC-MSC) in treating acute renal failure (ARF) has not been reported. UC-MSCs, 10(6), were transplantated via the left carotid artery into ARF rats which was established by clamping bilateral pedicles for 60 min and reperfusing. Serum creatinine and urea nitrogen decreased 4.8 times and 3.6 times as well as caspase-3 and IL-1beta decreased 5.8 times and 9 times compared to control groups, respectively. The percent of proliferative cell nuclear antigen (PCNA)-positive cells (53% +/- 7.5%) was higher than that in the control groups (17% +/- 4.5%). In addition, the tran...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3244685</comments>
            <pubDate>Thu, 04 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3244685</guid>        </item>
        <item>
            <title>Cholesterol biotransformation to androsta-1,4-diene-3,17-dione by growing cells of Chryseobacterium gleum.</title>
            <link>http://www.medworm.com/index.php?rid=3244692&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%3D20127502%26dopt%3DAbstract</link>
            <description>Authors: Chaudhari PN, Chaudhari BL, Chincholkar SB
    Cholesterol oxidase activity was studied during biotransformation of cholesterol to androsta-1,4-diene-3,17-dione (ADD) by Chryseobacterium gleum. Spent LB media, containing cholesterol (3 mM approximately 1 g l(-1)) where the bacterium was grown for 24 h, at 30 degrees C with constant shaking at 120 rpm, had the highest enzyme activity (167 U mg(-1)). The growing cells produced 0.076 g ADD from 1 g cholesterol l(-1).
    PMID: 20127502 [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=3244692</comments>
            <pubDate>Wed, 03 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3244692</guid>        </item>
        <item>
            <title>Improvement in organophosphorus hydrolase activity of cell surface-engineered yeast strain using Flo1p anchor system.</title>
            <link>http://www.medworm.com/index.php?rid=3224143&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%3D20111980%26dopt%3DAbstract</link>
            <description>Authors: Fukuda T, Tsuchiyama K, Makishima H, Takayama K, Mulchandani A, Kuroda K, Ueda M, Suye SI
    Organophosphorus hydrolase (OPH) hydrolyzes organophosphorus esters. We constructed the yeast-displayed OPH using Flo1p anchor system. In this system, the N-terminal region of the protein was fused to Flo1p and the fusion protein was displayed on the cell surface. Hydrolytic reactions with paraoxon were carried out during 24 h of incubation of OPH-displaying cells at 30 degrees C. p-Nitrophenol produced in the reaction mixture was detected by HPLC. The strain with highest activity showed 8-fold greater OPH activity compared with cells engineered using glycosylphosphatidylinositol anchor system, and showed 20-fold greater activity than Escherichia coli using the ice nucleation protein anch...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3224143</comments>
            <pubDate>Fri, 29 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3224143</guid>        </item>
        <item>
            <title>Encapsulation of recombinant E. coli expressing cyclopentanone monooxygenase in polyelectrolyte complex capsules for Baeyer-Villiger biooxidation of 8-oxabicyclo[3.2.1]oct-6-en-3-one.</title>
            <link>http://www.medworm.com/index.php?rid=3224142&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%3D20111981%26dopt%3DAbstract</link>
            <description>Authors: Huc&amp;#xED;k M, Bu&amp;#x10D;ko M, Gemeiner P, Stefuca V, Vikartovsk&amp;#xE1; A, Mihovilovi&amp;#x10D; MD, Rudroff F, Iqbal N, Chorv&amp;#xE1;t D, Lac&amp;#xED;k I
    Recombinant Escherichia coli cells, over-expressing cyclopentanone monooxygenase activity, were immobilized in polyelectrolyte complex capsules, made of sodium alginate, cellulose sulfate, poly(methylene-co-guanidine), CaCl(2) and NaCl. More than 90% of the cell viability was preserved during the encapsulation process. Moreover, the initial enzyme activity was fully maintained within encapsulated cells while it halved in free cells. Both encapsulated and free cells reached the end point of the Baeyer-Villiger biooxidation of 8-oxabicyclo[3.2.1]oct-6-en-3-one to 4,9-dioxabicyclo[4.2.1]non-7-en-3-one at the same time (48 h). Similarly, th...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3224142</comments>
            <pubDate>Fri, 29 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3224142</guid>        </item>
        <item>
            <title>Screening of DNA aptamer which binds to alpha-synuclein.</title>
            <link>http://www.medworm.com/index.php?rid=3224140&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%3D20111982%26dopt%3DAbstract</link>
            <description>Authors: Tsukakoshi K, Harada R, Sode K, Ikebukuro K
    alpha-Synuclein is a native, unfolded protein that causes several neurodegenerative diseases such as dementia with Lewy bodies and Parkinson's disease. We have now identified the first DNA aptamers against alpha-synuclein using native PAGE applied to the SELEX method. We call this aptamer &quot;M5-15&quot;; it is the alpha-synuclein-bound aptamer and was isolated after four cycles of screening. M5-15 is composed of three stem-loop structures that may play an important role in the binding to alpha-synuclein. Moreover, M5-15 specifically binds to the alpha-synuclein monomer and oligomer. We expect that this aptamer will become a useful tool in alpha-synuclein analysis and diagnosis.
    PMID: 20111982 [PubMed - as supplied by publisher] (Source:...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3224140</comments>
            <pubDate>Fri, 29 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3224140</guid>        </item>
        <item>
            <title>Enhanced plumbagin production from in vitro cultures of Drosera burmanii using elicitation.</title>
            <link>http://www.medworm.com/index.php?rid=3224139&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%3D20112127%26dopt%3DAbstract</link>
            <description>Authors: Putalun W, Udomsin O, Yusakul G, Juengwatanatrakul T, Sakamoto S, Tanaka H
    Methyl jasmonate, 50 muM, 0.5 mg yeast extract/l and 100 mg chitosan/l stimulated plumbagin production in Drosera burmanii whole plant cultures after 6 days of elicitation. Yeast extract (0.5 mg/l) was the most efficient enhancing plumbagin production in roots of D. burmanii to 8.8 +/- 0.5 mg/g dry wt that was 3.5-fold higher than control plants.
    PMID: 20112127 [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=3224139</comments>
            <pubDate>Fri, 29 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3224139</guid>        </item>
        <item>
            <title>10-Hydroxycamptothecin produced by a new endophytic Xylaria sp., M20, from Camptotheca acuminata.</title>
            <link>http://www.medworm.com/index.php?rid=3224138&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%3D20112128%26dopt%3DAbstract</link>
            <description>Authors: Liu K, Ding X, Deng B, Chen W
    A new 10-hydroxycamptothecin (HCPT)-producing fungus was isolated from Camptotheca acuminata. The strain was classified as a Xylaria sp. based on the internal transcribed spacer and 18S rDNA gene analysis. All elicitors tested, except methyl jasmonate, increased HCPT production in submerged culture. The maximum yield was 5.4 mg HCPT/l(-1), when salicylic acid was added at 0.1 mM to the culture medium.
    PMID: 20112128 [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=3224138</comments>
            <pubDate>Fri, 29 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3224138</guid>        </item>
        <item>
            <title>Erratum to: Enhanced tolerance of transgenic tall fescue plants overexpressing 2-Cys peroxiredoxin against methyl viologen and heat stresses.</title>
            <link>http://www.medworm.com/index.php?rid=3153942&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%3D20054609%26dopt%3DAbstract</link>
            <description>Authors: Kim KH, Alam I, Lee KW, Sharmin SA, Kwak SS, Lee SY, Lee BH
    
    PMID: 20054609 [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=3153942</comments>
            <pubDate>Thu, 07 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3153942</guid>        </item>
        <item>
            <title>Applications of membrane techniques for purification of natural products.</title>
            <link>http://www.medworm.com/index.php?rid=3146752&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%3D20049625%26dopt%3DAbstract</link>
            <description>Authors: Li J, Chase HA
    The recent development of various membrane-based techniques for the purification of valuable natural products is reviewed and covers the important research that has been conducted in the last 5 years on the utilization of microfiltration, ultrafiltration and nanofiltration techniques, either carried out on their own or coupled with other separation techniques, in order to achieve concentration and purification of natural products from their biological source. There is also a special focus on the research that has been undertaken to overcome the membrane fouling encountered in their usage.
    PMID: 20049625 [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=3146752</comments>
            <pubDate>Tue, 05 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3146752</guid>        </item>
        <item>
            <title>Platelet-rich plasma and 1,25(OH)(2) vitamin D (3) synergistically stimulate osteogenic differentiation of adult human mesenchymal stem cells.</title>
            <link>http://www.medworm.com/index.php?rid=3139585&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%3D20047066%26dopt%3DAbstract</link>
            <description>Authors: Feng Y, Sun Y, Jia W, Zhang C
    Mesenchymal stem cell proliferation and differentiation are regulated by growth factors and systemic hormones in a concerted manner. We have examined the effects of platelet-rich plasma (PRP) and its interaction with 1,25(OH)(2) vitamin D(3) [1,25(OH)(2)D(3)] on the differentiation and proliferation of human mesenchymal stem cells (hMSCs). PRP stimulated cell proliferation in a manner inversely proportional to the dose. Exposure to PRP inhibited hMSC osteogenic differentiation. Co-treatment with PRP and 1,25(OH)(2)D(3), however, synergistically stimulated osteogenic differentiation. Serial co-treatment with PRP and 1,25(OH)(2)D(3) showed that this synergistic effect was due to the modulation of a 1,25(OH)(2)D(3)-induced differentiation by PRP rath...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3139585</comments>
            <pubDate>Sun, 03 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3139585</guid>        </item>
        <item>
            <title>Mycogenic metal nanoparticles: progress and applications.</title>
            <link>http://www.medworm.com/index.php?rid=3139584&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%3D20047067%26dopt%3DAbstract</link>
            <description>Authors: Gade A, Ingle A, Whiteley C, Rai M
    Nanotechnology is relevant to diverse fields of science and technology. Due to the many advantages over non-biological systems, several research groups have exploited the use of biological systems for the synthesis of nanoparticles. Among the different microbes used for the synthesis of nanoparticles, fungi are efficient candidates for fabrication of metal nanoparticles both intra- and extracellulary. The nanoparticles synthesized using fungi present good polydispersity, dimensions and stability. The potential applications of nanotechnology and nanoparticles in different fields have revolutionized the health care, textile and agricultural industries and they are reviewed here.
    PMID: 20047067 [PubMed - as supplied by publisher] (Source: Bi...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3139584</comments>
            <pubDate>Sun, 03 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3139584</guid>        </item>
        <item>
            <title>Fusion expression of cecropin B-like antibacterial peptide in Escherichia coli and preparation of its antiserum.</title>
            <link>http://www.medworm.com/index.php?rid=3139583&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%3D20047068%26dopt%3DAbstract</link>
            <description>Authors: Yu F, Wang J, Zhang P, Hong Y, Liu W
    Antibacterial peptides have a broad range of antibacterial properties that makes them highly toxic for expression in Escherichia coli. For prepare an antiserum to detect these peptides, we developed a cecropin B mutant with a green fluorescent protein fusion partner resulting in high expression of a 37 kDa fusion peptide in E. coli with a yield of 7.9 mg/l culture medium after purification on Ni-IDA resin. Guinea pigs when immunized with the fusion peptide produced a specific antiserum which titers in excess of 1:25,600.
    PMID: 20047068 [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=3139583</comments>
            <pubDate>Sun, 03 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3139583</guid>        </item>
        <item>
            <title>Relationship between glucose catabolism and xanthan production in Xanthomonas oryzae pv. oryzae.</title>
            <link>http://www.medworm.com/index.php?rid=3130012&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%3D20039099%26dopt%3DAbstract</link>
            <description>Authors: Kim SY, Lee BM, Cho JY
    Two genes involved in central carbon metabolism were inactivated to modulate intracellular glucose 6-phosphate and to evaluate its effects on xanthan production in wild-type Xanthomonas oryzae pv. oryzae. Upon the inactivation of the phosphogluconate dehydratase gene (edd), intracellular glucose 6-phosphate increased from 0.05 to 1.17 mmol/g (dry cell wt). This was accompanied by increased xanthan production of up to 2.55 g/l (culture medium). In contrast, inactivation of 6-phosphogluconate dehydrogenase gene (gndA) did not influence intracellular glucose 6-phosphate nor xanthan production. The intracellular availability of glucose 6-phosphate is proposed as a rate-limiting factor in xanthan production, and it may be possible to increases production of x...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3130012</comments>
            <pubDate>Tue, 29 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3130012</guid>        </item>
        <item>
            <title>Purification and characterization of an anti-Prelog alcohol dehydrogenase from Oenococcus oeni that reduces 2-octanone to (R)-2-octanol.</title>
            <link>http://www.medworm.com/index.php?rid=3122583&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%3D20035369%26dopt%3DAbstract</link>
            <description>Authors: Meng F, Xu Y
    An anti-Prelog alcohol dehydrogenase from Oenococcus oeni that reduces 2-octanone to (R)-2-octanol was purified by 26-fold to homogeneity. The enzyme had a homodimeric structure consisting of 49 kDa subunits, required NADPH, but not NADH, as a cofactor and was a Zn-independent short-chain dehydrogenase. Aliphatic methyl ketones (chain length &amp;gt;/=6 carbon atoms) and aromatic methyl ketones were the preferred substrates for the enzyme, the best being 2-octanone. Maximum enzyme activity with 2-octanone was at 45 degrees C and at pH 8.0.
    PMID: 20035369 [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=3122583</comments>
            <pubDate>Fri, 25 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3122583</guid>        </item>
        <item>
            <title>Chitinolytic and antifungal activity of a Bacillus pumilus chitinase expressed in Arabidopsis.</title>
            <link>http://www.medworm.com/index.php?rid=3122582&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%3D20035370%26dopt%3DAbstract</link>
            <description>Authors: Dehestani A, Kazemitabar K, Ahmadian G, Jelodar NB, Salmanian AH, Seyedi M, Rahimian H, Ghasemi S
    The Bacillus pumilus SG2 chitinase gene (ChiS) and its truncated form lacking chitin binding (ChBD) and fibronectin type III (FnIII) domains were transformed to Arabidopsis plants and the expression, functionality and antifungal activity of the recombinant proteins were investigated. Results showed that while the two enzyme forms showed almost equal hydrolytic activity toward colloidal chitin, they exhibited a significant difference in antifungal activity. Recombinant ChiS in plant protein extracts displayed a high inhibitory effect on spore germination and radial growth of hyphae in Alternaria brassicicola, Fusarium graminearum and Botrytis cinerea, while the activity of the trun...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3122582</comments>
            <pubDate>Fri, 25 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3122582</guid>        </item>
        <item>
            <title>Human dermal fibroblast proliferation activity of usimine-C from Antarctic lichen Ramalina terebrata.</title>
            <link>http://www.medworm.com/index.php?rid=3122581&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%3D20035371%26dopt%3DAbstract</link>
            <description>Authors: Lee SG, Koh HY, Oh H, Han SJ, Kim IC, Lee HK, Yim JH
    Type I collagen is the major structural protein in dermis and its presence is used to monitor skin cell proliferation and aging. Recently, novel usimine compounds have been found in the Antarctic lichen Ramalina terebrata. In the present study, usimine-C induced cell proliferation of human dermal fibroblast, CCD-986SK, up to 1.6-fold after treating with 90 mug/ml for 48 h. Type I procollagen synthesis was significantly increased 1.3-fold, 3-fold, and 5-fold after treating with 0.14, 0.72, and 3.6 mug usimine-C/ml for 24 h, respectively, whereas no significant increase in type I procollagen was observed after treating with usimine-A or -B. Usimines are usnic acid derivatives. Considering that the difference among the derivati...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3122581</comments>
            <pubDate>Fri, 25 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3122581</guid>        </item>
        <item>
            <title>Controlling the adhesion of the diatom Navicula perminuta using poly(N-isopropylacrylamide-co-N-(1-phenylethyl) acrylamide) films.</title>
            <link>http://www.medworm.com/index.php?rid=3122580&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%3D20035372%26dopt%3DAbstract</link>
            <description>Authors: Cordeiro AL, Pettit ME, Callow ME, Callow JA, Werner C
    Poly(N-isopropylacrylamide)-co-N-(1-phenylethyl) acrylamide [P(NIPAAm-co-PEAAm)] thermo-responsive thin films with a lower critical solution temperature (LCST) adjusted to fit marine applications were used to investigate the effect of changes in the wetting properties of a surface on the adhesion of the diatom Navicula perminuta, an organism which forms slime films on surfaces immersed in an aquatic environment. Although the strength of attachment of cells was affected by whether the film was collapsed or expanded, no significant decrease in adhesion strength occurred upon temperature decrease. The effects were attributed to possible strong interactions between the hydrophobic segments of the responsive film when collapsed...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3122580</comments>
            <pubDate>Fri, 25 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3122580</guid>        </item>
        <item>
            <title>Homologous overexpression of a lipase from Burkholderia cepacia using the lambda Red recombinase system.</title>
            <link>http://www.medworm.com/index.php?rid=3122587&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%3D20033831%26dopt%3DAbstract</link>
            <description>Authors: Jia B, Yang JK, Liu WS, Li X, Yan YJ
    Red recombinase system of the lambda phage is widely used for recombination of short linear DNA fragments and genome. Using this system, we obtained T7 RNA polymerase (RNAP) substitution mutants in Burkholderia cepacia. To test the expression abilities of the T7 mutants, four different lipase expression vectors were transformed and the lipase activity of these recombinants was evaluated. Our results suggest that 500 nt homology between the unit and the genome is sufficient to generate mutations and this strategy enables the rapid establishment of mutant strains with efficiencies of 85%. After expression and purification, the highest purified lipase activity obtained was 3,990 U/l, nearly triple that of the wild-type organism.
    PMID: 2003...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3122587</comments>
            <pubDate>Thu, 24 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3122587</guid>        </item>
        <item>
            <title>Molecular characterization of flavonol synthase from poplar and its application to the synthesis of 3-O-methylkaempferol.</title>
            <link>http://www.medworm.com/index.php?rid=3122586&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%3D20033832%26dopt%3DAbstract</link>
            <description>Authors: Kim BG, Joe EJ, Ahn JH
    Biosynthesis of flavonoid derivatives requires enzyme(s) having high reactivity as well as regioselectivity. We have synthesized 3-O-kaempferol from naringenin using two enzymes. The first reaction, in which naringenin is converted to kaempferol, is mediated by flavonol synthase (FLS). An FLS (PFLS) with strong catalytic activity was cloned and characterized from the genome sequence of the poplar (Populus deltoides). PFLS consists of a 1,008 bp ORF encoding a 38 kDa protein. PFLS was expressed in Escherichia coli with a glutathione-S-transferase (GST) tagging. The purified recombinant PFLS was characterized. Catalytically, it was more efficient than the previously characterized FLSs. A mixture of two E. coli transformants harboring either PFLS or ROMT9 (...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3122586</comments>
            <pubDate>Thu, 24 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3122586</guid>        </item>
        <item>
            <title>Strain improvement of Lactobacillus lactis for D: -lactic acid production.</title>
            <link>http://www.medworm.com/index.php?rid=3122585&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%3D20033833%26dopt%3DAbstract</link>
            <description>Authors: Joshi DS, Singhvi MS, Khire JM, Gokhale DV
    Three mutants, isolated by repeated UV mutagenesis of Lactobacillus lactis NCIM 2368, produced increased D: -lactic acid concentrations. These mutants were compared with the wild type using 100 g hydrolyzed cane sugar/l in the fermentation medium. One mutant, RM2-24, produced 81 g lactic acid/l which was over three times that of the wild type. The highest D: -lactic acid (110 g/l) in batch fermentation was obtained with 150 g cane sugar/l with a 73% lactic acid yield. The mutant utilizes cellobiose efficiently, converting it into D: -lactic acid suggesting the presence of cellobiase. Thus, this strain could be used to obtain D: -lactic acid from cellulosic materials that are pre-hydrolyzed with cellulase.
    PMID: 20033833 [PubMed - ...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3122585</comments>
            <pubDate>Thu, 24 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3122585</guid>        </item>
        <item>
            <title>A novel basic fibroblast growth factor delivery system fabricated with heparin-incorporated fibrin-fibronectin matrices for repairing rat sciatic nerve disruptions.</title>
            <link>http://www.medworm.com/index.php?rid=3122584&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%3D20033834%26dopt%3DAbstract</link>
            <description>Authors: Han H, Ao Q, Chen G, Wang S, Zuo H
    Autologous nerve grafts are widely used in bridging critical gaps of peripheral nerves, but they remain associated with high morbidity of the donor site and lack of full recovery. As an alternative, we have focused on chitosan nerve conduits filled with a heparin-incorporated fibrin-fibronectin matrix serving as delivery systems for basic fibroblast growth factor (bFGF). The artificial nerve conduits were used for repairing sciatic nerve defects of 10 mm in adult rats. Three months post-operation, the conduction velocity recovery index (CVRI) and the muscle restoration rate (MRR) in animals of the experimental group were 32 +/- 4.1 and 77.4 +/- 7.9%, respectively, which were significantly higher than those of the PBS control group (17.8 +/- 1...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3122584</comments>
            <pubDate>Thu, 24 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3122584</guid>        </item>
        <item>
            <title>Anti-melanoma activity of hybrid peptide P18 and its mechanism of action.</title>
            <link>http://www.medworm.com/index.php?rid=3057249&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%3D19957017%26dopt%3DAbstract</link>
            <description>Authors: Huang W, Lu L, Shao X, Tang C, Zhao X
    The anticancer properties and mechanism of action of a hybrid peptide -P18 were investigated. It had significant cytotoxic activity against human melanoma cells and low toxicity to normal NIH-3T3 cells. It also induced cell death via necrosis rather than classical apoptosis. The peptide targets the cells membrane, causing a sustained depolarization of transmembrane potential resulting in the cells swelling and bursting, thereby triggering cytolysis. P18 peptide initially binds to the melanoma cell membrane via electrostatic interaction, causing the cell membrane to rupture. The effect may be mediated by the amphiphilic alpha-helical structure of P18 peptide, coupled with changes in ion channels and an increase in plasma membrane permeabili...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3057249</comments>
            <pubDate>Thu, 03 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3057249</guid>        </item>
        <item>
            <title>Proteomic analysis of Parietaria judaica pollen and allergen profiling by an immunoproteomic approach.</title>
            <link>http://www.medworm.com/index.php?rid=3057254&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%3D19953298%26dopt%3DAbstract</link>
            <description>Authors: Barranca M, Fontana S, Taverna S, Duro G, Zanella-Cleon I, Becchi M, De Leo G, Alessandro R
    Parietaria judaica pollen is a common cause of airway allergic disease in the Mediterranean area. Proteome analysis of mature Parietaria judaica pollen by two-dimensional gel electrophoresis (2-DE) and mass spectrometry has established the first reference proteome map of this weed. Proteins involved in a variety of cellular functions as well as the occurrence of allergens were detected. By using 2-DE and immunoblotting with sera from Parietaria judaica allergic patients we obtained a more detailed characterization of Parietaria judaica allergen profile so to improve our comprehension of the pathogenesis of pollen-induced allergic reaction.
    PMID: 19953298 [PubMed - as supplied by pub...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3057254</comments>
            <pubDate>Wed, 02 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3057254</guid>        </item>
        <item>
            <title>Pistil drip following pollination: a simple in planta Agrobacterium-mediated transformation in cotton.</title>
            <link>http://www.medworm.com/index.php?rid=3057253&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%3D19953299%26dopt%3DAbstract</link>
            <description>Authors: Tianzi C, Shenjie W, Jun Z, Wangzhen G, Tianzhen Z
    Transgenic cotton plants were developed by pistil drip inoculation in a solution containing Agrobacterium carrying a gene for resistance to the herbicide Basta (bar), 10% (w/v) sucrose, 0.05% (v/v) Silwet L-77 and 40 mg acetosyringone l(-1). Pistil drip during 17:00-19:00 on the first day of flowering resulted in 0.07-0.17% Basta-resistant plants/number of viable seeds generated, and stigma excision prior to pistil drip during this time period gave rise to a transformation efficiency of 0.46-0.93%, in contrast with 0.04-0.06% generated from pistil drip during 9:00-11:00 on the second day of flowering. PCR and Southern blot analysis confirmed the integration of the bar gene into the cotton genome, and a T1 and T2 generation her...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3057253</comments>
            <pubDate>Wed, 02 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3057253</guid>        </item>
        <item>
            <title>Overexpression of a soybean O-acetylserine (thiol) lyase-encoding gene GmOASTL4 in tobacco increases cysteine levels and enhances tolerance to cadmium stress.</title>
            <link>http://www.medworm.com/index.php?rid=3057252&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%3D19953300%26dopt%3DAbstract</link>
            <description>Authors: Ning H, Zhang C, Yao Y, Yu D
    O-Acetylserine (thiol) lyase (OASTL, EC 2.5.1.47) catalyzes the final step in cysteine biosynthesis. The soybean GmOASTL4 gene was overexpressed in tobacco. Transgenic plants showed markedly increased accumulation of transcripts and higher cysteine content compared with the wild-type. Upon exposure to cadmium stress, OASTL activity and cysteine levels increased significantly in transgenic plants. Cadmium accumulation and the activity of both superoxide dismutase and catalase enzymes were enhanced in transformants. These results demonstrate that overexpression of GmOASTL4 in tobacco can enhance cysteine levels and increase tolerance to cadmium stress.
    PMID: 19953300 [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=3057252</comments>
            <pubDate>Wed, 02 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3057252</guid>        </item>
        <item>
            <title>Production of a recombinant alkane hydroxylase (AlkB2) from Alcanivorax borkumensis.</title>
            <link>http://www.medworm.com/index.php?rid=3057251&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%3D19953301%26dopt%3DAbstract</link>
            <description>In this study, AlkB2 from A. borkumensis SK2 was expressed in Escherichia coli to examine the functionality of AlkB2 as a hydroxylating enzyme. Furthermore, the activity of the enzyme in the presence of the accessory proteins, rubredoxin (RubA) and rubredoxin reductase (RubB), produced in E. coli BL21(DE3)plysS cells, was determined. Recombinant AlkB2 is produced in an active form and rubredoxin is the intermediate electron donor to AlkB2 and can replace AlkG function, when NADH is the prime electron donor.
    PMID: 19953301 [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=3057251</comments>
            <pubDate>Wed, 02 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3057251</guid>        </item>
        <item>
            <title>Probiotic lactic acid bacterium from kanjika as a potential source of vitamin B(12): evidence from LC-MS, immunological and microbiological techniques.</title>
            <link>http://www.medworm.com/index.php?rid=3057250&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%3D19953302%26dopt%3DAbstract</link>
            <description>Authors: Madhu AN, Giribhattanavar P, Narayan MS, Prapulla SG
    Vitamin B(12) was produced by probiotic Lactobacillus plantarum in submerged fermentation (96 h) with successive anaerobic and aerobic phases of 48 h each to give 13 ng vitamin B(12)/g dry biomass. Sodium cyanide-mediated cell lysis, followed by benzyl alcohol/chloroform/water extraction, improved the release of intracellular vitamin B(12) for analysis. The presence of the K(+) adduct of cyanocobalamin (m/z of 1394) was established using electron spray ionization-mass spectra; growth of a mutant of Escherichia coli in the presence of cyanocobalamin ascertained its bioavailability.
    PMID: 19953302 [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=3057250</comments>
            <pubDate>Wed, 02 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3057250</guid>        </item>
        <item>
            <title>Biodegradation and biotransformation of organofluorine compounds.</title>
            <link>http://www.medworm.com/index.php?rid=3036445&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%3D19943179%26dopt%3DAbstract</link>
            <description>Authors: Murphy CD
    The carbon-fluorine bond is one of the strongest in nature, and the increasing use of organofluorine compounds in agriculture, human and veterinary medicine, and industry has raised concerns about their fate in the environment. Microorganisms can degrade organofluorine compounds, either via specific enzymatic hydrolysis of the C-F bond, or through transformation by catabolic enzymes with broad substrate specificities. Here our current understanding of organofluorine catabolism in microorganisms is summarised.
    PMID: 19943179 [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=3036445</comments>
            <pubDate>Fri, 27 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3036445</guid>        </item>
        <item>
            <title>Carrier-free immobilized enzymes for biocatalysis.</title>
            <link>http://www.medworm.com/index.php?rid=3036444&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%3D19943180%26dopt%3DAbstract</link>
            <description>Authors: Roessl U, Nah&amp;#xE1;lka J, Nidetzky B
    Methods for the preparation of carrier-free insoluble enzymes are reviewed. The technology of cross-linked enzyme aggregates has now been applied to a range of synthetically useful activities. Fusion proteins are also gaining momentum because they allow a relatively selective aggregation or even a specific self-assembly of the desired enzyme activity into insoluble particles in the absence of potentially denaturing chemicals required for precipitation and cross-linking. Recycling of insoluble protein particles for multiple rounds of batchwise reaction has been demonstrated in selected biotransformations. However, for application in a fully continuous biocatalytic process, low resistance to mechanical stress and high compressibility are issu...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3036444</comments>
            <pubDate>Fri, 27 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3036444</guid>        </item>
        <item>
            <title>Transesterification of oil mixtures catalyzed by microencapsulated cutinase in reversed micelles.</title>
            <link>http://www.medworm.com/index.php?rid=3036443&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%3D19943181%26dopt%3DAbstract</link>
            <description>Authors: Badenes SM, Lemos F, Cabral JM
    Recombinant cutinase from Fusarium solani pisi was used to catalyze the transesterification reaction between a mixture of triglycerides (oils) and methanol in reversed micelles of bis(2-ethylhexyl) sodium sulfosuccinate (AOT) in isooctane for the purposes of producing biodiesel. The use of a bi-phase lipase-catalyzed system brings advantages in terms of catalyst re-use and the control of water activity in the medium and around the enzyme micro-environment. Small-scale batch studies were performed to study the influence of the initial enzyme and alcohol concentrations, and the substrates molar ratio. Conversions in excess of 75 were obtained with reaction times under 24 h, which makes this enzymatic process highly competitive when compared to simi...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3036443</comments>
            <pubDate>Fri, 27 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3036443</guid>        </item>
        <item>
            <title>Susceptibility of bifidobacteria to lysozyme as a possible selection criterion for probiotic bifidobacterial strains.</title>
            <link>http://www.medworm.com/index.php?rid=3036442&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%3D19943182%26dopt%3DAbstract</link>
            <description>Authors: Rada V, Splichal I, Rockova S, Grmanova M, Vlkova E
    Resistance or susceptibility of bifidobacteria to lysozyme and growth of bifidobacteria in human milk were tested. Susceptible bifidobacterial strains stopped their growth almost immediately after the addition of lysozyme (400 mug/ml), moderately susceptible strains exhibited reduced growth rate, and growth curves of resistant strains were not affected. Strains of human origin were more resistant to lysozyme than animal strains. While strains of B. bifidum grew well in human milk samples, the growth B. animalis strains was inhibited after inoculation to human milk. The resistance to lysozyme seems to be a promising criterion for the selection of new probiotic bifidobacterial strains.
    PMID: 19943182 [PubMed - as supplied b...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3036442</comments>
            <pubDate>Fri, 27 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3036442</guid>        </item>
        <item>
            <title>Selection of RNA aptamers specific to active prostate-specific antigen.</title>
            <link>http://www.medworm.com/index.php?rid=3036441&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%3D19943183%26dopt%3DAbstract</link>
            <description>Authors: Jeong S, Han SR, Lee YJ, Lee SW
    A counter-SELEX procedure with recombinant purified active prostate specific antigen (PSA) was used to identify specific RNA aptamers against the active PSA. We developed two different kinds of counter-SELEX methods; one includes pre-clearance step with inactive proPSA protein, and the other with tagged GST protein. After 9 iterative selection cycles, several identical RNA aptamers can be identified from both counter-SELEX methods. Real-time PCR analysis and gel retardation experiment showed that the aptamers have a specific binding activity against the active PSA, but not for GST or proPSA. These aptamers could be of potential use as specific diagnostic, imaging and/or therapeutic agents against prostate cancer.
    PMID: 19943183 [PubMed - as ...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3036441</comments>
            <pubDate>Fri, 27 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3036441</guid>        </item>
        <item>
            <title>Microbial conversion of 5-sulfoisophthalic acid into 5-hydroxyisophthalic acid by Ochrobactrum anthropi S9.</title>
            <link>http://www.medworm.com/index.php?rid=3032297&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%3D19941033%26dopt%3DAbstract</link>
            <description>Authors: Yamada M, Yoshida T, Nagasawa T
    5-Hydroxyisophthalic acid-producing microorganisms were isolated from enrichment cultures using 5-sulfoisophthalic acid as a sulfur source. One bacterium, Ochrobactrum anthropi S9, had the highest 5-sulfoisophthalic acid-degrading activity, and stoichiometrically formed 5-hydroxyisophthalic acid, a raw material for polymer synthesis. Under optimum culture conditions, 1.3 mM 5-hydroxyisophthalic acid accumulated in the medium by 60 h. The addition of Na(2)SO(4), L: -methionine or L: -cysteine at 2 mM inhibited the conversion of 5-sulfoisophthalic acid. O. anthropi S9 cells converted 5-sulfoisophthalic acid, benzenesulfonic acid, 3-sulfobenzoic acid, 4-aminobenzenesulfonic acid, naphthalene-1-sulfonic acid and naphthalene-2-sulfonic acid into the ...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3032297</comments>
            <pubDate>Thu, 26 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3032297</guid>        </item>
        <item>
            <title>Enrichment separation of recombinant human CCR3 using detergent/polymer two-phase system.</title>
            <link>http://www.medworm.com/index.php?rid=3032296&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%3D19941034%26dopt%3DAbstract</link>
            <description>Authors: Ge B, Li W, Yin Y
    Studies on the structure and functions of membrane proteins are impeded by their lability, hydrophobicity, difficulty in purification and low yields. Human chemokine receptor 3 (CCR3) is a G protein-coupled receptor related to allergic diseases. A Triton X-100/PEG20000 two-phase system was employed for enrichment separation of CCR3 over-expressed in E. coli. Optimal CCR3 partitioning with partition coefficient around 8 was obtained at pH 7.0, ionic strength of 0.3 mol/kg and 3 h equilibration time. Total recovery of CCR3 reached 102 +/- 15%, which was much higher than 32 +/- 5% of the normally used ultracentrifugation method. The recovered CCR3 was finally purified by two chromatography steps giving a final protein of 87 kDa.
    PMID: 19941034 [PubMed - as s...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3032296</comments>
            <pubDate>Thu, 26 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3032296</guid>        </item>
        <item>
            <title>Retrocyclin 2: a new therapy against avian influenza H5N1 virus in vivo and vitro.</title>
            <link>http://www.medworm.com/index.php?rid=3032295&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%3D19941035%26dopt%3DAbstract</link>
            <description>Authors: Liang QL, Zhou K, He HX
    We tested the ability of retrocyclin 2, a type of theta defensin, to protect cells and chicken embryos from infection by H5N1 highly pathogenic avian influenza virus. A gene fragment of retrocyclin 2 was designed based on the protein sequence of retrocyclin 2 and cloned into the eukaryotic expression vector pcDNA4.01 (HismaxA), named pcDNA4-RC2. The expression vector pcDNA4-RC2 protected MDCK cells and chicken embryos from infection by the H5N1 virus through inhibition of virus replication and viral mRNA transcription. Retrocyclin 2 is therefore effective in preventing H5N1 virus infection in vivo and in vitro and could be considered as a new therapy for H5N1 influenza and other diseases.
    PMID: 19941035 [PubMed - as supplied by publisher] (Source: B...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3032295</comments>
            <pubDate>Thu, 26 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3032295</guid>        </item>
        <item>
            <title>Electrochemical selective detection of dopamine on microbial carbohydrate-doped multiwall carbon nanotube-modified electrodes.</title>
            <link>http://www.medworm.com/index.php?rid=3009055&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%3D19921114%26dopt%3DAbstract</link>
            <description>Authors: Jin JH, Cho E, Jung S
    Microbial carbohydrate-doped multiwall carbon nanotube (MWNT)-modified electrodes were prepared for the purpose of determining if 4-(2-aminoethyl)benzene-1,2-diol (3,4-dihydroxyphenylalanine; dopamine) exists in the presence of 0.5 mM ascorbic acid, a representative interfering agent in neurotransmitter detection. The microbial carbohydrate dopants were alpha-cyclosophorohexadecaose (alpha-C16) from Xanthomonas oryzae and cyclic-(1 --&amp;gt; 2)-beta-D: -glucan (Cys) from Rhizobium meliloti. The cyclic voltammetric responses showed that the highest sensitivity (5.8 x 10(-3) mA cm(-2) muM(-1)) is attained with the Cys-doped MWNT-modified ultra-trace carbon electrode, and that the alpha-C16-doped MWNT-modified glassy carbon electrode displays the best selectivi...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3009055</comments>
            <pubDate>Tue, 17 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3009055</guid>        </item>
        <item>
            <title>A series of novel directional cloning and expression vectors for blunt-end ligation of PCR products.</title>
            <link>http://www.medworm.com/index.php?rid=3009057&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%3D19915798%26dopt%3DAbstract</link>
            <description>Authors: Wu Q, Zhong X, Zhai C, Yang J, Chen X, Chen L, Wang W, Ma L
    Novel directional cloning and expression vectors were developed for blunt-end ligation of PCR products that are suitable for high-throughput cloning and simplifying the screening procedure. The PCR products, without further processing, are cloned into vectors digested with SchI and, following transformation, the desired recombinants give typical blue colonies on selectable plates. The principle of this selection strategy is that the construction also generates a full-length ideal lacO gene. To the best of our knowledge, this is the first time that this lacO reconstruction strategy has been applied in the selection of recombinants.
    PMID: 19915798 [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=3009057</comments>
            <pubDate>Sat, 14 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3009057</guid>        </item>
        <item>
            <title>Molecular activation of NF-kappaB, pro-inflammatory mediators, and signal pathways in gamma-irradiated mice.</title>
            <link>http://www.medworm.com/index.php?rid=3009056&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%3D19915799%26dopt%3DAbstract</link>
            <description>Authors: Ha YM, Chung SW, Kim JM, Kim DH, Kim JY, Lee EK, Lee J, Kim YJ, Yoo MA, Jeong KS, Chung HY
    The effects of gamma-irradiation on inflammatory gene expression, including NF-kappaB activation, in the kidney of C57/BL6 mice exposed to 1-9 Gy doses of (60)Co gamma-irradiation. Radiation enhanced the NF-kappaB activation and oxidative stress caused a dose-dependent disruption in the redox balance. The significance of this study is the new molecular information gained on gamma-irradiation effects through the activation of pro-inflammatory genes by NF-kappaB via the MAPK signaling pathway. Considering the exquisite sensitivity of NF-kappaB and other pro-inflammatory mediators to the redox status, we conclude that the activation of inflammatory processes by irradiation is likely initiat...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3009056</comments>
            <pubDate>Sat, 14 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3009056</guid>        </item>
        <item>
            <title>Mild hyperthermia prior to electroporation increases transfection efficiency in HCT 116, HeLa S3 and SGC 7901 cells.</title>
            <link>http://www.medworm.com/index.php?rid=2977950&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%3D19898781%26dopt%3DAbstract</link>
            <description>Authors: Wei ZL, Ogawa R, Takasaki I, Zhao QL, Zheng HC, Ahmed K, Hassan MA, Kondo T
    The change in transfection efficiency of electroporation by the combined treatment with mild preheating (40 degrees C for 30 min) was investigated. HCT 116, HeLa S3 and SGC 7901 cells were treated with electroporation in medium containing pBKCMV-Luc plasmid with or without preheating. After 24 h, luciferase activity was increased by 36, 28 and 77%; luciferase mRNA transcription was increased by 45, 50 and 68%; and fluorescein isothiocyanate-dextran accumulation was increased by 9, 35 and 15% in preheated groups, respectively. These results demonstrate that the transfection efficiency was enhanced by mild preheating. The mechanism partially involves increased macromolecular particle accumulation.
    PM...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2977950</comments>
            <pubDate>Sun, 08 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">2977950</guid>        </item>
        <item>
            <title>Recovery of succinic acid from fermentation broth.</title>
            <link>http://www.medworm.com/index.php?rid=2977949&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%3D19898782%26dopt%3DAbstract</link>
            <description>Authors: Kurzrock T, Weuster-Botz D
    Succinic acid is of high interest as bio-feedstock for the chemical industry. It is a precursor for a variety of many other chemicals, e.g. 1,4-butandiol, tetrahydrofuran, biodegradable polymers and fumaric acid. Besides optimized production strains and fermentation processes it is indispensable to develop cost-saving and energy-effective downstream processes to compete with the current petrochemical production process. Various methods such as precipitation, sorption and ion exchange, electrodialysis, and liquid-liquid extraction have been investigated for the recovery of succinic acid from fermentation broth and are reviewed critically here.
    PMID: 19898782 [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=2977949</comments>
            <pubDate>Sun, 08 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">2977949</guid>        </item>
        <item>
            <title>Growth kinetics and ginsenosides production in transformed hairy roots of American ginseng-Panax quinquefolium L.</title>
            <link>http://www.medworm.com/index.php?rid=2977948&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%3D19898783%26dopt%3DAbstract</link>
            <description>Authors: Mathur A, Gangwar A, Mathur AK, Verma P, Uniyal GC, Lal RK
    A thin, profusely branched, fast growing hairy root line of Panax quinquefolium (American ginseng) was established by co-culturing epicotyl explants with a wild type strain of Agrobacterium rhizogenes. The transformed roots grew by over 10-fold from the initial inoculum within 8 weeks. The crude ginsenosides content in the roots was about 0.2 g/g dry wt level up to the 10th week of culture. Ginsenosides Rb2, Rd, Re, Rf and Rg1 constituted 47-49% of the crude saponin fraction between 6 and 8 weeks of growth whereas, Rc ginsenoside was accumulated only after 9th weeks when the biomass started receding. PCR amplification analysis of the hairy roots confirmed their transgenic nature by showing the presence of Ri-TL DNA wit...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2977948</comments>
            <pubDate>Sun, 08 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">2977948</guid>        </item>
        <item>
            <title>An improved method for analysis of biomass sugars and galacturonic acid by anion exchange chromatography.</title>
            <link>http://www.medworm.com/index.php?rid=2977956&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%3D19898748%26dopt%3DAbstract</link>
            <description>Authors: Widmer W
    The most accurate analysis method for sugars in biomass, based on gas chromatography, requires a time consuming and laborious sample derivatation to trimethylsilanes or alditol acetates. In comparison, sample preparations for sugar analysis by liquid chromatography are simple water dilutions. However, HPLC methods either require long analysis times, use of expensive solvents, or do not give good resolution of sugars. A gradient method developed previously using a Dionex PA-1 column and pulsed-amperometric detection was modified to reduce analysis time from 75 to less than 40 min and provide good resolution of arabinose, rhamnose, galactose, xylose, glucose, fructose, sucrose, cellobiose, and galacturonic acid in both standards and hydrolyzed citrus waste biomass.
    ...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2977956</comments>
            <pubDate>Sat, 07 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">2977956</guid>        </item>
        <item>
            <title>Selective inhibitory potential of silver nanoparticles on the harmful cyanobacterium Microcystis aeruginosa.</title>
            <link>http://www.medworm.com/index.php?rid=2977955&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%3D19898749%26dopt%3DAbstract</link>
            <description>Authors: Park MH, Kim KH, Lee HH, Kim JS, Hwang SJ
    Silver nanoparticles (SNPs) at 1 mg/l inhibited the growth of the toxic cyanobacterium, Microcystis aeruginosa, by 87%. Similar results were obtained in field experiments. M. aeruginosa was more sensitive to SNPs than were green algae. SNPs may be a useful selective biocidal agent for the control of M. aeruginosa.
    PMID: 19898749 [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=2977955</comments>
            <pubDate>Sat, 07 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">2977955</guid>        </item>
        <item>
            <title>Production of biologically active IgG hinge-tag soluble epidermal growth factor receptors (ErbB).</title>
            <link>http://www.medworm.com/index.php?rid=2977954&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%3D19898750%26dopt%3DAbstract</link>
            <description>Authors: Otani T, Hashizume T, Nagaoka T, Fukuda T, Tang CK, Salomon DS, Seno M
    The extracellular domains (ECD) of epidermal growth factor receptors, ErbB1, 2, 3 and 4, were designed as soluble dimeric forms. Each ECD was fused to a short hinge region derived from IgG, such that the stable dimer could be formed with disulfide bridges. This hinge-tagged design minimized the molecular weight to approximately 50% of the conventional Fc-fusion design without an Fc domain of IgG. The refolded dimers could be easily analyzed and characterized by SDS-PAGE. Hinge-tagged soluble ErbBs demonstrated significant affinity for betacellulin and heregulin. The IgG hinge-tag should be a simple method to design soluble dimers that would be useful for high throughput screening of ligands, antagonists or ...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2977954</comments>
            <pubDate>Sat, 07 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">2977954</guid>        </item>
        <item>
            <title>Production of ethanol from thin stillage by metabolically engineered Escherichia coli.</title>
            <link>http://www.medworm.com/index.php?rid=2977953&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%3D19898751%26dopt%3DAbstract</link>
            <description>We report here the efficient production of ethanol from thin stillage by a metabolically engineered strain of Escherichia coli. Simultaneous utilization of glycerol and sugars was achieved by overexpressing either the fermentative or the respiratory glycerol-utilization pathway. However, amplification of the fermentative pathway (encoded by gldA and dhaKLM) led to more efficient consumption of glycerol and promoted the synthesis of reduced products, including ethanol. A previously constructed strain, EH05, containing mutations that prevented the accumulation of competing by-products (i.e. lactate, acetate, and succinate) and overexpressing the fermentative pathway for glycerol utilization [i.e. strain EH05 (pZSKLMgldA)], efficiently converted thin stillage supplemented with only mineral sa...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2977953</comments>
            <pubDate>Sat, 07 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">2977953</guid>        </item>
        <item>
            <title>Choice of plasmid preparation kit influences sequencing results.</title>
            <link>http://www.medworm.com/index.php?rid=2977952&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%3D19898752%26dopt%3DAbstract</link>
            <description>Authors: Hoffmann P, Hoffmann C, Weimann A
    Commercially available plasmid preparation kits are used in many laboratories to isolate plasmid DNA for subsequent dideoxy sequencing. We tested kits from seven different manufacturers for the purity of obtained plasmid preparations and compared the quality of sequencing results. The amount of RNA carry-over differed significantly (80-323 ng) and the usage of two kits led to protein remainders. Sequence read lengths (0-812 bases) and percentages of reading errors (1.6-100%) were also significantly different. We found the amount of protein contaminants to correlate with the percentage of reading errors (r = 0.63, P = 0.02).
    PMID: 19898752 [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=2977952</comments>
            <pubDate>Sat, 07 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">2977952</guid>        </item>
        <item>
            <title>Over-expression and characterization of recombinant prefoldin from hyperthermophilic archaeum Pyrococcus furiosus in E. coli.</title>
            <link>http://www.medworm.com/index.php?rid=2977951&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%3D19898753%26dopt%3DAbstract</link>
            <description>Authors: Chen H, Yang L, Zhang Y, Yang S
    Prefoldin is a hexameric chaperone that has been identified in eukaryotic cells and in Archaea. E. coli cells over-expressing the prefoldin gene from the hyperthermophilic, archaeum, Pyrococcus furiosus, grew well at 48 degrees C while control cells were unable to grow above 46 degrees C. The isolated and purified Pfu-prefoldin (specially the beta subunit and the prefoldin) thermally protected the activity of lysozyme.
    PMID: 19898753 [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=2977951</comments>
            <pubDate>Sat, 07 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">2977951</guid>        </item>
        <item>
            <title>Mutational analysis of the active site residues of a D: -psicose 3-epimerase from Agrobacterium tumefaciens.</title>
            <link>http://www.medworm.com/index.php?rid=2935407&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%3D19859667%26dopt%3DAbstract</link>
            <description>Authors: Kim HJ, Yeom SJ, Kim K, Rhee S, Kim D, Oh DK
    D: -Psicose 3-epimerase from Agrobacterium tumefacience catalyzes the conversion of D: -fructose to D: -psicose. According to mutational analysis, the ring at position 112, the negative charge at position 156, and the positive charge at position 215 were essential components for enzyme activity and for binding fructose and psicose. The surface contact area and distance to the bound substrate by molecular modeling suggest that the positive charge of Arg215 was involved in stabilization of cis-endiol intermediate. The distances between the catalytic residues (Glu150 and Glu244) and Mn(2+) are critical to the catalysis, and the negative charges of the metal-binding residues are important for interaction with metal ion. The kinetic para...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2935407</comments>
            <pubDate>Tue, 27 Oct 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">2935407</guid>        </item>
        <item>
            <title>Characterization of a recombinant L: -fucose isomerase from Caldicellulosiruptor saccharolyticus that isomerizes L: -fucose, D: -arabinose, D: -altrose, and L: -galactose.</title>
            <link>http://www.medworm.com/index.php?rid=2935409&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%3D19856146%26dopt%3DAbstract</link>
            <description>Authors: Ju YH, Oh DK
    A recombinant L: -fucose isomerase from Caldicellulosiruptor saccharolyticus was purified as a single 68 kDa band with an activity of 76 U mg(-1). The molecular mass of the native enzyme was 204 kDa as a trimer. The maximum activity for L: -fucose isomerization was at pH 7 and 75 degrees C in the presence of 1 mM Mn(2+). Its half-life at 70 degrees C was 6.1 h. For aldose substrates, the enzyme displayed activity in decreasing order for L: -fucose, with a k (cat) of 11,910 min(-1) and a K (m) of 140 mM, D: -arabinose, D: -altrose, and L: -galactose. These aldoses were converted to the ketoses L: -fuculose, D: -ribulose, D: -psicose, and L: -tagatose, respectively, with 24, 24, 85, 55% conversion yields after 3 h.
    PMID: 19856146 [PubMed - as supplied by publish...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2935409</comments>
            <pubDate>Sun, 25 Oct 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">2935409</guid>        </item>
        <item>
            <title>Inhibitory effect of curcumin on liver injury in a murine model of endotoxemic shock.</title>
            <link>http://www.medworm.com/index.php?rid=2935408&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%3D19856147%26dopt%3DAbstract</link>
            <description>Authors: Yun SS, Kim SP, Kang MY, Nam SH
    The effect of curcumin on lipopolysaccharide/D: -galactosamine (LPS/GalN)-induced acute shock model of liver injury was examined in mice. The simultaneous administration of LPS (5-20 mug kg(-1), i.p.) and GalN (700 mg kg(-1), i.p.) markedly increased the serum tumor necrosis factor-alpha (TNF-alpha), glutamic oxaloacetic transaminase/glutamic pyruvic transaminase (GOT/GPT), and massive hepatic necrosis and inflammation, leading to 100% lethality. Pre-administration of curcumin (100 mg kg(-1), i.p.) 3 h before induction with LPS/GalN imparted a large extent of protection against acute elevation in serum TNF-alpha and serum GOT/GPT. Hepatic necrosis and lethality caused by LPS/GalN was also greatly reduced by curcumin treatment. The results demons...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2935408</comments>
            <pubDate>Sun, 25 Oct 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">2935408</guid>        </item>
        <item>
            <title>Immobilization of Escherichia coli cells with cis-epoxysuccinate hydrolase activity for D: (-)-tartaric acid production.</title>
            <link>http://www.medworm.com/index.php?rid=2917088&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%3D19844664%26dopt%3DAbstract</link>
            <description>Authors: Pan H, Bao W, Xie Z, Zhang J, Li Y
    Immobilization of cis-epoxysuccinate hydrolase-containing E. coli for D: (-)-tartaric acid production was screened by various methods. The highest recovery of activity was obtained by entrapment in kappa-carrageenan gel. 23.6 g biomass/l and 43.4 g kappa-carrageenan/l were the best immobilization conditions optimized by response surface methodology with 83% yield (114 U/g). Cell autolysis was observed after immobilization. Immobilized cells showed high pH (5-10) stability, thermal (up to 65 degrees C) stability, conversion rate (&amp;gt;99.5%), enantioselectivity (ee &amp;gt; 99.6%), and were less affected by metal ions and surfactants compared with free cells. Conversion rate for immobilized cells preserved 93% after 10 repeated batches (5% for free...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2917088</comments>
            <pubDate>Tue, 20 Oct 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2917088</guid>        </item>
        <item>
            <title>Metabolic engineering of Streptomyces venezuelae for malonyl-CoA biosynthesis to enhance heterologous production of polyketides.</title>
            <link>http://www.medworm.com/index.php?rid=2910829&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%3D19838628%26dopt%3DAbstract</link>
            <description>Authors: Maharjan S, Park JW, Yoon YJ, Lee HC, Sohng JK
    Using metabolic engineering, we developed Streptomyces venezuelae YJ028 as an efficient heterologous host to increase the malonyl-CoA pool to be directed towards enhanced production of various polyketides. To probe the applicability of newly developed hosts in the heterologous production of polyketides, we expressed type III polyketide synthase, 1,3,6,8-tetrahydroxynaphthalene synthase, in these hosts. Flaviolin production was doubled by expression of acetyl-CoA carboxylase (ACCase) and 4-fold by combined expression of ACCase, metK1-sp and afsR-sp. Thus, the newly developed Streptomyces venezuelae YJ028 hosts produce heterologous polyketides more efficiently than the parent strain.
    PMID: 19838628 [PubMed - as supplied by publi...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2910829</comments>
            <pubDate>Fri, 16 Oct 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2910829</guid>        </item>
        <item>
            <title>A novel bioreactor for immobilized phototrophs.</title>
            <link>http://www.medworm.com/index.php?rid=2910828&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%3D19838629%26dopt%3DAbstract</link>
            <description>Authors: Fermont S, Shama G
    A novel configuration of photobioreactor is described in which filaments of alginate containing immobilized cells of a leaky mutant of Dunaliella parva are wound round a central light well which is located within a glass outer chamber so that a liquid medium is caused to flow in the annular space between the outside chamber and the alginate filaments. Glycerol production by D. parva was maintained for 700 h and the highest concentration of glycerol attained was approx. 12 mg l(-1).
    PMID: 19838629 [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=2910828</comments>
            <pubDate>Fri, 16 Oct 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2910828</guid>        </item>
        <item>
            <title>Ammonium and phosphate limitation in 1,3-propanediol production by Klebsiella pneumoniae.</title>
            <link>http://www.medworm.com/index.php?rid=2910827&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%3D19838630%26dopt%3DAbstract</link>
            <description>Authors: Zheng ZM, Xu YZ, Wang TP, Dong CQ, Yang YP, Liu DH
    Excretion of 1,3-propanediol (1,3-PD) by K. pneumoniae was compared in ammonium- and phosphate-limited chemostat cultures running with an excess of glycerol. 59 and 43% catabolic flux were directed to 1,3-PD in ammonia-limited cultures and phosphate-limited cultures at dilution rate of 0.1 h(-1), respectively. Ammonia-limited fed-batch cultures produced 61 g 1,3-PD l(-1) and a total of 15 g l(-1) organic acid in 36 h. However, phosphate-limited fed-batch cultures excreted 61 g lactate l(-1) and 44 g 1,3-PD l(-1).
    PMID: 19838630 [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=2910827</comments>
            <pubDate>Fri, 16 Oct 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2910827</guid>        </item>
        <item>
            <title>Quantitation of non-amplified genomic DNA by bead-based hybridization and template mediated extension coupled to alkaline phosphatase signal amplification.</title>
            <link>http://www.medworm.com/index.php?rid=2910825&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%3D19838631%26dopt%3DAbstract</link>
            <description>Authors: Martins SA, Prazeres DM, Fonseca LP, Monteiro GA
    Klenow I polymerase activity was combined with solid phase DNA hybridization to detect non-amplified genomic DNA (gDNA) sequences from Escherichia coli. Aminopropyl-controlled pore glass surface-bound oligonucleotides were hybridized to fragmented gDNA. The template-mediated extension at the 3'-terminus of the immobilized probe was then promoted in the presence of Klenow I polymerase and digoxigenin-labeled nucleotides. Detection of the extended probes was accomplished with an anti-digoxigenin alkaline phosphatase conjugate protocol coupled to colorimetric or fluorescent detection. Using the colorimetric protocol, the proof-of-concept was established. The fluorescence-based methodology, on the other hand, provided the basis for ...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2910825</comments>
            <pubDate>Fri, 16 Oct 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2910825</guid>        </item>
        <item>
            <title>Characterisation and expression of a novel holotype crystal protein gene, cry56Aa1, from Bacillus thuringiensis strain Ywc2-8.</title>
            <link>http://www.medworm.com/index.php?rid=2910824&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%3D19838632%26dopt%3DAbstract</link>
            <description>Authors: Zhu J, Zheng AP, Tan FR, Wang SQ, Deng QM, Li SC, Wang LX, Li P
    Bacillus thuringiensis isolate Ywc2-8, from soil in Sichuan Basin in western China, contains a spherical crystal harbouring two insecticidal crystal proteins with masses of 70 kDa and 130 kDa. A novel cry-type gene, encoding a 664 amino acid protein with 34% homology to cry29Aa1, was found and cloned from this strain. This gene belongs to a novel holotype cry and is designated as cry56Aa1. It was expressed in E. coli. Insecticidal activity assays showed that recombinant Cry56Aa1 was toxic to both Dipteran (Aedes aegypti) and Lepidopteran (Plutella xylostella and Helicoverpa armigera) pests. Cloning of this gene may help to overcome the increasing resistance of pests to currently used insecticides.
    PMID: 198386...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2910824</comments>
            <pubDate>Fri, 16 Oct 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2910824</guid>        </item>
        <item>
            <title>New insights on O(2) uptake mechanisms in two-phase partitioning bioreactors.</title>
            <link>http://www.medworm.com/index.php?rid=2910822&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%3D19838633%26dopt%3DAbstract</link>
            <description>The objective of this paper was to quantify the direct oxygen uptake from the vector/water interface in a culture of Pseudomonas putida, performed in a stirred tank reactor, using glucose as substrate and silicone oil as vector. Despite of a sufficient dissolved O(2) concentration in the vector phase (17 mg l(-1)) and a significant vector surface area (4,000 m(-1)) no significant direct O(2) uptake from the vector/water interface was observed, compared to O(2) uptake from the aqueous phase. From these results it was concluded that, direct O(2) or substrate uptake from the vector/water interface might not be significant in TPPBs.
    PMID: 19838633 [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=2910822</comments>
            <pubDate>Fri, 16 Oct 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2910822</guid>        </item>
        <item>
            <title>Recombinant canstatin inhibits tumor growth in an orthotopic AT-84 oral squamous cell carcinoma model.</title>
            <link>http://www.medworm.com/index.php?rid=2910821&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%3D19838634%26dopt%3DAbstract</link>
            <description>Authors: Hwang-Bo J, Yoo KH, Jeong HS, Chung IS
    The inhibitory effect of recombinant canstatin on tumor growth was investigated using an orthotopic oral squamous cell carcinoma (AT-84 cells) animal (C3H/HeN) model. Recombinant canstatin from stably transfected Drosophila S2 cells was purified to homogeneity using a simple one-step Ni NTA affinity fractionation. In our oral cancer model, the final volume and weight of tumors in groups treated with purified canstatin were both reduced to 44% of values for a control group treated with PBS. Blood or lymphatic vessel densities of tumors in the canstatin-treated group were reduced to 72% and 44% of control group values, respectively. Recombinant canstatin at 20 mug/ml effectively inhibited tube formation in HUVEC and lymphatic endothelial ce...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2910821</comments>
            <pubDate>Fri, 16 Oct 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2910821</guid>        </item>
        <item>
            <title>Conversion of alpha-amyrin into centellosides by plant cell cultures of Centella asiatica.</title>
            <link>http://www.medworm.com/index.php?rid=2910820&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%3D19838635%26dopt%3DAbstract</link>
            <description>Authors: Hernandez-Vazquez L, Bonfill M, Moyano E, Cusido RM, Navarro-Oca&amp;#xF1;a A, Palazon J
    Plant cell cultures of Centella asiatica produce small quantities of centellosides: madecassosid &amp;gt; asiaticosid &amp;gt; madecassic acid &amp;gt; asiatic acid. To obtain a more efficient production system of these bioactive triterpenoid compounds, we developed a process where the substrate, alpha-amyrin, was converted into centellosides by cell suspensions of C. asiatica. When alpha-amyrin in acetone was added at 0.01 mg/ml(-1) to the culture medium, together with the permeabilizing agent DMSO, after 7 days nearly 50% had penetrated the plant cells, of which almost 84% was transformed into centellosides. The system therefore efficiently converts alpha-amyrin into centellosides, thus opening a new po...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2910820</comments>
            <pubDate>Fri, 16 Oct 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2910820</guid>        </item>
        <item>
            <title>Molecular characterization of OsPAP2: transgenic expression of a purple acid phosphatase up-regulated in phosphate-deprived rice suspension cells.</title>
            <link>http://www.medworm.com/index.php?rid=2910819&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%3D19838636%26dopt%3DAbstract</link>
            <description>Authors: Hur YJ, Jin BR, Nam J, Chung YS, Lee JH, Choi HK, Yun DJ, Yi G, Kim YH, Kim DH
    A phosphate starvation-induced, purple, acid phosphatase cDNA was cloned from rice, Oryza sativa. The cDNA encoding the phosphatase (OsPAP2) has 1,893 bp with an open reading frame of 630 amino acid residues. The deduced amino acid sequence of OsPAP2 shows identities of 60-63% with other plant purple acid phosphatases and appears to have five conserved motifs containing the residues involved in metal binding. OsPAP2 expression is up-regulated in the rice plant and in cell cultures in the absence of phosphate (P( i )). The induced expression of OsPAP2 is a specific response to P( i ) starvation, and is not affected by the deprivation of other nutrients. OsPAP2 expression was responsive to the level o...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2910819</comments>
            <pubDate>Fri, 16 Oct 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2910819</guid>        </item>
        <item>
            <title>Expression of Trichoderma reesei endo-beta-glucanase II in silkworm, Bombyx mori L. by using BmNPV/Bac-to-Bac expression system and its bioactivity assay.</title>
            <link>http://www.medworm.com/index.php?rid=2910818&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%3D19838637%26dopt%3DAbstract</link>
            <description>Authors: Zhou L, Wu X, Lan L, Liu J
    The silkworm, Bombyx mori, was used to produce recombinant endo-beta-glucanase II (rEGII). The EGII gene (egl2) was cloned from the cellulolytic fungus Trichoderma reesei and inserted into B. mori nucleopolyhedrovirus (BmNPV) genome using BmNPV/Bac-to-Bac expression vector. For expression of rEGII, both the BmN cells and B. mori larvae were infected with the recombinant virus. The putative rEGII yield was about 386 mug per larva and the enzyme activity of the purified rEGII was approx 352 U/mg of rEGII. The optimal activity of this purified protein was observed at 55 degrees C and pH 4, respectively.
    PMID: 19838637 [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=2910818</comments>
            <pubDate>Fri, 16 Oct 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2910818</guid>        </item>
        <item>
            <title>Cloning of a novel lipase gene, lipJ08, from Candida rugosa and expression in Pichia pastoris by codon optimization.</title>
            <link>http://www.medworm.com/index.php?rid=2910817&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%3D19841868%26dopt%3DAbstract</link>
            <description>Authors: Xu L, Jiang X, Yang J, Liu Y, Yan Y
    A novel lipase gene, lipJ08, was cloned from Candida rugosa ATCC14830, along with the already reported five lipase genes (lip1-lip5). Nucleotide sequencing indicated that the lipJ08 gene contains a 1650 bp open reading frame (ORF) without introns. The deduced amino acid sequence corresponds to 534 amino acid residues, including a putative signal sequence of 15 amino acid residues. Seventeen of the non-universal serine codons (CTG) of lipJ08 were converted into universal serine codons (TCT) by PCR-based mutagenesis. The native and codon-optimized lipJ08 genes were expressed in Pichia pastoris. The hydrolytic activity of the recombinant LIPJ08 was 4.7 U/ml, whereas the activity of the recombinant wild-type lipase could not be detected.
    PMI...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2910817</comments>
            <pubDate>Fri, 16 Oct 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2910817</guid>        </item>
        <item>
            <title>Soluble pig lymphocyte activation gene-3 (LAG-3; CD223) inhibits human-to-pig xenogeneic mixed lymphocyte reaction.</title>
            <link>http://www.medworm.com/index.php?rid=2902061&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%3D19834647%26dopt%3DAbstract</link>
            <description>In this study, we constructed soluble pig LAG-3 containing a critical binding site (D1 and D2 region) to MHC class II molecules, combined with a constant region of an immunoglobulin (Ig) heavy chain. Flow cytometry analyses indicated that soluble pig LAG-3 binds to both pig and human MHC class II molecules. Moreover, soluble pig LAG-3 can inhibit human lymphocyte proliferation in the human-pig xenogeneic mixed lymphocyte reaction in a dose-dependent manner. These results indicate that soluble pig LAG-3 may be useful for controlling the xenogeneic T cell immune responses between the human and pig.
    PMID: 19834647 [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=2902061</comments>
            <pubDate>Thu, 15 Oct 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2902061</guid>        </item>
        <item>
            <title>In vitro myogenic and adipogenic differentiation model of genetically engineered bovine embryonic fibroblast cell lines.</title>
            <link>http://www.medworm.com/index.php?rid=2902060&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%3D19834648%26dopt%3DAbstract</link>
            <description>Authors: Yin J, Jin X, Beck S, Kang DH, Hong Z, Li Z, Jin Y, Zhang Q, Choi YJ, Kim SC, Kim H
    Our current understanding of muscle and adipose tissue development has been largely restricted to the study of murine myogenic and adipogenic cell lines, since attempts to establish these cell lines from other species have met with only limited success. Here we report that a spontaneously immortalized bovine embryonic fibroblast cell line (BEFS) undergoes differentiation into adipogenic or myogenic lineages when ectopically transduced with PPARgamma2 (an adipogenic lineage determinant) or MyoD (a myogenic lineage determinant) and grown in adipogenic and myogenic differentiation culture media (ADCM and MDCM, respectively). We also found that PPARgamma2-overexpressing BEFS cells (BEFS-PPARgamma2)...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2902060</comments>
            <pubDate>Thu, 15 Oct 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2902060</guid>        </item>
        <item>
            <title>Enhanced ascorbic acid accumulation in transgenic potato confers tolerance to various abiotic stresses.</title>
            <link>http://www.medworm.com/index.php?rid=2887354&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%3D19821071%26dopt%3DAbstract</link>
            <description>Authors: Hemavathi , Upadhyaya CP, Akula N, Young KE, Chun SC, Kim DH, Park SW
    L: -Ascorbic acid (Vitamin C, AsA) is an important component of human nutrition. Plants and several animals can synthesize their own ascorbic acid, whereas humans lack the gene essential for ascorbic acid biosynthesis and must acquire from their diet. In the present study, we developed transgenic potato (Solanum tuberosum L. cv. Taedong Valley) over-expressing L: -gulono-gamma-lactone oxidase (GLOase gene; NCBI Acc. No. NM022220), isolated from rat cells driven by CaMV35S constitutive promoter that showed enhanced AsA accumulation. Molecular analyses of four independent transgenic lines performed by PCR, Southern and RT-PCR revealed the stable integration of the transgene in the progeny. The transformation f...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2887354</comments>
            <pubDate>Sat, 10 Oct 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2887354</guid>        </item>
        <item>
            <title>Fungal endophytes-induced abscisic acid is required for flavonoid accumulation in suspension cells of Ginkgo biloba.</title>
            <link>http://www.medworm.com/index.php?rid=2887353&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%3D19821072%26dopt%3DAbstract</link>
            <description>Authors: Hao G, Du X, Zhao F, Ji H
    Treatment of suspension cells of Ginkgo biloba with fungal endophytes resulted in accumulation of flavonoids, increased abscisic acid (ABA) production and activation of phenylalanine ammonia-lyase (PAL). Fluridone, an inhibitor of ABA biosynthesis, was effective in inhibiting fungal endophytes-induced ABA biosynthesis, increase of PAL activity and flavonoids accumulation. Moreover, exogenous application of ABA enhanced PAL activity and increased accumulation of flavonoids in G. biloba cells with or without fungal endophytes elicitor. These finding suggest a causal relationship between ABA release and both PAL activity and flavonoid accumulation under fungal endophytes treatment and that ABA is involved in fungal endophytes-induced flavonoids accumulat...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2887353</comments>
            <pubDate>Sat, 10 Oct 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2887353</guid>        </item>
        <item>
            <title>Surface display of active lipase in Saccharomyces cerevisiae using Cwp2 as an anchor protein.</title>
            <link>http://www.medworm.com/index.php?rid=2887352&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%3D19821073%26dopt%3DAbstract</link>
            <description>Authors: Liu W, Zhao H, Jia B, Xu L, Yan Y
    Lipase Lip2 from Yarrowia lipolytica was displayed on the cell surface of Saccharomyces cerevisiae using Cwp2 as an anchor protein. Successful display of the lipase on the cell surface was confirmed by immunofluorescence microscopy and halo assay. The length of linker sequences was further examined to confirm that the correct conformation of Lip2 was maintained. The results showed that the displayed Lip2 exhibited the highest activity at 7.6 +/- 0.4 U/g (dry cell) when using (G(4)S)(3) sequence as the linker, with an optimal temperature and pH at 40 degrees C and pH 8.0. The displayed lipase did not lose any activity after being treated with 0.1% Triton X-100 and 0.1% Tween 80 for 30 min, and it retained 92% of its original activity after incu...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2887352</comments>
            <pubDate>Sat, 10 Oct 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2887352</guid>        </item>
        <item>
            <title>Enhanced proliferation capacity of porcine tenocytes in low O(2) tension culture.</title>
            <link>http://www.medworm.com/index.php?rid=2887351&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%3D19821074%26dopt%3DAbstract</link>
            <description>In conclusion, low O(2) tension culture can significantly enhance the expansion capacity of tenocytes without affecting their phenotype and functions.
    PMID: 19821074 [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=2887351</comments>
            <pubDate>Sat, 10 Oct 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2887351</guid>        </item>
        <item>
            <title>Post-culture treatment protocols for PLGA membrane scaffolds.</title>
            <link>http://www.medworm.com/index.php?rid=2887350&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%3D19821075%26dopt%3DAbstract</link>
            <description>Authors: Ellis MJ, Forsey R, Chaudhuri JB
    The interactions of post-culture treatments reagents used for fixing, lysing and cell quantification on poly(lactide-co-glycolide) (PLGA) flat sheet membrane scaffolds are presented. Lysing with Alkaline buffer solution/Triton X-100/MilliQ water (ATM) and fixing with 10% Neutral Buffered Formalin (10% NBF) had no affect on membrane structure while fixing with 95% ethanol caused smoothing of the surface, shrinkage and a reduction in surface area of 55, 48 and 33, for 100:0, 75:25 and 50:50 (PLA:PGA), respectively. PicoGreen assay was selected for cell (560pZIPv.neo) quantification since the background noise would not affect readings for cell numbers over 3,000 cells/cm(2), while the background reading was too high for MTT and Methylene Blue (MB)...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2887350</comments>
            <pubDate>Sat, 10 Oct 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2887350</guid>        </item>
        <item>
            <title>Evaluation of ultrasound velocity measurements for estimating protease activities using casein as substrate.</title>
            <link>http://www.medworm.com/index.php?rid=2887349&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%3D19821076%26dopt%3DAbstract</link>
            <description>Authors: Born K, Manns A, Dzeyk K, Lutz-Wahl S, Gau D, Fischer L
    Ultrasonic resonator technology (URT) was compared with the well established UV-Vis/ninhydrin assay to estimate protease activities in defined buffer systems. Hydrolysis of casein was measured using subtilisin, trypsin, halophilic protease from Haloferax mediterranei and Bacillus lentus alkaline protease. Sensitivity, reproducibility, working range as well as the limit of detection and the limit of quantification were comparable for both methods. Salt concentrations (0.5 M NaCl) interfered with the URT method. The quantification of protease activity by URT was possible when the product concentration measured by the UV-Vis/ninhydrin assay was correlated to the corresponding ultrasonic velocity signals.
    PMID: 19821076 [...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2887349</comments>
            <pubDate>Sat, 10 Oct 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2887349</guid>        </item>
        <item>
            <title>Screening for conditions of enhanced production of a recombinant beta-glucanase secreted into the medium by Escherichia coli.</title>
            <link>http://www.medworm.com/index.php?rid=2877261&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%3D19816658%26dopt%3DAbstract</link>
            <description>Authors: Spexard M, Beshay U, Risse JM, Miksch G, Flaschel E
    The extracellular production of a hybrid bacterial beta-glucanase using Escherichia coli was studied by using combinations of promoters of varying strength for both a beta-glucanase as the target protein and the Kil protein as the releasing factor. Four strains with different combinations of promoter strengths were cultivated in shake-flasks on four different media to assess the cross-influence of promoter and medium in a general manner. Promoters were taken from natural as well as synthetic sequences known to exhibit either weak or strong promoter strength. By far the highest extracellular glucanase activity (&amp;gt;200 U ml(-1)) was achieved when a strain harbouring the kil gene under control of a strong synthetic stationary-p...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2877261</comments>
            <pubDate>Thu, 08 Oct 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2877261</guid>        </item>
        <item>
            <title>Validation of extraction methods for total RNA and miRNA from bovine blood prior to quantitative gene expression analyses.</title>
            <link>http://www.medworm.com/index.php?rid=2856023&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%3D19789844%26dopt%3DAbstract</link>
            <description>Authors: Hammerle-Fickinger A, Riedmaier I, Becker C, Meyer HH, Pfaffl MW, Ulbrich SE
    The benefit and precision of blood diagnosis by quantitative real-time PCR (qPCR) is limited by sampling procedures and RNA extraction methods. We have compared five different RNA extraction protocols from bovine blood regarding RNA and miRNA yield, quality, and most reproducible data in the qRT-PCR with the lowest point of quantification. Convincing results in terms of highest quantity, quality, and best performance for mRNA qPCR were obtained by leukocyte extraction following blood lysis as well as extraction of PAXgene stabilized blood. The best microRNA qPCR results were obtained for samples extracted by the leukocyte extraction method.
    PMID: 19789844 [PubMed - as supplied by publisher] (Sourc...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2856023</comments>
            <pubDate>Tue, 29 Sep 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2856023</guid>        </item>
        <item>
            <title>Potential adenovirus-mediated gene therapy of glioma cancer.</title>
            <link>http://www.medworm.com/index.php?rid=2847242&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%3D19784809%26dopt%3DAbstract</link>
            <description>Authors: Fu YJ, Du J, Yang RJ, Yin LT, Liang AH
    Malignant gliomas are typically characterized by rapid cell proliferation and a marked propensity to invade and damage surrounding tissues. They are the main brain tumors notoriously resistant to currently available therapies, since they fail to undergo apoptosis upon anticancer treatments. With recent advances in neuroscience and improved understanding of the molecular mechanisms of invasive migration, gene therapy provides a new strategy for treating glioma cancer. Brain tumor gene therapy using viral vectors and stem cells has shown promise in animal model and human patient studies. Here, we review recent studies on engineering adenoviral vectors that can be used as therapy for brain tumors. The new findings presented in this study are...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2847242</comments>
            <pubDate>Sat, 26 Sep 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2847242</guid>        </item>
        <item>
            <title>Thymidine production by overexpressing NAD(+) kinase in an Escherichia coli recombinant strain.</title>
            <link>http://www.medworm.com/index.php?rid=2829199&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%3D19774345%26dopt%3DAbstract</link>
            <description>Authors: Lee HC, Kim JS, Jang W, Kim SY
    Intracellular NADPH/NADP(+) ratio in cells grown on various production media with different carbon and nitrogen sources had a positive correlation with the thymidine production. To improve thymidine production in a previously engineered E. coli strain, NAD(+) kinase was overexpressed in it resulting in the NADPH/NADP(+) ratio shifting from 0.184 to 0.267. The [NADH + NADP(+)]/[NAD(+) + NADPH] ratio was, however, not significantly altered. In jar fermentation, 740 mg thymidine l(-1) was produced in parental strain, while 940 mg l(-1) of thymidine was produced in NAD(+) kinase-expressing strain.
    PMID: 19774345 [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=2829199</comments>
            <pubDate>Tue, 22 Sep 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2829199</guid>        </item>
        <item>
            <title>Rolling circle amplification of genomic templates for inverse PCR (RCA-GIP): a method for 5'- and 3'-genome walking without anchoring.</title>
            <link>http://www.medworm.com/index.php?rid=2810197&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%3D19760115%26dopt%3DAbstract</link>
            <description>Authors: Tsaftaris A, Pasentzis K, Argiriou A
    We have devised an improved method of genome walking, named rolling circle amplification of genomic templates for Inverse PCR (RCA-GIP). The method is based on the generation of circular genomic DNA fragments, followed by rolling circle amplification of the circular genomic DNA using varphi29 DNA polymerase without need for attachment of anchor sequences. In this way from the circular genomic DNA fragments, after RCA amplification, a large amount of linear concatemers is generated suitable for Inverse PCR template that can be amplified, sequenced or cloned allowing the isolation of the 3'- and 5'- of unknown ends of genomic sequences. To prove the concept of the proposed methodology, we used this procedure to isolate the promoter regions fr...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2810197</comments>
            <pubDate>Wed, 16 Sep 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2810197</guid>        </item>
        <item>
            <title>Production of pure beta-glucan by Aureobasidium pullulans after pullulan synthetase gene disruption.</title>
            <link>http://www.medworm.com/index.php?rid=2810196&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%3D19760116%26dopt%3DAbstract</link>
            <description>Authors: Kang BK, Yang HJ, Choi NS, Ahn KH, Park CS, Yoon BD, Kim MS
    By disruption of the pullulan synthetase gene (pul) of Aureobasidium pullulans IMS822 KCTC11179BP, we constructed a mutant strain, A. pullulans NP1221, which produced a pure beta-glucan exopolysaccharide. The mutant NP1221 was white, whereas the wild-type strain produced a black dye. When we compared fermentation kinetics between wide-type and mutant strains, the mutant NP1221 did not produce pullulan. Substrate uptake rate and beta-glucan production were similar in both strains. However, the biomass yield of mutant NP1221 was 2.3-fold (9.2 g l(-1)) greater than that of wild-type.
    PMID: 19760116 [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=2810196</comments>
            <pubDate>Wed, 16 Sep 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2810196</guid>        </item>
        <item>
            <title>Pr-1, a novel antifungal protein from pumpkin rinds.</title>
            <link>http://www.medworm.com/index.php?rid=2810195&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%3D19760117%26dopt%3DAbstract</link>
            <description>Authors: Park SC, Lee JR, Kim JY, Hwang I, Nah JW, Cheong H, Park Y, Hahm KS
    A novel antifungal protein, M(r) = ca. 40 kDa, was isolated from pumpkin rind and designated Pr-1. When purified by anion exchange chromatography and HPLC, it inhibited growth of several fungi including Botrytis cinerea, Fusarium oxysporum, Fusarium solani and Rhizoctonia solani, as well as the yeast, Candida albicans, at 10-20 muM. It did not inhibit growth of Escherichia coli or Staphylococcus aureus even at 200 muM. Laser scanning microscopy of fungal cells exposed to rhodamine-labeled Pr-1 revealed that the protein accumulated and was localized on the cell surface. Uptake of the vital stain, SYTOX Green, was enhanced when fungal conidia were treated with Pr-1 suggesting that the protein has membrane permea...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2810195</comments>
            <pubDate>Wed, 16 Sep 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2810195</guid>        </item>
        <item>
            <title>Diastereoselective synthesis of L: -threo-3,4-dihydroxyphenylserine by low-specific L: -threonine aldolase mutants.</title>
            <link>http://www.medworm.com/index.php?rid=2810194&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%3D19760118%26dopt%3DAbstract</link>
            <description>Authors: Gwon HJ, Baik SH
    Diastereoselectivity-enhanced mutants of L: -threonine aldolase (L: -TA) for L: -threo-3,4-dihydroxyphenylserine (L: -threo-DOPS) synthesis were isolated by error-prone PCR followed by a high-throughput screening. The most improved mutant was achieved from the mutant T3-3mm2, showing a 4-fold increase over the wild-type L: -TA. When aldol condensation activity was examined using whole cells of T3-3mm2, its de was constantly maintained at 55% during the batch reactions for 80 h, yielding 3.8 mg L: -threo-DOPS/ml.
    PMID: 19760118 [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=2810194</comments>
            <pubDate>Wed, 16 Sep 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2810194</guid>        </item>
        <item>
            <title>Fed-batch operation of an industrial cell culture process in shaken microwells.</title>
            <link>http://www.medworm.com/index.php?rid=2810193&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%3D19760119%26dopt%3DAbstract</link>
            <description>Authors: Silk NJ, Denby S, Lewis G, Kuiper M, Hatton D, Field R, Baganz F, Lye GJ
    Recently we have demonstrated batch suspension culture of mammalian cells in microwell plates. Here we describe a method for fed-batch culture of an industrially relevant GS-CHO (Glutamine Synthetase-Chinese Hamster Ovary) cell line in shaken 24-standard round well (24-SRW) plates. Use of a commercially available 'sandwich lid' and appropriate dilution of the bolus feeds counteracted liquid evaporation from the wells resulting in similar cell growth and antibody formation kinetics in both 24-SRW plates (800 mul) and shaken flasks (50 ml). Peak viable cell densities obtained were 8 +/- 0.5 x 10(6) and 9 +/- 1.3 x 10(6) ml(-1), respectively, while comparable final titres of a whole IgG of approximately 1.5 ...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2810193</comments>
            <pubDate>Wed, 16 Sep 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2810193</guid>        </item>
        <item>
            <title>Preparation of cross-linked carboxymethyl chitosan for repairing sciatic nerve injury in rats.</title>
            <link>http://www.medworm.com/index.php?rid=2810192&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%3D19760120%26dopt%3DAbstract</link>
            <description>Authors: Wang G, Lu G, Ao Q, Gong Y, Zhang X
    A successful nerve regeneration process was achieved with nerve repair tubes made up of 1-ethyl-3(3-dimethylaminopropyl) carbodiimide hydrochloride (EDC) cross-linked carboxymethyl chitosan (CM-chitosan) with improved biodegradability. Chitosan has a very slow degradation rate, while the EDC cross-linked CM-chitosan tubes degraded to 30% of original weight during 8 weeks of incubation in lysozyme solution. In vitro cell culture indicated that the CM-chitosan films presented no cytotoxicity to Schwann cells. From in vivo studies using a 10 mm rat sciatic nerve defect model investigated by histomorphometry analysis, the average diameter of the fibers and the average thickness of myelin sheath in the CM-chitosan tubes were 3.7 +/- 0.33 and 0.33...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2810192</comments>
            <pubDate>Wed, 16 Sep 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2810192</guid>        </item>
        <item>
            <title>Constitutive production of the receptor-binding domain of the F18 fimbriae on the surface of Lactococcus lactis using synthetic promoters.</title>
            <link>http://www.medworm.com/index.php?rid=2810191&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%3D19760121%26dopt%3DAbstract</link>
            <description>Authors: Lindholm A, Palva A
    Nine synthetic constitutive promoters with different activities were produced for the surface display of the receptor-binding domain of the F18 fimbrial adhesin FedF in Lactococcus lactis. The promoters were synthesized from an oligonucleotide, designed to allow for randomization of bases between defined lactococcal promoter consensus regions. However, promoters with spontaneous modifications were selected for fedF expression, indicating that the consensus promoter was too strong. The amount of FedF on the surface of the best performing promoter clone was comparable to the amount of FedF produced by a L. lactis strain with an optimized NICE expression system. Stability of FedF production further suggested that an optimal constitutive expression level was at...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2810191</comments>
            <pubDate>Wed, 16 Sep 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2810191</guid>        </item>
        <item>
            <title>Residue Tyr224 is critical for the thermostability of Geobacillus sp. RD-2 lipase.</title>
            <link>http://www.medworm.com/index.php?rid=2810190&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%3D19763406%26dopt%3DAbstract</link>
            <description>Authors: Wu L, Liu B, Hong Y, Sheng D, Shen Y, Ni J
    A thermophilic lipase (lipGRD) from Geobacillus sp. RD-2, isolated from a hot spring in Yunnan, China, was cloned and over-expressed in Escherichia coli. The function of the conserved residue, Tyr224, near the presumed temperature switch site was analyzed by site-directed saturation mutagenesis. The activity of the wild type lipGRD was optimal at 55 degrees C and pH 7.5, but that from mutant Y224C was optimally active at 35 degrees C, whereas Y224P lipase was optimally active at 65 degrees C. Furthermore, the latter lipase retained 60% of its activity after incubation at 65 degrees C for 5 h. The conserved residue Tyr224, which is close to the lid helix, is the key amino acid residue determining the thermostability of the thermostable...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2810190</comments>
            <pubDate>Tue, 08 Sep 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2810190</guid>        </item>
        <item>
            <title>Stability of transgenes in long-term micropropagation of plants of transgenic birch (Betula platyphylla).</title>
            <link>http://www.medworm.com/index.php?rid=2770515&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%3D19731043%26dopt%3DAbstract</link>
            <description>Authors: Zeng F, Qian J, Luo W, Zhan Y, Xin Y, Yang C
    The stability of integration and expression level of transgenes in long-term micropropagation clones of transgenic birch (Betula platyphylla Suk.) was examined. Multiplexed PCR and reverse primer PCR demonstrated stable integration of transgenes into regenerated plants. Expression levels of the bgt and gus genes among shoot plantlets, subcultured 4, 7, 9 and 15 times, were significantly different. The transcriptional expression level of extraneous genes in regenerated plants decreased with increasing subculture number. Transcriptional gene silencing (TGS) occured in regenerated transgenic lines. The silencing rate of GUS in the 5th subculture plants was 22-65%. TGS in regenerated plants could be reactivated with 5-azacytidine (Azac)...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2770515</comments>
            <pubDate>Wed, 02 Sep 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2770515</guid>        </item>
        <item>
            <title>Cellulose hydrolysis by immobilized Trichoderma reesei cellulase.</title>
            <link>http://www.medworm.com/index.php?rid=2770514&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%3D19731044%26dopt%3DAbstract</link>
            <description>Authors: Jones PO, Vasudevan PT
    Cellulose hydrolysis by immobilized Trichoderma reesei cellulase in the presence of a low viscosity ionic liquid, 1-ethyl-3-methylimidazolium diethyl phosphate (EMIM-DEP), was investigated. Preparation of the carrier-free immobilized cellulase was optimized with respect to concentration of the cross-linker and the type of precipitant. The addition of 2% (v/v) EMIM-DEP during hydrolysis gave an initial reaction rate 2.7 times higher than the hydrolysis rate with no ionic liquid. The initial yield after 2 h was 0.7 g glucose/g cellulose, and the carrier-free immobilized cellulase (CFIC) was effectively re-used five times.
    PMID: 19731044 [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=2770514</comments>
            <pubDate>Wed, 02 Sep 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2770514</guid>        </item>
        <item>
            <title>Electricity generation coupled to oxidation of propionate in a microbial fuel cell.</title>
            <link>http://www.medworm.com/index.php?rid=2770513&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%3D19731045%26dopt%3DAbstract</link>
            <description>Authors: Jang JK, Chang IS, Hwang HY, Choo YF, Lee J, Cho KS, Kim BH, Nealson KH
    Propionate was used as fuel to enrich an electrochemically-active microbial consortium in a microbial fuel cell, and the bacterial consortium was analyzed by culture-independent methods including denaturing gradient gel electrophoresis (DGGE) of the 16S rDNA, and by fluorescent in situ hybridization (FISH). MFCs fed with propionate produced a current of 4.88 +/- 0.1 mA stably on 100 mg propionate/l as COD within 3 weeks of the enrichment. When the MFCs were fed with H(2)-saturated fuel containing propionate, the current dropped to 3.82 +/- 0.07 mA. The maximum current generated was up to 8.8 mA when MFCs were fed with 200 mg propionate/l as COD. The DGGE of 16S rDNA showed that propionate-enriched MFCs hav...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2770513</comments>
            <pubDate>Wed, 02 Sep 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2770513</guid>        </item>
        <item>
            <title>1,3-Dichloro-2-propanol induces apoptosis via both calcium and ROS in mouse melanoma cells.</title>
            <link>http://www.medworm.com/index.php?rid=2770512&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%3D19731046%26dopt%3DAbstract</link>
            <description>Authors: Park SY, Kim YH, Kim YH, Lee SJ
    We demonstrated that the apoptotic cell death of mouse melanoma cells exposed to 1,3-dichloro-2-propanol (DCP) was Ca(2+) dependent. 1,3-DCP inhibited the growth of mouse melanoma cells in a concentration-dependent manner. Furthermore, a terminal nick-end labeling of fragmented DNA (TUNEL) assay demonstrated that 1,3-DCP-induced apoptosis. Moreover, reactive oxygen species and Ca(2+), generated by mouse melanoma cells that were exposed to 1,3-DCP, resulted in the activation of NF-kappaB and MAPKs. Finally, treatment with BAPTA, an intracellular Ca(2+) chelator, completely inhibited the apoptosis that was induced by 1,3-DCP treatment of B16F10 cells.
    PMID: 19731046 [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=2770512</comments>
            <pubDate>Wed, 02 Sep 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2770512</guid>        </item>
        <item>
            <title>Sortase-mediated protein ligation: an emerging biotechnology tool for protein modification and immobilisation.</title>
            <link>http://www.medworm.com/index.php?rid=2766859&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%3D19728105%26dopt%3DAbstract</link>
            <description>Authors: Proft T
    Sortases are transpeptidases produced by Gram-positive bacteria to anchor cell surface proteins covalently to the cell wall. The Staphylococcus aureus sortase A (SrtA) cleaves a short C-terminal recognition motif (LPXTG) on the target protein followed by the formation of an amide bond with the pentaglycine cross-bridge in the cell wall. Over recent years, several researchers have exploited this specific reaction for a range of biotechnology applications, including the incorporation of non-native peptides and non-peptidic molecules into proteins, the generation of nucleic acid-peptide conjugates and neoglycoconjugates, protein circularisation, and labelling of cell surface proteins on living cells.
    PMID: 19728105 [PubMed - as supplied by publisher] (Source: Biotechn...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2766859</comments>
            <pubDate>Mon, 31 Aug 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2766859</guid>        </item>
        <item>
            <title>Roles of Ile66 and Ala107 of D: -psicose 3-epimerase from Agrobacterium tumefaciens in binding O6 of its substrate, D: -fructose.</title>
            <link>http://www.medworm.com/index.php?rid=2766858&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%3D19728106%26dopt%3DAbstract</link>
            <description>Authors: Kim HJ, Lim BC, Yeom SJ, Kim YS, Kim D, Oh DK
    Using site-directed mutagenesis, we investigated the roles of Ile66 and Ala107 of D: -psicose 3-epimerase from Agrobacterium tumefaciens in binding O6 of its true substrate, D: -fructose. When Ile66 was substituted with alanine, glycine, cysteine, leucine, phenylalanine, tryptophan, tyrosine or valine, all the mutants dramatically increased the K (m) for D: -tagatose but slightly decreased the K (m) for D: -fructose, indicating that Ile66 is involved in substrate recognition. When Ala107 was substituted by either isoleucine or valine, the substituted mutants had lower thermostability than the wild-type enzyme whereas the proline-substituted mutant had higher thermostability. Thus, Ala107 is involved in enzyme stability.
    PMID: 1...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2766858</comments>
            <pubDate>Mon, 31 Aug 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2766858</guid>        </item>
        <item>
            <title>Metabolic evolution of non-transgenic Escherichia coli SZ420 for enhanced homoethanol fermentation from xylose.</title>
            <link>http://www.medworm.com/index.php?rid=2766857&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%3D19728107%26dopt%3DAbstract</link>
            <description>Authors: Chen K, Iverson AG, Garza EA, Grayburn WS, Zhou S
    Efficient utilization of pentose sugars (xylose and arabinose) is an essential requirement for economically viable ethanol production from cellulosic biomass. The desirable pentose-fermenting ethanologenic biocatalysts are the native microorganisms or the engineered derivatives without recruited exogenous gene(s). We have used a metabolic evolution (adaptive selection) approach to improve a non-transgenic homoethanol Escherichia coli SZ420 (ldhA pflB ackA frdBC pdhR::pflBp6-aceEF-lpd) for xylose fermentation. An improved mutant, E. coli KC01, was evolved through a 3 month metabolic evolution process. This evolved mutant increased pyruvate dehydrogenase activity by 100%, cell growth rate (h(-1)) by 23%, volumetric ethanol produc...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2766857</comments>
            <pubDate>Mon, 31 Aug 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2766857</guid>        </item>
        <item>
            <title>A dual-reporter system for specific tracing of pancreatic ss-cell lines that non-invasively measures viable in vivo islet cells.</title>
            <link>http://www.medworm.com/index.php?rid=2766856&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%3D19728108%26dopt%3DAbstract</link>
            <description>Authors: Kim SK, Kim JY, Choi YS, Lee MK, Lee BW, Lee HC, Lee EJ
    Islet transplantation is a potential treatment for type 1 diabetes. Currently, islet graft survival is measured using invasive methods to determine blood glucose, insulin, and C-peptide levels, even though these variables have limited value. To trace beta-cell survival and functional status, we constructed an adenovirus/adenoassociate virus hybrid vector (Hyb-DR) carrying two reporter genes, luciferase and green fluorescent protein (GFP), linked by the internal ribosome entry site and driven by the rat insulin II promoter. Luciferase activity increased and positive GFP expression was observed in beta-cell lines (MIN6N8 and INS-1E) infected with Hyb-DR. Using an in vivo imaging instrument, the GFP signal was detected in th...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2766856</comments>
            <pubDate>Mon, 31 Aug 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2766856</guid>        </item>
        <item>
            <title>High-level expression, purification and characterization of a recombinant medium-temperature alpha-amylase from Bacillus subtilis.</title>
            <link>http://www.medworm.com/index.php?rid=2766855&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%3D19728109%26dopt%3DAbstract</link>
            <description>Authors: Liu Y, Lu F, Chen G, Snyder CL, Sun J, Li Y, Wang J, Xiao J
    Alpha-amylases are important industrial enzymes with a wide range of applications. Although medium-temperature alpha amylase (AmyE) has some practical advantages, its low yield has limited its applications. When an amyE gene from Bacillus subtilis BF768 was cloned into vector pWB980 and over-expressed in B. subtilis WB600, high activities (723 U ml(-1)) of secreted AmyE were produced. Recombinant AmyE was purified to a specific activity of 36 U mg(-1) having optimal activity at pH 6.0 and 60 degrees C.
    PMID: 19728109 [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=2766855</comments>
            <pubDate>Mon, 31 Aug 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2766855</guid>        </item>
        <item>
            <title>Construction and expression of a recombinant fibronectin(III)10 protein for integrin-mediated cell adhesion.</title>
            <link>http://www.medworm.com/index.php?rid=2742053&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%3D19707723%26dopt%3DAbstract</link>
            <description>Authors: Kim HW, Kang W, Jeon E, Jang JH
    Specific sequences of cell-adhesive peptide/proteins are often required for the bio-inert synthetic polymers to improve cell adhesion. We have developed a recombinant fibronectin fragment (FN(III)10), the central cell-binding domain containing RGD motif, to endow biomaterial surfaces with abilities to promote an integrin-mediated cell adhesion. Immobilized FN(III)10 stimulated adhesion of MC3TC-E1 cells in an integrin-dependent manner.
    PMID: 19707723 [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=2742053</comments>
            <pubDate>Tue, 25 Aug 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2742053</guid>        </item>
        <item>
            <title>Migratory response of mesenchymal stem cells to macrophage migration inhibitory factor and its antagonist as a function of colony-forming efficiency.</title>
            <link>http://www.medworm.com/index.php?rid=2735108&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%3D19705068%26dopt%3DAbstract</link>
            <description>Authors: Fischer-Valuck BW, Barrilleaux BL, Phinney DG, Russell KC, Prockop DJ, O'Connor KC
    Human mesenchymal stem cells (MSCs) are capable of repairing pulmonary disorders, but their efficacy is limited by poor engraftment. A strategy is proposed to augment MSC migration to lung tissue by antagonizing macrophage migration inhibitory factor (MIF), a pro-inflammatory cytokine. Recombinant MIF (85 ng/ml) inhibited in vitro chemokinesis of multipotent MSCs by nearly 50 and 20% for donor preparations with colony-forming efficiencies of 22 +/- 4% and 66 +/- 3%, respectively (P &amp;lt; 0.05). The small-molecule MIF antagonist, (S,R)-3-(4-hydroxyphenyl)-4,5-dihydro-5-isoxazole acetic acid methyl ester (ISO-1, 85 mug/ml), restored MSC migration for all donors to levels found in the absence of MIF...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2735108</comments>
            <pubDate>Mon, 24 Aug 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2735108</guid>        </item>
        <item>
            <title>Evaluation of small ligand-protein interaction by ligation reaction with DNA-modified ligand.</title>
            <link>http://www.medworm.com/index.php?rid=2735107&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%3D19705069%26dopt%3DAbstract</link>
            <description>Authors: Sugita R, Mie M, Funabashi H, Kobatake E
    A method for the evaluation of interactions between protein and ligand using DNA-modified ligands, including signal enhancement of the DNA ligation reactions, is described. For proof of principle, a DNA probe modified by biotin was used. Two DNA probes were prepared with complementary sticky-ends. While one DNA probe was modified at the 5'-end of the sticky-end, the other was not modified. The probes could be ligated together by T4 DNA ligase along the strand without biotin modification. However, in the presence of streptavidin or anti-biotin Fab, the ligation reaction joining the two probes could not occur on either strand.
    PMID: 19705069 [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=2735107</comments>
            <pubDate>Mon, 24 Aug 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2735107</guid>        </item>
        <item>
            <title>Kinetic and metabolic analysis of mouse embryonic stem cell expansion under serum-free conditions.</title>
            <link>http://www.medworm.com/index.php?rid=2735106&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%3D19705070%26dopt%3DAbstract</link>
            <description>Authors: Fernandes TG, Fernandes-Platzgummer AM, da Silva CL, Diogo MM, Cabral JM
    There is a need for a deeper understanding of the biochemical events affecting embryonic stem (ES) cell culture by analyzing the expansion of mouse ES cells in terms of both cell growth and metabolic kinetics. The influence of the initial cell density on cell expansion was assessed. Concomitantly, the biochemical profile of the culture was evaluated, which allowed measuring the consumption of important substrates, such as glucose and glutamine, and the production of metabolic byproducts, like lactate. The results suggest a more efficient cell metabolism in serum-free conditions and a preferential use of glutaminolysis as an energy source during cell expansion at low seeding densities. This work contribute...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2735106</comments>
            <pubDate>Mon, 24 Aug 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2735106</guid>        </item>
        <item>
            <title>Continuous cultivation approach for fermentative succinic acid production from crude glycerol by Basfia succiniciproducens DD1.</title>
            <link>http://www.medworm.com/index.php?rid=2735105&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%3D19705071%26dopt%3DAbstract</link>
            <description>Authors: Scholten E, Renz T, Thomas J
    A continuous cultivation process for the fermentative production of succinic acid from glycerol with the recently isolated bacterium Basfia succiniciproducens DD1 was developed. Crude glycerol (5.1 g l(-1)) was used as C-source and NH(4)OH as N-source and pH-control agent. The problem of wall growth was solved by transfers of the cultivation broth into an empty identical fermentor. The resulting continuous cultivation process was maintained for more than 80 days. Glycerol-limited steady states were established for dilution rates between 0.004 and 0.018 h(-1). Higher dilution rates resulted in glycerol accumulation. Succinic acid concentrations, productivities, yields and specific productivities increased with increasing dilution rates: at 0.018 h(-...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2735105</comments>
            <pubDate>Mon, 24 Aug 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2735105</guid>        </item>
        <item>
            <title>Metabolic changes of salicylic acid-elicited Catharanthus roseus cell suspension cultures monitored by NMR-based metabolomics.</title>
            <link>http://www.medworm.com/index.php?rid=2735109&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%3D19701606%26dopt%3DAbstract</link>
            <description>Authors: Mustafa NR, Kim HK, Choi YH, Verpoorte R
    The effect of salicylic acid (SA) on the metabolic profile of Catharanthus roseus suspension cells throughout a time course (0, 6, 12, 24, 48 and 72 h after treatment) was investigated using NMR spectroscopy and multivariate data analysis. When compared to control cell lines, SA-treated cells showed a high level of sugars (glucose and sucrose) up to 48 h after treatment, followed by a dynamic change in amino acids, phenylpropanoids, and tryptamine. Additionally, one compound-2,5-dihydroxybenzoic-5-O-glucoside-was detected solely in SA-treated cells.
    PMID: 19701606 [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=2735109</comments>
            <pubDate>Fri, 21 Aug 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2735109</guid>        </item>
        <item>
            <title>Grape skins (Vitis vinifera L.) catalyze the in vitro enzymatic hydroxylation of p-coumaric acid to caffeic acid.</title>
            <link>http://www.medworm.com/index.php?rid=2724081&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%3D19696970%26dopt%3DAbstract</link>
            <description>Authors: Arnous A, Meyer AS
    The ability of grape skins to catalyze in vitro conversion of p-coumaric acid to the more potent antioxidant caffeic acid was studied. Addition of different concentrations of p-coumaric to red grape skins (Cabernet Sauvignon) resulted in formation of caffeic acid. This caffeic acid formation (Y) correlated positively and linearly to p-coumaric acid consumption (X): Y = 0.5 X + 9.5; R (2) = 0.96, P &amp;lt; 0.0001. The kinetics of caffeic acid formation with time in response to initial p-coumaric acid levels and at different grape skin concentrations, indicated that the grape skins harboured an o-hydroxylation activity, proposedly a monophenol- or a flavonoid 3'-monooxygenase activity (EC 1.14.18.1 or EC 1.14.13.21). The K (m) of this crude o-hydroxylation activi...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2724081</comments>
            <pubDate>Thu, 20 Aug 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2724081</guid>        </item>
        <item>
            <title>Identification of mokB involved in monacolin K biosynthesis in Monascus pilosus.</title>
            <link>http://www.medworm.com/index.php?rid=2720332&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%3D19693441%26dopt%3DAbstract</link>
            <description>Authors: Sakai K, Kinoshita H, Nihira T
    Monacolin K (MK), which is widely used as an antihypercholesterolemia medicine, is produced as a fungal secondary metabolite through the polyketide pathway. The MK biosynthetic gene cluster proposed for Monascus pilosus BCRC38072 was also identified in M. pilosus NBRC4480. The mokB gene, located at the end of the putative gene cluster and possibly encoding polyketide synthase, was disrupted. The mokB disruptant did not produce MK, but accumulated an intermediate that was confirmed to be monacolin J, indicating that mokB encodes the polyketide synthase responsible for the biosynthesis of side-chain diketide moiety.
    PMID: 19693441 [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=2720332</comments>
            <pubDate>Wed, 19 Aug 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2720332</guid>        </item>
        <item>
            <title>Characterization of native Bacillus thuringiensis strains and selection of an isolate active against Spodoptera frugiperda and Peridroma saucia.</title>
            <link>http://www.medworm.com/index.php?rid=2720331&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%3D19693442%26dopt%3DAbstract</link>
            <description>Authors: Alvarez A, Virla EG, Pera LM, Baigor&amp;#xED; MD
    Twelve Bacillus thuringiensis (Bt) strains, isolated from larvae and soil samples in Argentina, were molecularly and phenotypically characterized and their insecticidal activities against Spodoptera frugiperda and Peridroma saucia were determined. One isolate-Bt RT-produced more than 93% mortality on first instar larvae of both species, which was higher than that produced by the reference strain Bt 4D1. Bt RT carried a different cry gene profile than Bt 4D1. Scanning electron microscopy showed the presence of bipyramidal and cuboidal crystals. Phenotypic characterization revealed lytic enzymes that could contribute to Bt pathogenicity.
    PMID: 19693442 [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=2720331</comments>
            <pubDate>Wed, 19 Aug 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2720331</guid>        </item>
        <item>
            <title>A multiplex PCR technique to characterize human bone marrow derived mesenchymal stem cells.</title>
            <link>http://www.medworm.com/index.php?rid=2720330&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%3D19693443%26dopt%3DAbstract</link>
            <description>Authors: Rallapalli S, Bishi DK, Verma RS, Cherian KM, Guhathakurta S
    Human mesenchymal stem cells (MSCs), with capacity to differentiate into adipocytes, osteoblasts and chondrocytes, offer potential for the development of novel treatments. A critical question in MSCs biology is whether this cell population possesses a relatively uniform differentiation capability or is comprised of distinct subsets of progenitors committed to differentiate in particular pathways. To quantify the changes during growth of MSCs, we analyzed the mesenchymal phenotype and differentiation ability using a multi-marker PCR with six primer sets specific for CD73, CD90, CD105, CD166, CD45 and beta-actin allowing a gel-based differential detection of the PCR products. To determine degree of variability of MSCs ...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2720330</comments>
            <pubDate>Wed, 19 Aug 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2720330</guid>        </item>
        <item>
            <title>Probing key targets in insulin signaling and adipogenesis using a methanolic extract of Costus pictus and its bioactive molecule, methyl tetracosanoate.</title>
            <link>http://www.medworm.com/index.php?rid=2720329&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%3D19693444%26dopt%3DAbstract</link>
            <description>Authors: Shilpa K, Sangeetha KN, Muthusamy VS, Sujatha S, Lakshmi BS
    A methanolic extract of Costus pictus (CPME) showed optimum anti-diabetic activity at 100 ng/ml. Bioactivity-guided purification of CPME led to the isolation of methyl tetracosanoate (MT) which showed an optimum glucose uptake at 1 ng/ml. CPME at 10 mug/ml inhibited adipogenesis whereas fully differentiated adipocytes exhibited a 3-fold increase in lipid accumulation compared to pre-adipocytes. Gene and protein expression of key targets in insulin signaling and adipogenesis pathway revealed that CPME exhibited anti-diabetic activity along with anti-adipogenic activity whereas MT demonstrated only anti-diabetic activity.
    PMID: 19693444 [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=2720329</comments>
            <pubDate>Wed, 19 Aug 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2720329</guid>        </item>
        <item>
            <title>Delivery of recombinant bone morphogenetic proteins for bone regeneration and repair. Part A: Current challenges in BMP delivery.</title>
            <link>http://www.medworm.com/index.php?rid=2720340&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%3D19690804%26dopt%3DAbstract</link>
            <description>Authors: Haidar ZS, Hamdy RC, Tabrizian M
    Recombinant human bone morphogenetic proteins (rhBMPs) have been extensively investigated for developing therapeutic strategies aimed at the restoration and treatment of orthopaedic as well as craniofacial conditions. In this first part of the review, we discuss the rationale for the necessary use of carrier systems to deliver rhBMP-2 and rhBMP-7 to sites of bone tissue regeneration and repair. General requirements for growth factor delivery systems emphasizing the distinction between localized and release-controlled delivery strategies are presented highlighting the current limitations in the development of an effective rhBMP delivery system applicable in clinical bone tissue engineering.
    PMID: 19690804 [PubMed - as supplied by publisher] ...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2720340</comments>
            <pubDate>Tue, 18 Aug 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2720340</guid>        </item>
        <item>
            <title>A seed coat-specific promoter for canola.</title>
            <link>http://www.medworm.com/index.php?rid=2720339&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%3D19690805%26dopt%3DAbstract</link>
            <description>Authors: El-Mezawy A, Wu L, Shah S
    The canola industry generates more than $11 billion of yearly income to the Canadian economy. One problem of meal quality is the dark polyphenolic pigments that accumulate in the seed coat. Seed coat-specific promoters are a pre-requisite to regulate the genes involved in seed coat development and metabolism. The beta-glucuronidase (GUS) reporter gene was used to test an Arabidopsis promoter in developing and mature seeds of canola (Brassica napus). The promoter tested is the regulatory region of the laccase gene (AtLAC15) from Arabidopsis thaliana. The AtLAC15 promoter::GUS construct was inserted into canola double haploid line DH12075 using Agrobacterium-mediated transformation. Southern blot analysis using a 536 bp GUS probe showed variation among ...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2720339</comments>
            <pubDate>Tue, 18 Aug 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2720339</guid>        </item>
        <item>
            <title>Aerobic microbial manufacture of nanoscale selenium: exploiting nature's bio-nanomineralization potential.</title>
            <link>http://www.medworm.com/index.php?rid=2720338&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%3D19690806%26dopt%3DAbstract</link>
            <description>Authors: Tejo Prakash N, Sharma N, Prakash R, Raina KK, Fellowes J, Pearce CI, Lloyd JR, Pattrick RA
    The potential of the environment to yield organisms that can produce functional bionanominerals is demonstrated by selenium-tolerant, aerobic bacteria isolated from a seleniferous rhizosphere soil. An isolate, NS3, was identified as a Bacillus species (EU573774.1) based on morphological and 16S rRNA characterization. This strain reduced Se(IV) under aerobic conditions to produce amorphous alpha Se(0) nanospheres. A room-temperature washing treatment was then employed to remove the biomass and resulted in the production of clusters of hexagonal Se(0) nano-rods. The Se(0) nanominerals were analyzed using electron microscopy and X-ray diffraction techniques. This Bacillus isolate has the p...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2720338</comments>
            <pubDate>Tue, 18 Aug 2009 23:00:00 +0100</pubDate>
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        <item>
            <title>Construction of a novel zero background prokaryotic expression vector: potential advantages.</title>
            <link>http://www.medworm.com/index.php?rid=2720337&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%3D19690807%26dopt%3DAbstract</link>
            <description>Authors: Mandi N, Kotwal P, Padmanabhan S
    A novel DNA sequence, derived from the antisense strand of the DNA gyrase inhibitor protein, CcdB, was toxic to E. coli. This protein (~6 kDa) decreased the growth rate of E. coli K12 by three orders of magnitude upon induction. The expressed toxic protein in E. coli K12 was soluble while it was insoluble in induced E. coli BL21. A high efficiency prokaryotic cloning/expression vector was constructed using this toxic gene sequence and gave zero background with ~100% cloning efficiency requiring no dephosphorylation. The toxic gene product also affected the survival of a ccdB resistant cell line, thus indicating a different mechanism of toxicity, other than DNA gyrase inhibition, as compared to the ccdB toxicity.
    PMID: 19690807 [PubMed - as ...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2720337</comments>
            <pubDate>Tue, 18 Aug 2009 23:00:00 +0100</pubDate>
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        <item>
            <title>A MOFRL family glycerate kinase from the thermophilic crenarchaeon, Sulfolobus tokodaii, with unique enzymatic properties.</title>
            <link>http://www.medworm.com/index.php?rid=2720336&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%3D19690808%26dopt%3DAbstract</link>
            <description>Authors: Liu B, Wu L, Liu T, Hong Y, Shen Y, Ni J
    A glycerate kinase gene (ST2037) from the hyperthermophilic crenarchaeon Sulfolobus tokodaii was cloned and expressed in Escherichia coli. The purified homodimeric protein (45 kDa) specifically catalyzed the formation of 2-phosphoglycerate with D: -glycerate as substrate. The thermostable enzyme displayed maximum activity (over 20 min) at 90 degrees C and pH 4.5. The maximal activity was in the presence of Co(2+). The MOFRL family glycerate kinase used AMP as phosphate donor with maximal activity towards GTP. These characteristics of the enzyme suggested its potential in the catalytic production of 2-phosphoglycerate.
    PMID: 19690808 [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=2720336</comments>
            <pubDate>Tue, 18 Aug 2009 23:00:00 +0100</pubDate>
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        <item>
            <title>Increasing M2 epitope density enhances systemic and mucosal immune responses to influenza A virus.</title>
            <link>http://www.medworm.com/index.php?rid=2720335&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%3D19690809%26dopt%3DAbstract</link>
            <description>Authors: Pei S, Xiong N, Zhang Y, Chen S
    Recombinant proteins bearing one (sM2) or three (3sM2) copies of M2 epitope from influenza virus were expressed in Escherichia coli. Mice were administrated with these two proteins and systemic and mucosal immune responses were analyzed. Compared with sM2, 3sM2 induced M2-specific serum IgG and mucosal IgA antibodies with neutralizing activity more efficiently in the whole immune course and the later mucosal immunization improved this advantage. MDCK cells pretreated with 3sM2 antisera showed less pathogenic morphological changes compared with that of pretreated with sM2. Together, our results demonstrated that high epitope density in one recombinant protein can enhance humoral immune responses in both systemic and mucosal immunization, and comb...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2720335</comments>
            <pubDate>Tue, 18 Aug 2009 23:00:00 +0100</pubDate>
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        <item>
            <title>Chemoporation using saponins or cholates: an alternative method for transformation of bacterial cells.</title>
            <link>http://www.medworm.com/index.php?rid=2720334&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%3D19690810%26dopt%3DAbstract</link>
            <description>Authors: Ravnikar M, Irman A, Radi&amp;#x107; N, Lunder M, Strukelj B
    A new method for fast transformation of competent bacterial cells has been developed. The transformation is induced with cholic acid analogues or saponins which cause reversible disruption of the bacterial membrane. This method shortens the time of transformation without significant loss of transformation efficiency in comparison to heat shock method and is the first reported chemically-induced transformation. New data about interactions between cholates and biomembranes is revealed that may contribute to better understanding of bacterial transformation.
    PMID: 19690810 [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=2720334</comments>
            <pubDate>Tue, 18 Aug 2009 23:00:00 +0100</pubDate>
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        <item>
            <title>Delivery of recombinant bone morphogenetic proteins for bone regeneration and repair. Part B: Delivery systems for BMPs in orthopaedic and craniofacial tissue engineering.</title>
            <link>http://www.medworm.com/index.php?rid=2720333&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%3D19690811%26dopt%3DAbstract</link>
            <description>Authors: Haidar ZS, Hamdy RC, Tabrizian M
    Localized and release-controlled delivery systems for the sustained expression of the biologic potency of rhBMPs are essential. A substantial number of biomaterials have been investigated thus far. Most fail after implantation or administration mainly due to either being too soft, difficult to control and/or stabilize mechanically. In the second part of this review, we review a representative selection of rhBMP-2 and rhBMP-7 carrier materials and delivery systems ranging from simple nano/microparticles to complex 3-D scaffolds in sites of orthopaedic and craniofacial bone regeneration and repair.
    PMID: 19690811 [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=2720333</comments>
            <pubDate>Tue, 18 Aug 2009 23:00:00 +0100</pubDate>
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        <item>
            <title>Proteomics of proteins associated with astaxanthin accumulation in the green algae Haematococcus lacustris under the influence of sodium orthovanadate.</title>
            <link>http://www.medworm.com/index.php?rid=2713014&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%3D19685207%26dopt%3DAbstract</link>
            <description>Authors: Tran NP, Park JK, Hong SJ, Lee CG
    An extensive proteomics analysis has identified proteins associated with astaxanthin accumulation in the green algae Haematococcus lacustris under oxidative stress induced by sodium orthovanadate (SOV). Measurement of total carotenoid accumulation per cell biomass showed an increase from 81 to 136 pg/cell after being exposed to 2.5 mM SOV, when compared to the control cells at day 3 of cultivation. A total of 83 proteins were differentially expressed in SOV-treated H. lacustris in comparison with control cells. They consisted of 34 down-regulated and 49 up-regulated proteins. Of these, 17 highly-expressed proteins were analyzed by MALDI-TOF-MS to identify the function of the differentially expressed proteins in response to oxidative stress in ...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2713014</comments>
            <pubDate>Fri, 14 Aug 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2713014</guid>        </item>
        <item>
            <title>Construction and characterization of a novel staphylokinase variant with thrombin-inhibitory activity.</title>
            <link>http://www.medworm.com/index.php?rid=2713013&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%3D19685208%26dopt%3DAbstract</link>
            <description>Authors: Wang M, Wang Y, Wang J, Zou M, Liu S, Xu T, Cai X, Wu C, Wang J, Xu D
    Staphylokinase (SAK) is an effective thrombolysis agent for therapy of myocardial infarction. We have constructed a fusion SAK variant (SAK-HV) with a thrombin-binding domain composed of 12 amino acids from hirudin and expressed it in Escherichia coli and purified the resultant protein. SAK-HV maintained fibrinolytic activity similar to SAK and had anticoagulant activity attributable to its hirudin segment. Measurement of thrombin-binding activity in vitro demonstrated that SAK-HV possessed binding activity with thrombin while SAK did not. SAK-HV might thus be a more potent thrombolytic agent with anticoagulation property than SAK.
    PMID: 19685208 [PubMed - as supplied by publisher] (Source: Biotechnology...</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2713013</comments>
            <pubDate>Fri, 14 Aug 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2713013</guid>        </item>
        <item>
            <title>Improved ethanol tolerance in Escherichia coli by changing the cellular fatty acids composition through genetic manipulation.</title>
            <link>http://www.medworm.com/index.php?rid=2713012&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%3D19685209%26dopt%3DAbstract</link>
            <description>Authors: Luo LH, Seo PS, Seo JW, Heo SY, Kim DH, Kim CH
    To investigate the effect of cellular fatty acids composition on ethanol tolerance in Escherichia coli, we overexpressed either des, encoding fatty acid desaturase from Bacillus subtilis, or fabA, encoding beta-hydroxydecanoyl thio-ester dehydrase from E. coli, or both genes together, into E. coli. Recombinant E. coli harboring fabA had elevated tolerance against ethanol compared to wild type strain. In contrast, des decreased resistance to ethanol. Co-expression of both genes together complemented ethanol tolerance of E. coli. This result indicates how to engineer bacterial strains to be resistant to higher concentrations of ethanol.
    PMID: 19685209 [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=2713012</comments>
            <pubDate>Fri, 14 Aug 2009 23:00:00 +0100</pubDate>
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            <title>cry1 genes from Bacillus thuringiensis: specificity determination and implications for primer design.</title>
            <link>http://www.medworm.com/index.php?rid=2654099&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%3D19636520%26dopt%3DAbstract</link>
            <description>Authors: Davolos CC, Guidelli-Thuler AM, de Abreu IL, Sena JA, Lemos MV
    Some pest management programs employ PCR to identify cry1 genes from Bacillus thuringiensis to predict bacterial toxicity towards different insect pests. However, due to changes on the mode of action of the Cry proteins, new primers had to be designed to detect the new genes. Therefore, an 'in-silico' study of genetic sequences from five cry1 subclasses was carried out and characterized by molecular tools. The design of new primers allows for more precise selection of B. thuringiensis isolates, helping to better direct the programs employing biological control.
    PMID: 19636520 [PubMed - as supplied by publisher] (Source: Biotechnology Letters)</description>
            <author>Biotechnology Letters</author>
            <type>journals</type>
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            <pubDate>Mon, 27 Jul 2009 23:00:00 +0100</pubDate>
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