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        <title>New Biotechnology via MedWorm.com</title>
        <description>MedWorm.com provides a medical RSS filtering service. Over 6000 RSS medical sources are combined and output via different filters. This feed contains the latest items from the 'New Biotechnology' source.</description>
        <link><![CDATA[http://www.medworm.com/rss/search.php?qu=New+Biotechnology&t=New+Biotechnology&s=Search&f=source]]></link>
        <lastBuildDate>Mon, 06 Feb 2012 18:10:54 +0100</lastBuildDate>
        <item>
            <title>Global transcriptional changes of Clostridium acetobutylicum cultures with increased butanol:acetone ratios.</title>
            <link>http://www.medworm.com/index.php?rid=5658890&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22285530%26dopt%3DAbstract</link>
            <description>In this study, first insights on the molecular level were gained to explore the effect of methyl viologen addition to cultures of Clostridium acetobutylicum. Employing batch fermentation in mineral salts medium, the butanol:acetone ratio was successively increased from 2.3 to 12.4 on a 100-ml scale in serum bottles and from 1.4 to 16.5 on a 1300-ml scale in bioreactors, respectively. The latter cultures were used for DNA microarray analyses to provide new information on the transcriptional changes referring to methyl viologen exposure and thus, exhibit gene expression patterns according to the manipulation of the cellular redox balance. Methyl viologen-exposed cultures revealed lower expression levels of the sol operon (CAP0162-0164) and the adjacent adc gene (CAP0165) responsible for solv...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5658890</comments>
            <pubDate>Sat, 21 Jan 2012 05:00:00 +0100</pubDate>
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        <item>
            <title>Simple scale-up of recombinant antibody production using an UCOE containing vector.</title>
            <link>http://www.medworm.com/index.php?rid=5578033&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22226921%26dopt%3DAbstract</link>
            <description>Authors: Boscolo S, Mion F, Licciulli M, Macor P, De Maso L, Brce M, Antoniou M, Marzari R, Santoro C, Sblattero D
    Abstract
    Recombinant proteins, in particular antibodies, have become fundamental in biomedical research where they are used in numerous therapeutic and diagnostic applications. For this reason there is an increasing demand for quick and economical production systems for recombinant proteins in mammalian cells. Among different approaches employed for rapidly obtaining stable and highly producing cell lines, is the use of expression vectors with transgenes under control of a ubiquitous chromatin-opening element (UCOE). UCOEs consist of methylation-free CpG islands encompassing dual divergently transcribed promoters of housekeeping genes and confer resistance to transcrip...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5578033</comments>
            <pubDate>Wed, 28 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5578033</guid>        </item>
        <item>
            <title>Next-generation biomarkers based on 100-parameter functional super-resolution microscopy TIS.</title>
            <link>http://www.medworm.com/index.php?rid=5559929&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22209707%26dopt%3DAbstract</link>
            <description>Authors: Schubert W, Gieseler A, Krusche A, Serocka P, Hillert R
    Abstract
    Functional super-resolution (fSR) microscopy is based on the automated toponome imaging system (TIS). fSR-TIS provides insight into the myriad of different cellular functionalities by direct imaging of large subcellular protein networks in morphologically intact cells and tissues, referred to as the toponome. By cyclical fluorescence imaging of at least 100 molecular cell components, fSR-TIS overcomes the spectral limitations of fluorescence microscopy, which is the essential condition for the detection of protein network structures in situ/in vivo. The resulting data sets precisely discriminate between cell types, subcellular structures, cell states and diseases (fSR). With up to 16bits per protein, the powe...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5559929</comments>
            <pubDate>Wed, 21 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5559929</guid>        </item>
        <item>
            <title>Social and legal determinants for the marketing of GM products in Poland.</title>
            <link>http://www.medworm.com/index.php?rid=5559928&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22210291%26dopt%3DAbstract</link>
            <description>Authors: Twardowski T, Małyska A
    Abstract
    The development of biotechnology is influenced by many factors unique for a specific region. In Poland the lack of legislative solutions (to facilitate the promotion of the inventions) and the public resistance against certain sectors of biotechnology are significant factors limiting any further development. Although, science and technology are the front runners in any innovation, the significance of social and legal aspects is difficult to overestimate. In our opinion those factors are interconnected and crucial for marketing of innovative products, therefore, we indicate and explain the most important issues restraining the implementation of innovative biotechnology in the context of national specificity in Poland.
    PMID: 22210291 [Pu...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5559928</comments>
            <pubDate>Wed, 21 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5559928</guid>        </item>
        <item>
            <title>Recent advances in environmental biotechnology.</title>
            <link>http://www.medworm.com/index.php?rid=5419290&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22083036%26dopt%3DAbstract</link>
            <description>Authors: 
    PMID: 22083036 [PubMed - in process] (Source: New Biotechnology)</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5419290</comments>
            <pubDate>Fri, 18 Nov 2011 11:36:15 +0100</pubDate>
            <guid isPermaLink="false">5419290</guid>        </item>
        <item>
            <title>Fatty acid profiling and molecular characterization of some freshwater microalgae from India with potential for biodiesel production.</title>
            <link>http://www.medworm.com/index.php?rid=5379453&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22044601%26dopt%3DAbstract</link>
            <description>Authors: Kaur S, Sarkar M, Srivastava RB, Gogoi HK, Kalita MC
    Abstract
    We determined the fatty acid compositions of six species of freshwater microalgae belonging to the Chlorophyta, which were isolated from freshwater bodies in Assam, India. All six microalgae -Desmodesmus sp. DRLMA7, Desmodesmus elegans DRLMA13, Scenedesmus sp. DRLMA5, Scenedesmus sp. DRLMA9 Chlorella sp. DRLMA3 and Chlorococcum macrostigmatum DRLMA12-showed similar fatty acid profiles 16:0, 16:4, 18:1, 18:2, and 18:3 as major components. We also compared fatty acid compositions during the late exponential and stationary growth phases of D. elegans DRLMA13 and Scenedesmus sp. DRLMA9 in BG11 medium. We observed enhanced percentages of total saturated and monounsaturated fatty acids with a concomitant decrease in p...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5379453</comments>
            <pubDate>Sat, 22 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5379453</guid>        </item>
        <item>
            <title>Monitored whole gene in vitro evolution of an anti-hRaf-1 affibody molecule towards increased binding affinity.</title>
            <link>http://www.medworm.com/index.php?rid=5379457&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22027369%26dopt%3DAbstract</link>
            <description>Authors: Grimm S, Salahshour S, Nygren PA
    Abstract
    The use of library technologies for the generation of affinity proteins often includes an affinity maturation step, based on the construction of secondary libraries from which second generation variants with improved affinities are selected. Here, we describe for the first time the affinity maturation of affibody molecules based on step-wise in vitro molecular evolution, involving cycles of error-prone PCR (epPCR) amplification for the introduction of diversity over the entire 58-residue three-helix bundle structure and ribosome display (RD) for the selection of improved variants. The model affibody molecule for the process was Z(RAF322), binding with a 1.9μm equilibrium dissociation constant (K(D)) to human Raf-1 (hRaf-1), a prot...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5379457</comments>
            <pubDate>Wed, 19 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5379457</guid>        </item>
        <item>
            <title>Expressing the human proteome for affinity proteomics: optimising expression of soluble protein domains and in vivo biotinylation.</title>
            <link>http://www.medworm.com/index.php?rid=5379456&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22027370%26dopt%3DAbstract</link>
            <description>We present a summary of the approaches used to generate purified human proteins or protein domains, a test case demonstrating the ability to rapidly generate new proteins, and an optimisation study on the modification of &amp;gt;70 proteins by biotinylation in vivo. These results provide a unique synergy between large-scale structural projects and the recent efforts to produce a wide coverage of affinity reagents to the human proteome.
    PMID: 22027370 [PubMed - as supplied by publisher] (Source: New Biotechnology)</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5379456</comments>
            <pubDate>Wed, 19 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5379456</guid>        </item>
        <item>
            <title>Wave characterization for mammalian cell culture: residence time distribution.</title>
            <link>http://www.medworm.com/index.php?rid=5379455&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22027371%26dopt%3DAbstract</link>
            <description>This study evaluated the residence time distribution (RTD) in Wave, allowing the characterization of mixing and flow and the comparison with ideal models and a Stirred tank reactor (STR) used for mammalian cell culture. RTD was determined using methylene blue with pulse input methodology, at three flow rates common in mammalian cell culture (3.3×10(-5)m(3)/h, 7.9×10(-5)m(3)/h, and 1.25×10(-4)m(3)/h) and one typical of microbial culture (5×10(-3)m(3)/h). Samples were taken periodically and the absorbance read at 660nm. It was observed that Wave behavior diverted from ideal models, but was similar to STR. Therefore, the deviations are not related to the particular Wave rocking mechanism, but could be associated with the inadequacy of these reactors to operate in continuous mode or to a p...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5379455</comments>
            <pubDate>Tue, 18 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5379455</guid>        </item>
        <item>
            <title>Classification of protein profiles from antibody microarrays using heat and detergent treatment.</title>
            <link>http://www.medworm.com/index.php?rid=5379458&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22023822%26dopt%3DAbstract</link>
            <description>Authors: Häggmark A, Neiman M, Drobin K, Zwahlen M, Uhlen M, Nilsson P, Schwenk JM
    Abstract
    Antibody microarrays offer new opportunities for exploring the proteome and to identify biomarker candidates in human serum and plasma. Here, we have investigated the effect of heat and detergents on an antibody-based suspension bead array (SBA) assay using polyclonal antibodies and biotinylated plasma samples. With protein profiles from more than 2300 antibodies generated in 384-plex antibody SBAs, three major classes of heat and detergent susceptibility could be described. The results show that washing of the beads with SDS (rather than Tween) after target binding lowered intensity levels of basically all profiles and that about 50% of the profiles appeared to be lowered to a similar exte...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5379458</comments>
            <pubDate>Fri, 14 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5379458</guid>        </item>
        <item>
            <title>Recombinant Protein Production 6 (Vienna, February 2011).</title>
            <link>http://www.medworm.com/index.php?rid=5379454&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22032951%26dopt%3DAbstract</link>
            <description>Authors: Gasser B, Mattanovich D, Maurer M, Sauer M
    Abstract
    The sixth edition of the Conference on Recombinant Protein Production saw a return of physiology-based cell and process engineering. While the application of omics technologies to cell engineering has been constantly on the rise during the past decade, the concept of systems biotechnology is now also applied on bioprocesses bringing new insights into process design and production strategies. The conference brought an extensive comparative view on host cell physiology, covering all areas of bacterial, yeast, fungal, insect, plant and mammalian protein production hosts. Global (genome scale) cellular analysis led to local cell engineering strategies covering also interspecies host optimization strategies, and bringing energ...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5379454</comments>
            <pubDate>Fri, 14 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5379454</guid>        </item>
        <item>
            <title>Recombinant protein production 6: a comparative view on host physiology.</title>
            <link>http://www.medworm.com/index.php?rid=5379461&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22019830%26dopt%3DAbstract</link>
            <description>Authors: Cole J, Ferrer P, Mattanovich D, Archer D
    PMID: 22019830 [PubMed - as supplied by publisher] (Source: New Biotechnology)</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5379461</comments>
            <pubDate>Thu, 13 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5379461</guid>        </item>
        <item>
            <title>High hydrostatic pressure treatment for the inactivation of Staphylococcus aureus in human blood plasma.</title>
            <link>http://www.medworm.com/index.php?rid=5379483&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22008386%26dopt%3DAbstract</link>
            <description>Authors: Rivalain N, Roquain J, Boiron JM, Maurel JP, Largeteau A, Ivanovic Z, Demazeau G
    Abstract
    For the past 30years, pressure inactivation of microorganisms has been developed in biosciences, in particular for foods and more recently for biological products, including pharmaceutical ones. In many past studies, the effect of high hydrostatic pressure (HHP) processes on pathogens focused mainly on the effect of an increase of the pressure value. To assure the safety of pharmaceutical products containing fragile therapeutic components, development of new decontamination processes at the lowest pressure value is needed to maintain their therapeutic properties. The aim of this study was therefore to evaluate the impact of the process parameters characterizing high-pressure treatment...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5379483</comments>
            <pubDate>Tue, 11 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5379483</guid>        </item>
        <item>
            <title>Continuous steroid biotransformations in microchannel reactors.</title>
            <link>http://www.medworm.com/index.php?rid=5379482&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22008387%26dopt%3DAbstract</link>
            <description>Authors: Marques MP, Fernandes P, Cabral JM, Znidaršič-Plazl P, Plazl I
    Abstract
    The use of microchannel reactor based technologies within the scope of bioprocesses as process intensification and production platforms is gaining momentum. Such trend can be ascribed a particular set of characteristics of microchannel reactors, namely the enhanced mass and heat transfer, combined with easier handling and smaller volumes required, as compared to traditional reactors. In the present work, a continuous production process of 4-cholesten-3-one by the enzymatic oxidation of cholesterol without the formation of any by-product was assessed. The production was carried out within Y-shaped microchannel reactors in an aqueous-organic two-phase system. Substrate was delivered from the organic ph...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5379482</comments>
            <pubDate>Sat, 08 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5379482</guid>        </item>
        <item>
            <title>Bacterial cell disruption: a crucial step in protein production.</title>
            <link>http://www.medworm.com/index.php?rid=5296441&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21979792%26dopt%3DAbstract</link>
            <description>Authors: Peternel S
    Abstract
    Recombinant protein production significantly improved in the past three decades. Novel expression systems were developed, growth conditions optimised and the technology and thus monitoring and analysis significantly enhanced. However, the studies of bacterial cell disruption were more or less neglected. The existing methods were acceptable until the final product of protein production was soluble and pure protein. However recently, inclusion bodies (IBs) as whole protein particles were also recognised as the final product. Classical methods for bacterial cell disruption are therefore not always suitable, sufficient or even appropriate for isolation of such particulate material. Some of the currently existing methods for bacterial cell disruption were re...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5296441</comments>
            <pubDate>Sat, 01 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5296441</guid>        </item>
        <item>
            <title>Intracellular protein production in Trichoderma reesei (Hypocrea jecorina) with hydrophobin fusion technology.</title>
            <link>http://www.medworm.com/index.php?rid=5296442&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21971507%26dopt%3DAbstract</link>
            <description>Authors: Mustalahti E, Saloheimo M, Joensuu JJ
    Abstract
    Insufficient accumulation and the lack of efficient purification methods are the two major bottlenecks hindering the recombinant production of many proteins. Alternative production schemes are urgently needed for proteins that remain challenging to express and purify with conventional techniques. We have found that hydrophobin fusions targeted to endoplasmic reticulum (ER) can enhance the expression of target proteins simultaneously providing means for straightforward purification. Here we show that hydrophobin fusion technology induces formation of large protein bodies in the filamentous fungus Trichoderma reesei. The fusion protein remained soluble in the ER-derived protein bodies. A simple and scalable aqueous two-phase sys...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5296442</comments>
            <pubDate>Wed, 28 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5296442</guid>        </item>
        <item>
            <title>An evaluation of aerobic and anaerobic sludges as start-up material for microbial fuel cell systems.</title>
            <link>http://www.medworm.com/index.php?rid=5296444&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21968392%26dopt%3DAbstract</link>
            <description>Authors: Lobato J, Cañizares P, Fernández FJ, Rodrigo MA
    Abstract
    The operation of microbial fuel cells (MFCs) seeded with the same quantities of aerobic or anaerobic sludge has been compared. The two sludges consisted of mixed cultures obtained from the aerobic reactor and anaerobic digester, respectively, of a municipal Wastewater Treatment Plant (WWTP). Both the sludges were diluted with their sedimentation supernatant to avoid modifying their metabolism. The results show that the type of sludge has a major impact on the performance of the system. Seeding an MFC with anaerobic acclimated sludge leads to a more rapid start-up of electricity production and the absence of a lag period. In the MFC seeded with anaerobic sludge, the steady-state operation conditions were achieved in...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5296444</comments>
            <pubDate>Sat, 24 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5296444</guid>        </item>
        <item>
            <title>An improved system for the surface immobilisation of proteins on Bacillus thuringiensis vegetative cells and spores through a new spore cortex-lytic enzyme anchor.</title>
            <link>http://www.medworm.com/index.php?rid=5296443&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21968393%26dopt%3DAbstract</link>
            <description>Authors: Shao X, Ni H, Lu T, Jiang M, Li H, Huang X, Li L
    Abstract
    An improved surface-immobilisation system was engineered to target heterologous proteins onto vegetative cells and spores of Bacillus thuringiensis plasmid-free recipient strain BMB171. The sporulation-dependent spore cortex-lytic enzyme from B. thuringiensis YBT-1520, SceA, was expressed in vegetative cells and used as the surface anchoring motif. Green fluorescent protein (GFP) and a Bacillus endo-β-1,3-1,4-glucanase (BglS) were used as the fusion partners to test the binding efficiency and the functional activities of immobilised surface proteins. The surface localisation of the SceA-GFP fusion protein on vegetative cells and spores was confirmed by Western blot, immunofluorescence microscopy and flow cytometry....</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5296443</comments>
            <pubDate>Sat, 24 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5296443</guid>        </item>
        <item>
            <title>A simple method for extracting DNA from Cryptosporidium oocysts using the anionic surfactant LSS.</title>
            <link>http://www.medworm.com/index.php?rid=5246403&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21924387%26dopt%3DAbstract</link>
            <description>In this study, we discussed a simple method for detecting Cryptosporidium DNA with the anionic surfactant, n-lauroylsarcosine sodium salt (LSS) using the loop-mediated isothermal amplification (LAMP) to eliminate the need for the freeze-thaw method and the DNA extraction kits. As a result, Bst DNA polymerase was inhibited by 0.1% LSS but not 0.01% LSS and 5% Triton X-100 or Tween 20. Although DNA was extracted from the oocysts by incubating with 0.1% LSS at 90°C for 15min, Bst DNA polymerase was inhibited by 0.1% LSS. The inhibition by 0.1% LSS was suppressed by adding 5% of the nonionic surfactants, Triton X-100 or Tween 20. The concentration of LSS in a LAMP tube was 0.01% while that in an incubation tube was 0.1%, because LSS in an incubation tube was diluted by a factor of 10 at the D...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5246403</comments>
            <pubDate>Sat, 10 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5246403</guid>        </item>
        <item>
            <title>Analysis of PCBs degradation abilities of biphenyl dioxygenase derived from Enterobacter sp. LY402 by molecular simulation.</title>
            <link>http://www.medworm.com/index.php?rid=5246402&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21925295%26dopt%3DAbstract</link>
            <description>Authors: Cao YM, Xu L, Jia LY
    Abstract
    Enterobacter sp. LY402 is a bacterium isolated from polluted soil. It can efficiently degrade polychlorinated biphenyls (PCBs) under aerobic conditions. However, the degradation was limited when it comes to high chlorine or double para-substituted PCBs. Biphenyl dioxygenase (BDO) is the key enzyme in the PCBs biodegradation process. It has been confirmed that the α-subunit of the iron-sulfur protein of biphenyl 2,3-dioxygenase (BphA1) directly influenced catalytic activities and substrate specificity. To know the degradation characteristics of BDO to PCBs, we analyzed PCBs degradation abilities of BphA1 from Enterobacter sp. LY402 by experiment and molecular simulation. Firstly, the degradation experiment of PCBs was performed, and the degrad...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5246402</comments>
            <pubDate>Sat, 10 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5246402</guid>        </item>
        <item>
            <title>Biotransformation of furfural and 5-hydroxymethyl furfural (HMF) by Clostridium acetobutylicum ATCC 824 during butanol fermentation.</title>
            <link>http://www.medworm.com/index.php?rid=5246401&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21925629%26dopt%3DAbstract</link>
            <description>Authors: Zhang Y, Han B, Ezeji TC
    Abstract
    The ability of fermenting microorganisms to tolerate furan aldehyde inhibitors (furfural and 5-hydroxymethyl furfural (HMF)) will enhance efficient bioconversion of lignocellulosic biomass hydrolysates to fuels and chemicals. The effect of furfural and HMF on butanol production by Clostridium acetobutylicum 824 was investigated. Whereas specific growth rates, μ, of C. acetobutylicum in the presence of furfural and HMF were in the range of 15-85% and 23-78%, respectively, of the uninhibited Control, μ increased by 8-15% and 23-38% following exhaustion of furfural and HMF in the bioreactor. Using high performance liquid chromatography and spectrophotometric assays, batch fermentations revealed that furfural and HMF were converted to furfur...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5246401</comments>
            <pubDate>Sat, 10 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5246401</guid>        </item>
        <item>
            <title>Batch reactor performance for the enzymatic synthesis of cephalexin: influence of catalyst enzyme loading and particle size.</title>
            <link>http://www.medworm.com/index.php?rid=5246400&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21925630%26dopt%3DAbstract</link>
            <description>Authors: Valencia P, Flores S, Wilson L, Illanes A
    Abstract
    A mathematical model is presented for the kinetically controlled synthesis of cephalexin that describes the heterogeneous reaction-diffusion process involved in a batch reactor with glyoxyl-agarose immobilized penicillin acylase. The model is based on equations considering reaction and diffusion components. Reaction kinetics was considered according to the mechanism proposed by Schroën, while diffusion of the reacting species was described according to Fick's law. Intrinsic kinetic and diffusion parameters were experimentally determined in independent experiments. It was found that from the four kinetic constants, the one corresponding to the acyl-enzyme complex hydrolysis step had the greatest value, as previously report...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5246400</comments>
            <pubDate>Sat, 10 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5246400</guid>        </item>
        <item>
            <title>Decolourisation and detoxification in the fungal treatment of textile wastewaters from dyeing processes.</title>
            <link>http://www.medworm.com/index.php?rid=5218756&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21911089%26dopt%3DAbstract</link>
            <description>In this study a selected fungal strain, Bjerkandera adusta (Willdenow) P. Karsten MUT 3060, was tested in different culture conditions to assess its real potential for bioremediation of textile wastewaters in terms of both decolourisation and detoxification. The fungus efficiently decolourised (colour removal up to 96%) four simulated wastewaters that mimic the recalcitrance of real ones for pH values, concentration of dyes, additives and salts. In the culture condition with the lowest N content, the decolourisation was coupled with an important detoxification of two simulated effluents, underlining the important influence of the cultural medium composition not only on the degradation but also on the detoxification of industrial wastes. In the other cases, despite an extensive decolourisat...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5218756</comments>
            <pubDate>Mon, 05 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5218756</guid>        </item>
        <item>
            <title>Biotreatment of a gas-phase volatile mixture from fibreglass and composite manufacturing industries.</title>
            <link>http://www.medworm.com/index.php?rid=5218755&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21911090%26dopt%3DAbstract</link>
            <description>In this study, the performance of a steady-state biofilter inoculated with the fungus Sporothrix variecibatus was tested at different empty bed residence times (EBRTs), and at different inlet concentrations of ATS, corresponding to total pollutant loading rates ranging from 30 to 490gm(-3)hour(-1). Styrene was somewhat better removed (47-100%) in the biofilter than acetone (34-100%) and toluene (42-100%), with maximum elimination capacities (EC(max)) of 108, 72 and 144gm(-3)hour(-1), for ATS, respectively. Besides, it was observed that, although increasing the concentration of ATS decreased their removal, the presence of toluene also decreased the EC(max) of both acetone and toluene in the ternary mixture. During transient operations, the biofilter was subjected to intermittent shutdown an...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5218755</comments>
            <pubDate>Sat, 03 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5218755</guid>        </item>
        <item>
            <title>Visualising individual sequence-specific protein-DNA interactions in situ.</title>
            <link>http://www.medworm.com/index.php?rid=5218757&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21906700%26dopt%3DAbstract</link>
            <description>We present herein an approach to visualise individual PDIs within cells, based on the in situ proximity ligation assay (PLA). This assay, previously used for the detection of protein-protein interactions in situ, was adapted for analysis of target PDIs, using padlock probes to identify unique DNA sequences in complex genomes. As a proof-of-principle we detected histone H3 interacting with a 26bp consensus sequence of the Alu-repeat abundantly expressed in the human genome, but absent in mice. However, the mouse genome contains a highly similar sequence, providing a model system to analyse the selectivity of the developed methods. Although efficiency of detection currently is limiting, we conclude that in situ PLA can be used to achieve a highly selective analysis of PDIs in single cells.
 ...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5218757</comments>
            <pubDate>Wed, 31 Aug 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5218757</guid>        </item>
        <item>
            <title>On the trail to therapeutic antibodies.</title>
            <link>http://www.medworm.com/index.php?rid=5218758&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21896343%26dopt%3DAbstract</link>
            <description>Authors: Taussig MJ
    PMID: 21896343 [PubMed - as supplied by publisher] (Source: New Biotechnology)</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5218758</comments>
            <pubDate>Tue, 30 Aug 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5218758</guid>        </item>
        <item>
            <title>A novel halotolerant xylanase from marine isolate Bacillus subtilis cho40: gene cloning and sequencing.</title>
            <link>http://www.medworm.com/index.php?rid=5218759&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21890005%26dopt%3DAbstract</link>
            <description>We report here a novel halotolerant xylanase from marine bacterium Bacillus subtilis cho40 isolated from Chorao island of mandovi estuary Goa, India. Extracellular xylanase was produced by using agricultural residue such as wheat bran as carbon source under solid-state fermentation (SSF). The optimal pH and temperature of xylanase were reported to be 6.0 and 60°C, respectively. Xyn40 was highly salt-tolerant, and showed highest activity at 0.5M NaCl. Xylanase activity was greatly induced (140%) when pre-incubated with 0.5M NaCl for 4h. The xylanase gene, xyn40, from marine bacterium B. subtilis cho40 was cloned, and expressed in Escherichia coli. The xylanase gene was 645bp long and had a 215 amino acid ORF protein with a molecular mass of 22.9kDa. It had all features of xylanase enzyme a...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5218759</comments>
            <pubDate>Fri, 19 Aug 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5218759</guid>        </item>
        <item>
            <title>Overexpression and characterization of a novel transgalactosylic and hydrolytic β-galactosidase from a human isolate Bifidobacterium breve B24.</title>
            <link>http://www.medworm.com/index.php?rid=5218760&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21888996%26dopt%3DAbstract</link>
            <description>Authors: Yi SH, Alli I, Park KH, Lee B
    Abstract
    After the complete gene of a β-galactosidase from human isolate Bifidobacterium breve B24 was isolated by PCR and overexpressed in E. coli, the recombinant β-galactosidase was purified to homogeneity and characterized for the glycoside transferase (GT) and glycoside hydrolase (GH) activities on lactose. One complete ORF encoding 691 amino acids (2076bp) was the structural gene, LacA (galA) of the β-gal gene. The recombinant enzyme shown by activity staining and gel-filtration chromatography was composed of a homodimer of 75kDa with a total molecular mass of 150kDa. The K(m) value for lactose (95.58mM) was 52.5-fold higher than the corresponding K(m) values for the synthetic substrate ONPG (1.82mM). This enzyme with the optimum of p...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5218760</comments>
            <pubDate>Wed, 10 Aug 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5218760</guid>        </item>
        <item>
            <title>Antibody array analysis of labelled proteomes: how should we control specificity?</title>
            <link>http://www.medworm.com/index.php?rid=5141288&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21840428%26dopt%3DAbstract</link>
            <description>Authors: Holm A, Wu W, Lund-Johansen F
    Abstract
    Researchers who use protein binders in multiplexed assays can be divided into two camps. One believes that arrays with proteome-wide coverage will become a reality once we have developed binders for all proteins. The sceptics claim that detection with immobilized protein binders and sample labelling will not provide the required specificity. In this article, we review the evidence showing that antibody array analysis of labelled samples can provide meaningful data and discuss the issues raised by the sceptics. We argue that direct the evidence for monospecificity has yet to be published. This will require assays designed to resolve the proteins captured by each binder. One option is to combine array measurement with protein separation...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5141288</comments>
            <pubDate>Wed, 03 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5141288</guid>        </item>
        <item>
            <title>Efficient media for high menaquinone-7 production: response surface methodology approach.</title>
            <link>http://www.medworm.com/index.php?rid=5141289&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21839866%26dopt%3DAbstract</link>
            <description>Authors: Berenjian A, Mahanama R, Talbot A, Biffin R, Regtop H, Valtchev P, Kavanagh J, Dehghani F
    Abstract
    The aim of this study was to assess the effect of nutrients on the production of menaquinone-7 and determine the optimum conditions to achieve a high concentration of this product. Bacillus subtilis natto was fermented at 40°C for a period of six days. Design of experiments was used for screening the most effective nutrients, and central composite face design was employed for the optimization. The optimum media consisted of 5% (w/v) yeast extract; 18.9% (w/v) soy peptone; 5% (w/v) glycerol and 0.06% (w/v) K(2)HPO(4). The pH, bacterial growth, concentrations of amino acids, glycerol and menaquinone-7 were measured at the optimum fermentation media each day. Total free amino a...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5141289</comments>
            <pubDate>Tue, 02 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5141289</guid>        </item>
        <item>
            <title>Asymmetric reduction of a ketone by wet and lyophilized cells of Geotrichum candidum in organic solvents.</title>
            <link>http://www.medworm.com/index.php?rid=5141290&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21835274%26dopt%3DAbstract</link>
            <description>Authors: Bhattacharyya MS, Singh A, Banerjee UC
    Abstract
    Sixteen organic co-solvents were screened for stereoselective reduction of 1-acetonapthone in aqueous media by whole cells of Geotrichum candidum. Benzyl alcohol was found to be a good co-solvent as it afforded a high coversion and reduced deactivation of the cells. Half-lives of the wet and lyophilized whole cell biocatalysts in pure benzyl alcohol were 23.07 and 11.21 hours, respectively. The initial reaction rates at 30°C were 13.1 and 11.0μmol/min, respectively, for the wet and lyophilized cells. With optimized conditions in a reaction medium containing phosphate buffer and benzyl alcohol (1:1 by vol) with 230mM 1-acetonapthone, more than 98% and 81% conversion (ee &amp;gt;99%) was achieved in 5 hours with the wet and lyoph...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5141290</comments>
            <pubDate>Fri, 29 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5141290</guid>        </item>
        <item>
            <title>Highly efficient bioethanol production by a Saccharomyces cerevisiae strain with multiple stress tolerance to high temperature, acid and ethanol.</title>
            <link>http://www.medworm.com/index.php?rid=5141291&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21820088%26dopt%3DAbstract</link>
            <description>We describe here the breeding and performance of such a multiple-tolerant strain of Saccharomyces cerevisiae strain generated by a spore-to-cell hybridization technique without recombinant DNA technology. A heterothallic strain showing a high-temperature (41°C) tolerant (Htg(+)) phenotype, a derivative from a strain isolated from nature, was crossed with a homothallic strain displaying high-ethanol productivity (Hep(+)), a stock culture at the Thailand Institute of Scientific and Technological Research. The resultant hybrid TJ14 displayed ability to rapidly utilize glucose, and produced ethanol (46.6g/l) from 10% glucose fermentation medium at high temperature (41°C). Not only ethanol productivity at 41°C but also acid tolerance (Acd(+)) was improved in TJ14 as compared with its parenta...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5141291</comments>
            <pubDate>Mon, 25 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5141291</guid>        </item>
        <item>
            <title>Selective inactivation of M-MuLV RT RNase H activity by site-directed PEGylation: an improved ability to synthesize long cDNA molecules.</title>
            <link>http://www.medworm.com/index.php?rid=5097793&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21807127%26dopt%3DAbstract</link>
            <description>Authors: Radzvilavicius T, Lagunavicius A
    Moloney murine leukemia virus reverse transcriptase (M-MuLV RT) is a domain structured enzyme that has the N-terminally located DNA polymerization activity and C-terminally located RNase H activity, which interferes with the efficient synthesis of long cDNA molecules. Here we present the PEGylation as a tool for engineering the M-MuLV RT derivative deficient in RNase H activity. We demonstrate that site-directed chemical modification (SDCM) of the RNase H domain by selectively PEGylating C635, one of the eight cysteine residues present in the reverse transcriptase (RT), specifically inactivated its ribonucleolytic activity. As a consequence, the efficiency of long cDNA molecules synthesis by modified enzyme was greatly increased.
    PMID: 2180...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5097793</comments>
            <pubDate>Fri, 22 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5097793</guid>        </item>
        <item>
            <title>Coupling two sizes of CSTR-type bioreactors for sequential lactic acid and xylitol production from hemicellulosic hydrolysates of vineshoot trimmings.</title>
            <link>http://www.medworm.com/index.php?rid=5097794&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21807126%26dopt%3DAbstract</link>
            <description>This study develops a system for the efficient valorisation of hemicellulosic hydrolysates of vineshoot trimmings. By connecting two reactors of 2L and 10L, operational conditions were set up for the sequential production of lactic acid and xylitol in continuous fermentation, considering the dependence of the main metabolites and fermentation parameters on the dilution rate. In the first bioreactor, Lactobacillus rhamnosus consumed all the glucose to produce lactic acid at 31.5°C, with 150rpm and 1L of working volume as the optimal conditions. The residual sugars were employed for the xylose to xylitol bioconversion by Debaryomyces hansenii in the second bioreactor at 30°C, 250rpm and an air-flow rate of 2Lmin(-1). Several steady states were reached at flow rates (F) in the range of 0.54...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5097794</comments>
            <pubDate>Thu, 21 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5097794</guid>        </item>
        <item>
            <title>Neural network models for biological waste-gas treatment systems.</title>
            <link>http://www.medworm.com/index.php?rid=5097795&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21784184%26dopt%3DAbstract</link>
            <description>Authors: Rene ER, Estefanía López M, Veiga MC, Kennes C
    This paper outlines the procedure for developing artificial neural network (ANN) based models for three bioreactor configurations used for waste-gas treatment. The three bioreactor configurations chosen for this modelling work were: biofilter (BF), continuous stirred tank bioreactor (CSTB) and monolith bioreactor (MB). Using styrene as the model pollutant, this paper also serves as a general database of information pertaining to the bioreactor operation and important factors affecting gas-phase styrene removal in these biological systems. Biological waste-gas treatment systems are considered to be both advantageous and economically effective in treating a stream of polluted air containing low to moderate concentrations of the ta...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5097795</comments>
            <pubDate>Sun, 17 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5097795</guid>        </item>
        <item>
            <title>Influence of temperature, pH and dissolved oxygen concentration on enhanced biological phosphorus removal under strictly aerobic conditions.</title>
            <link>http://www.medworm.com/index.php?rid=5006173&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21718809%26dopt%3DAbstract</link>
            <description>Authors: Nittami T, Oi H, Matsumoto K, Seviour RJ
    Previous research has suggested that enhanced biological phosphorus removal (EBPR) from wastewater can be achieved under continuous aerobic conditions over the short term. However, little is known how environmental conditions might affect aerobic EBPR performance. Consequently we have investigated the impact of temperature, pH and dissolved oxygen (DO) concentrations on EBPR performance under strictly aerobic conditions. A sequencing batch reactor (SBR) was operated for 108 days on a six-hour cycle (four cycles a day). The SBR ran under alternating anaerobic-aerobic conditions as standard and then operated under strictly aerobic conditions for one cycle every three or four days. SBR operational temperature (10, 15, 20, 25 and 30°C), pH...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5006173</comments>
            <pubDate>Sun, 26 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5006173</guid>        </item>
        <item>
            <title>Effect of 2,4,6-trichlorophenol on the microbial activity of adapted anaerobic granular sludge bioaugmented with Desulfitobacterium strains.</title>
            <link>http://www.medworm.com/index.php?rid=5006166&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21718810%26dopt%3DAbstract</link>
            <description>Authors: Puyol D, Mohedano AF, Rodriguez JJ, Sanz JL
    The anaerobic degradation of 2,4,6-trichlorophenol (246TCP) has been studied in batch experiments. Granular sludges previously acclimated to 2,4-dichlorophenol (24DCP) and then adapted to at a load of 330μM 246TCPd(-1) in two expanded granular sludge bed (EGSB) reactors were used. One of the reactors had been bioaugmented with Desulfitobacterium strains whereas the other served as control. 246TCP was tested at concentrations between 250 and 760μM. The study focused on the fate of both fermentation products and chlorophenols derived from dechlorination of 246TCP. This compound mainly affected the biodegradation of acetate and propionate, which were inhibited at 246TCP concentrations above 380μM. Lactate and ethanol were also accumu...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5006166</comments>
            <pubDate>Sun, 26 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5006166</guid>        </item>
        <item>
            <title>Biotransformation of the organochlorine pesticide trans-chlordane by wood-rot fungi.</title>
            <link>http://www.medworm.com/index.php?rid=5006163&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21718811%26dopt%3DAbstract</link>
            <description>In this study, trans-chlordane was metabolized with the wood-rot fungi species Phlebia lindtneri, Phlebia brevispora and Phlebia aurea, which are capable of degrading polychlorinated dibenzo-p-dioxin and heptachlor epoxide. At the end of 42 days of incubation, over 50% of trans-chlordane was degraded by the fungal treatments in pure cultures. These fungi transformed trans-chlordane to at least eleven metabolites including a large amount of hydroxylated products such as 3-hydroxychlordane, chlordene chlorohydrin, heptachlor diol, monohydroxychlordene and dihydroxychlordene. P. lindtneri particularly can metabolize oxychlordane, a recalcitrant epoxide product of chlordane, into a hydroxylated product through substitution of chlorine atom by hydroxyl group. The present results suggest that hy...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5006163</comments>
            <pubDate>Sun, 26 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5006163</guid>        </item>
        <item>
            <title>Production of high amounts of 3-hydroxypropionaldehyde from glycerol by Lactobacillus reuteri with strongly increased biocatalyst lifetime and productivity.</title>
            <link>http://www.medworm.com/index.php?rid=5006160&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21729774%26dopt%3DAbstract</link>
            <description>Authors: Krauter H, Willke T, Vorlop KD
    3-Hydroxypropionaldehyde (3HPA) is a promising versatile substance derived from the renewable feedstock glycerol. It is a product of glycerol metabolism in Lactobacillus reuteri. Because of toxic effects, the biotechnological production is poor. In this work the biocatalyst lifetime and product formation could be drastically increased. In the established two-step process already applied, cells are grown in the first step under anaerobic conditions, and in the second step the immobilised or suspended biocatalyst is used for 3HPA-production under strict anaerobic conditions. In the first step it was possible to reach a biomass concentration of 5.5g CDW/L (OD(600)≈23.4). In the second step, normally, 3HPA accumulates to a toxic concentration and t...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5006160</comments>
            <pubDate>Fri, 24 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5006160</guid>        </item>
        <item>
            <title>Granular activated carbon based microbial fuel cell for simultaneous decolorization of real dye wastewater and electricity generation.</title>
            <link>http://www.medworm.com/index.php?rid=5006162&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21718812%26dopt%3DAbstract</link>
            <description>In this study, a granular activated carbon based microbial fuel cell (GACB-MFC) was used without using any expensive materials like Nafion membrane and platinum catalyst for simultaneous decolorization of real dye wastewater and bioelectricity generation. After 48hours of GACB-MFC operation, 73% color was removed at anode and 77% color was removed at cathode. COD removal was 71% at the anode and 76% at the cathode after 48hours. Toxicity measurements showed that cathode effluent was almost nontoxic after 24hours. The anode effluent was threefold less toxic compared to original dye wastewater after 48hours. The GACB-MFC produced a power density of 1.7W/m(3) with an open circuit voltage 0.45V. One of the advantages of the GACB-MFC system is that pH was automatically adjusted from 12.4 to 7.2...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5006162</comments>
            <pubDate>Mon, 20 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5006162</guid>        </item>
        <item>
            <title>Optimization of Brassica napus (canola) explant regeneration for genetic transformation.</title>
            <link>http://www.medworm.com/index.php?rid=5006161&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21722759%26dopt%3DAbstract</link>
            <description>Authors: Maheshwari P, Selvaraj G, Kovalchuk I
    Brassica napus (canola) is the second largest oilseed crop in the world. It is among the first crops to be genetically transformed, and genetically modified cultivars are in commercial production at very significant levels. Despite the early lead with respect to transgenesis, there remain cultivars that are recalcitrant to transformation. To address this, we have conducted an elaborate investigation of the conditions for regenerating shoots from hypocotyl explants from four genetic lines: Invigor 5020, Westar and Topas as well as a microspore culture derived line of Topas (Line 4079). We analyzed the effect of hormonal combinations in regeneration medium, donor plant age and explant type on the regeneration capacity of these plants. The an...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5006161</comments>
            <pubDate>Mon, 20 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5006161</guid>        </item>
        <item>
            <title>Strategy for purification of aggregation prone β-glucosidases from the cell wall of yeast: a preparative scale approach.</title>
            <link>http://www.medworm.com/index.php?rid=5006174&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21704202%26dopt%3DAbstract</link>
            <description>We report here a preparative method for purification of large quantities of two closely related cell bound β-glucosidases from Pichia etchellsii that belong to Family 3 glycosylhydrolases. A combination of ion-exchange and gel filtration chromatography was used to process milligram quantities of protein with recoveries of up to 53%. A simple affinity based separation resulted in resolution of the two proteins, BGL I and BGL II with high recovery and high specific activities of 74IU/mg and 32IU/mg protein respectively. Peptide sequences of BGL II indicated it to be a novel member of Family 3. Methods reported here present a successful strategy for obtaining large quantities of these enzymes.
    PMID: 21704202 [PubMed - as supplied by publisher] (Source: New Biotechnology)</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5006174</comments>
            <pubDate>Tue, 14 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5006174</guid>        </item>
        <item>
            <title>The processive endoglucanase EngZ is active in crystalline cellulose degradation as a cellulosomal subunit of Clostridium cellulovorans.</title>
            <link>http://www.medworm.com/index.php?rid=4959073&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21689799%26dopt%3DAbstract</link>
            <description>In conclusion, EngZ was highly expressed in cellulolytic systems and demonstrated processive endoglucanase activity, suggesting that it plays a major role in the hydrolysis of crystalline cellulose and acts as a cellulosomal enzyme in C. cellulovorans.
    PMID: 21689799 [PubMed - as supplied by publisher] (Source: New Biotechnology)</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4959073</comments>
            <pubDate>Sun, 12 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4959073</guid>        </item>
        <item>
            <title>Pseudomonas resinovorans SPR1, a newly isolated strain with potential of transforming eugenol to vanillin and vanillic acid.</title>
            <link>http://www.medworm.com/index.php?rid=4959072&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21689800%26dopt%3DAbstract</link>
            <description>In this study a novel strain was isolated with the capability to grow on eugenol as a source of carbon and energy. This strain was identified as Pseudomonas resinovorans (GenBank accession no. HQ198585) based on phenotypic characterization and phylogenetic analysis of 16S rDNA gene. The intermediates coniferyl alcohol, coniferyl aldehyde, ferulic acid, vanillin and vanillic acid were detected in the culture supernatant during eugenol biotransformation with this strain. The products were confirmed by thin layer chromatography (TLC), high performance liquid chromatography (HPLC) and spectral data achieved from UV-vis, FTIR and mass spectroscopy. Using eugenol as substrate and resting cells of P. resinovorans SPR1, which were harvested at the end of the exponential growth phase, without furth...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4959072</comments>
            <pubDate>Sun, 12 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4959072</guid>        </item>
        <item>
            <title>Separation of clavulanic acid from fermented broth of amino acids by an aqueous two-phase system and ion-exchange adsorption.</title>
            <link>http://www.medworm.com/index.php?rid=4959076&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21683811%26dopt%3DAbstract</link>
            <description>Authors: da Silva CS, Cuel MF, Barreto VO, Kwong WH, Hokka CO, Barboza M
    The clavulanic acid is a substance which inhibits the β-lactamases used with penicillins for therapeutic treatment. After the fermentation, by-products of low molecular weight such as amino acids lysine, histidine, proline and tyrosine are present in the fermented broth. To remove these impurities the techniques of extraction by an aqueous two-phase system of 17% polyethylene glycol molecular weight 600 and 15% potassium phosphate were used for a partial purification. A subsequent ion-exchange adsorption was used for the recuperation of the clavulanic acid of the top phase and purification getting a concentration factor of 2 and purification of 100% in relation to the amino acids lysine, histidine, proline and ty...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4959076</comments>
            <pubDate>Sat, 11 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4959076</guid>        </item>
        <item>
            <title>Fungi isolated from olive ecosystems and screening of their potential biotechnological use.</title>
            <link>http://www.medworm.com/index.php?rid=4959075&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21689797%26dopt%3DAbstract</link>
            <description>This study investigated the fungi diversity of fresh olive (Olea europaea L.) fruits, olive paste (crushed olives) and olive pomace (solid waste) and screened and quantified enzymatic activities with biotechnological applications. Fungi were randomly isolated from olive cultivars from Castilla La Mancha region (Spain). Identification included comparison of their polymerase chain reaction (PCR) amplicons of the ITS1-5.8S-ITS2 ribosomal DNA region, followed by nucleotide sequence analysis. Fourteen different species with DNA sequences of different similarities were identified, belonging to seven different genera (Aspergillus, Penicillium, Rhizomucor, Mucor, Rhizopus, Lichtheimia and Galactomyces). Aspergillus fumigatus, followed by Galactomyces geotrichum, Penicillium commune and Rhizomucor ...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4959075</comments>
            <pubDate>Sat, 11 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4959075</guid>        </item>
        <item>
            <title>CTAB, Triton X-100 and freezing-thawing treatments of Candida guilliermondii: Effects on permeability and accessibility of the glucose-6-phosphate dehydrogenase, xylose reductase and xylitol dehydrogenase enzymes.</title>
            <link>http://www.medworm.com/index.php?rid=4959079&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21664992%26dopt%3DAbstract</link>
            <description>Authors: Cortez DV, Roberto IC
    Cells of Candida guilliermondii (ATCC 201935) were permeabilised with surfactant treatment (CTAB or Triton X-100) or a freezing-thawing procedure. Treatments were monitored by in situ activities of the key enzymes involved in xylose metabolism, that is, glucose-6-phosphate dehydrogenase (G6PD), xylose reductase (XR) and xylitol dehydrogenase (XD). The permeabilising ability of the surfactants was dependent on its concentration and incubation time. The optimum operation conditions for the permeabilisation of C. guilliermondii with surfactants were 0.41mM (CTAB) or 2.78mM (Triton X-100), 30°C, and pH 7 at 200rpm for 50min. The maximum permeabilisation measured in terms of the in situ G6PD activity observed was, in order, as follows: CTAB (122.4±15.7U/g(ce...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4959079</comments>
            <pubDate>Tue, 31 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4959079</guid>        </item>
        <item>
            <title>The effect of the symbiosis between Tagetes erecta L. (marigold) and Glomus intraradices in the uptake of Copper(II) and its implications for phytoremediation.</title>
            <link>http://www.medworm.com/index.php?rid=4959078&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21664993%26dopt%3DAbstract</link>
            <description>Authors: Castillo OS, Dasgupta-Schubert N, Alvarado CJ, Zaragoza EM, Villegas HJ
    Phytoremediation is an environmental biotechnology that seeks to remediate pollution caused by bioaccumulative toxins like copper (Cu). Symbiotic mycorrhizal associations can increase the uptake and delivery of low mobility nutrients and micronutrients to the host plant because they solubilize these substances and increase their catchment area. To analyze the effect of mycorrhizae on the phytoaccumulation of Cu, we studied their ability to solubilize Cu(II) and enhance its absorption by the plant Tagetes erecta L. colonized with the arbuscular mycorrhizal fungus Glomus intraradices. Plants were grown for nine weeks in a growth chamber under controlled conditions of temperature, relative humidity and photop...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4959078</comments>
            <pubDate>Tue, 31 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4959078</guid>        </item>
        <item>
            <title>Recombinant protein purification using complementary peptides as affinity tags.</title>
            <link>http://www.medworm.com/index.php?rid=4959077&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21664994%26dopt%3DAbstract</link>
            <description>Authors: Martínez-Ceron MC, Targovnik AM, Urtasun N, Cascone O, Miranda MV, Camperi SA
    Affinity tags have become highly popular tools for purifying recombinant proteins from crude extracts by affinity chromatography. Besides, short peptides are excellent ligands for affinity chromatography, as they are not likely to cause an immune response in case of leakage into the product, they are more stable than antibodies to elution and cleaning conditions and they usually have very acceptable selectivity. Hydropathically complementary peptides designed de novo show enough selectivity to be used successfully as peptide ligands for protein purification from crude extracts. Recognition specificity and selectivity in the interaction between the complementary peptide pair His-Leu-Leu-Phe-Pro-Ile-I...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4959077</comments>
            <pubDate>Tue, 31 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4959077</guid>        </item>
        <item>
            <title>A comparative study of solvent-assisted pretreatment of biodiesel derived crude glycerol on growth and 1,3-propanediol production from Citrobacter freundii.</title>
            <link>http://www.medworm.com/index.php?rid=4959074&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21689798%26dopt%3DAbstract</link>
            <description>The objective of the present investigation was to evaluate the impact of biodiesel-derived crude glycerol upon microbial growth and production of 1,3-propanediol by Citrobacter freundii. Five different grades of crude glycerols (obtained from biodiesel preparation using jatropha, soybean, sunflower, rice bran and linseed oils) were used. Crude glycerol caused significant inhibition of microbial growth and subsequently 1,3-propanediol production as compared to pure glycerol. Therefore, a process was developed for the treatment of crude glycerol using solvents before fermentation wherein four different non-polar solvents were examined yielding different grades of pretreated glycerol. Subsequently, the potential toxic effects of pretreated glycerol on the growth and 1,3-propanediol production...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4959074</comments>
            <pubDate>Tue, 31 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4959074</guid>        </item>
        <item>
            <title>Bacterial tyrosinases: old enzymes with new relevance to biotechnology.</title>
            <link>http://www.medworm.com/index.php?rid=4959080&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21664502%26dopt%3DAbstract</link>
            <description>This article will summarise the reports on the biotechnological applications of bacterial tyrosinases as well as the current information available on the different types of this enzyme.
    PMID: 21664502 [PubMed - as supplied by publisher] (Source: New Biotechnology)</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4959080</comments>
            <pubDate>Mon, 30 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4959080</guid>        </item>
        <item>
            <title>Co-cultivation of mutant Penicillium oxalicum SAU(E)-3.510 and Pleurotus ostreatus for simultaneous biosynthesis of xylanase and laccase under solid-state fermentation.</title>
            <link>http://www.medworm.com/index.php?rid=4911044&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21642024%26dopt%3DAbstract</link>
            <description>Authors: Dwivedi P, Vivekanand V, Pareek N, Sharma A, Singh RP
    Co-cultivation of mutant Penicillium oxalicum SAU(E)-3.510 and Pleurotus ostreatus MTCC 1804 was evaluated for the production of xylanase-laccase mixture under solid-state fermentation (SSF) condition. Growth compatibility between mutant P. oxalicum SAU(E)-3.510 and white rot fungi (P. ostreatus MTCC 1804, Trametes hirsuta MTCC 136 and Pycnoporus sp. MTCC 137) was analyzed by growing them on potato dextrose agar plate. Extracellular enzyme activities were determined spectrophotometrically. Under derived conditions, paired culturing of mutant P. oxalicum SAU(E)-3.510 and P. ostreatus MTCC 1804 resulted in 58% and 33% higher levels of xylanase and laccase production, respectively. A combination of sugarcane bagasse and black ...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4911044</comments>
            <pubDate>Thu, 26 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4911044</guid>        </item>
        <item>
            <title>Efficient shoot regeneration from internodal explants of Populus angustifolia, Populus balsamifera and Populus deltoids.</title>
            <link>http://www.medworm.com/index.php?rid=4911045&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21640207%26dopt%3DAbstract</link>
            <description>Authors: Maheshwari P, Kovalchuk I
    In the present study, interactions between the duration of treatment with auxin and different cytokinins and their effect on shoot regeneration were evaluated with the aim to establish a rapid and efficient in vitro regeneration method applicable to a variety of Populus species. Three different species, Populus angustifolia, P. balsamifera, and P. deltoids, were chosen for that purpose. We were successful in regenerating plantlets from stem and petiole explants from all three chosen species using a four-step simple procedure. The first step was callus induction when the explants were exposed to an auxin-rich medium for 0-20 days. During the second step, they were transferred onto a cytokinin-rich medium for shoot bud induction. In the third step, the ...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4911045</comments>
            <pubDate>Tue, 24 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4911045</guid>        </item>
        <item>
            <title>Expression and characterization of an extremely thermostable β-glycosidase (mannosidase) from the hyperthermophilic archaeon Pyrococcus furiosus DSM3638.</title>
            <link>http://www.medworm.com/index.php?rid=4911047&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21624508%26dopt%3DAbstract</link>
            <description>Authors: Park SH, Park KH, Oh BC, Alli I, Lee BH
    Genomic analysis of the hyperthermophilic archaeon Pyrococcus furiosus revealed the presence of an open reading frame (ORF PF0356) similar to the enzymes in glycoside hydrolase family 1. This β-glycosidase, designated PFTG (P. furiosus thermostable glycosidase), was cloned and expressed in Escherichia coli. The expressed enzyme was purified by heat treatment and Ni-NTA affinity chromatography. The gene was composed of 1452bp encoding 483 amino acids for a protein with a predicted molecular mass of 56,326Da. The temperature and pH optima were 100°C and 5.0 in sodium citrate buffer, respectively. The substrate specificity of PFTG suggests that it possesses characteristics of both β-galactosidase and β-mannosidase activities. However, t...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4911047</comments>
            <pubDate>Sun, 22 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4911047</guid>        </item>
        <item>
            <title>Hepatoprotection of quercetin against oxidative stress by induction of metallothionein expression through activating MAPK and PI3K pathways and enhancing Nrf2 DNA-binding activity.</title>
            <link>http://www.medworm.com/index.php?rid=4911046&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21624509%26dopt%3DAbstract</link>
            <description>Authors: Weng CJ, Chen MJ, Yeh CT, Yen GC
    Flavonoids are natural phenolic substances widely found in fruit, vegetables, grains, and wine. Most of these compounds exert health-promoting effects seem to attribute to their antioxidant activity. Metallothioneins (MT) has been suggested to protect against acute heavy metal toxicity in the liver, and the proteins of MT can be induced by various stimuli including antioxidant. Measuring the induction of MT genes may provide an efficient approach to understand the chemopreventive mechanisms of flavonoids. The antioxidant activity of eight flavonoids was determined by TEAC and ORAC assays and their effects on MT protein were also measured. HepG2 cells were employed to explore the mechanisms underlying flavonoid-induced MT induction. Statistical ...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4911046</comments>
            <pubDate>Sun, 22 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4911046</guid>        </item>
        <item>
            <title>Effects of phospholipids on the antioxidant activity of α-tocopherol in the singlet oxygen oxidation of canola oil.</title>
            <link>http://www.medworm.com/index.php?rid=4911048&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21621019%26dopt%3DAbstract</link>
            <description>This study evaluated the effects of phosphatidylcholine (PC) or phosphatidylethanolamine (PE) on the antioxidative activity of α-tocopherol during oxidation of canola oil by singlet oxygen at 10°C for seven hours. Singlet oxygen was produced by chlorophyll b (4ppm) under 1700lux. The oxidation of oil was evaluated by headspace oxygen consumption by gas chromatography and peroxide values (POVs). Concentrations of PC, PE, chlorophyll, and α-tocopherol were determined by HPLC. PC and PE protected chlorophyll from degradation, but they accelerated the degradation of α-tocopherol under singlet oxygen. Contents of PC and PE did not change for seven hours under singlet oxygen. α-Tocopherol significantly lowered POV and headspace oxygen consumption of canola oil under singlet oxygen, and its ...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4911048</comments>
            <pubDate>Wed, 18 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4911048</guid>        </item>
        <item>
            <title>Bio-generated metal binding polysaccharides as catalysts for synthetic applications and organic pollutant transformations.</title>
            <link>http://www.medworm.com/index.php?rid=4911049&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21616180%26dopt%3DAbstract</link>
            <description>Authors: Baldi F, Marchetto D, Paganelli S, Piccolo O
    Iron and palladium binding an exopolysaccharide (EPS) were obtained and purified from cultures of bacterial cells of Klebsiella oxytoca BAS-10. The strain BAS-10 was able to grow under anaerobic conditions with Fe(III)-citrate as energy and carbon source, producing Fe(III)-EPS that was extracted and used as catalyst in the oxidation reaction of phenol with H(2)O(2). The same bacterial strain was cultivated anaerobically with Na-citrate and Pd(2)(NO)(3) was added during the exponential growth to afford a Pd-EPS, named Bio-Pd (A), that, after isolation and purification, was used as catalyst in the reductive dehalogenation of chlorobenzene as model reaction. For comparison other two palladium binding polysaccharides were prepared: (a) ...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4911049</comments>
            <pubDate>Mon, 16 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4911049</guid>        </item>
        <item>
            <title>An acetylcholinesterase biosensor for determination of low concentrations of Paraoxon and Dichlorvos.</title>
            <link>http://www.medworm.com/index.php?rid=4860141&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21600321%26dopt%3DAbstract</link>
            <description>Authors: Di Tuoro D, Portaccio M, Lepore M, Arduini F, Moscone D, Bencivenga U, Mita DG
    The characterization of an economic and ease-to-use carbon paste acetylcholinesterase (AChE) based biosensor to determine the concentration of pesticides Paraoxon and Dichlorvos is discussed. AChE hydrolyses acetylthiocholine (ATCh) in thiocoline (TC) and acetic acid (AA). When AChE is immobilized into a paste carbon working electrode kept at +410mV vs. Ag/AgCl electrode, the enzyme reaction rate using acetylthiocholine chloride (ATCl) as substrate is monitored as a current intensity. Because Paraoxon and Dichlorvos inhibit the AChE reaction, the decrease of the current intensity, at fixed ATCl concentration, is a measure of their concentration. Linear calibration curves for Paraoxon and Dichlorvos ...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4860141</comments>
            <pubDate>Sat, 07 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4860141</guid>        </item>
        <item>
            <title>Sequential application of electron donors and humic acids for the anaerobic bioremediation of chlorinated aliphatic hydrocarbons.</title>
            <link>http://www.medworm.com/index.php?rid=4860140&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21600322%26dopt%3DAbstract</link>
            <description>Authors: Scherr KE, Nahold MM, Lantschbauer W, Loibner AP
    In situ anaerobic bioremediation of chlorinated solvents such as perchloroethene (PCE) frequently faces the problem of accumulating toxic, lower chlorinated compounds such as dichloroethene (cis-DCE) and vinyl chloride (VC). In the present study, the efficacy of the sequential application of electron donors, supporting reductive dechlorination, and of humic acids, acting as extracellular electron shuttles facilitating the anaerobic oxidation of recalcitrant intermediates, was explored in microcosm studies. Upon one initial dose of lactose, supplied in a 1000-fold superstoichiometric electron equivalent ratio, PCE was completely converted into cis-DCE within 35days. Repeated electron donor additions did not entail exhaustive cis-...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4860140</comments>
            <pubDate>Sat, 07 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4860140</guid>        </item>
        <item>
            <title>Sequencing batch biofilter granular reactor for textile wastewater treatment.</title>
            <link>http://www.medworm.com/index.php?rid=4860143&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21558025%26dopt%3DAbstract</link>
            <description>Authors: Lotito AM, Di Iaconi C, Fratino U, Mancini A, Bergna G
    Textile wastewater is difficult to treat as it usually contains considerable amounts of different pollutants, which are often recalcitrant, toxic and inhibitory. Therefore, complex treatment schemes based on the sequence of various steps are usually required for an effective treatment. This explains why textile effluents are often treated in centralized plants and sometimes mixed with municipal wastewater. The adoption of new technologies for on-site treatment, instead, would be optimal, deeply reducing treatment costs. An innovative technology exhibiting several characteristics appropriate for the attainment of such a goal is sequencing batch biofilter granular reactor (SBBGR). To assess the suitability of this technology...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4860143</comments>
            <pubDate>Fri, 29 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4860143</guid>        </item>
        <item>
            <title>Bioflocculation of microalgae and bacteria combined with flue gas to improve sewage treatment.</title>
            <link>http://www.medworm.com/index.php?rid=4860142&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21565287%26dopt%3DAbstract</link>
            <description>Authors: Van Den Hende S, Vervaeren H, Desmet S, Boon N
    Although microalgae are promising for a cradle-to-cradle design approach of sewage treatment, their application is hampered by high harvesting costs and low C:N ratios of sewage. Therefore, the potential of microalgal bacterial flocs (MaB-flocs) was investigated for the secondary treatment of sewage supplemented with different flue gas flow rates (FGFRs) from a coal power plant. Effluent (N, P, turbidity and pH) and off gas discharge levels (NO(x), SO(x)) met the European discharge limits with a hydraulic retention time of only 0.67 days and an FGFR of 0.6Lh(-1) (0.0025vvm). This FGFR provided sufficient carbon and resulted in removal efficiencies of 48±7% CO(2), 87±5% NO(x) and 99±1% SO(2). MaB-flocs settled fast reaching up t...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4860142</comments>
            <pubDate>Fri, 29 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4860142</guid>        </item>
        <item>
            <title>An atypical HLH protein OsLF in rice regulates flowering time and interacts with OsPIL13 and OsPIL15.</title>
            <link>http://www.medworm.com/index.php?rid=4804725&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21549224%26dopt%3DAbstract</link>
            <description>In this study, we isolated the OsLF gene by its association with the T-DNA insertion in the rice late flowering mutant named A654. The OsLF gene encodes an atypical HLH protein composed of 419 amino acids (aa). Overexpression of the OsLF gene in wild type rice recapitulated the late flowering phenotype of A654, indicating that the OsLF gene negatively regulates flowering. Flowering genes downstream of OsPRR1 such as OsGI and Hd1 were down regulated in the A654 mutant. Yeast two hybrid and colocalization assays revealed that OsLF interacts strongly with OsPIL13 and OsPIL15 that are potentially involved in light signaling. In addition, OsPIL13 and OsPIL15 colocalize with OsPRR1, an ortholog of the Arabidopsis APRR1 gene that controls photoperiodic flowering response through clock function. T...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4804725</comments>
            <pubDate>Tue, 26 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4804725</guid>        </item>
        <item>
            <title>Production and properties of two collagenases from bacteria and their application for collagen extraction.</title>
            <link>http://www.medworm.com/index.php?rid=4804724&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21549225%26dopt%3DAbstract</link>
            <description>Authors: Suphatharaprateep W, Cheirsilp B, Jongjareonrak A
    Two collagenolytic protease (collagenase) producing bacteria, a Gram positive Bacillus cereus CNA1 and a Gram negative Klebsiella pneumoniae CNL3, were isolated under alkaline and acidic conditions, respectively. The production of collagenase by these two bacteria was optimized. Glycerol was the suitable carbon source for collagenase production by both strains. The optimal initial pH values for collagenase production by CNA1 and CNL3 were 7.5 and 6.0, respectively, and the optimal temperature was 37°C for both strains. The maximum activity of the partially purified collagenase from CNA1 was at pH 7.0 and 45°C. Its pH and thermal stability were in the range of 6-8 and below 40°C, respectively. The maximum activity of the part...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4804724</comments>
            <pubDate>Tue, 26 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4804724</guid>        </item>
        <item>
            <title>Lipase from marine Aspergillus awamori BTMFW032: Production, partial purification and application in oil effluent treatment.</title>
            <link>http://www.medworm.com/index.php?rid=4804723&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21549226%26dopt%3DAbstract</link>
            <description>In this study, medium for lipase production under submerged fermentation was optimized statistically employing response surface method toward maximal enzyme production. Medium with soyabean meal-0.77% (w/v); (NH(4))(2)SO(4)-0.1m; KH(2)PO(4)-0.05m; rice bran oil-2% (v/v); CaCl(2)-0.05m; PEG 6000-0.05% (w/v); and NaCl-1% (w/v); and inoculum-1% (v/v); pH 3.0; incubation temperature 35°C and incubation period-five days were identified as optimal conditions for maximal lipase production by statistical modeling. The time course experiment under optimized condition, after statistical modeling, indicated that enzyme production commenced after 36hours of incubation and reached a maximum after 96hours (495.0U/ml), whereas maximal specific activity of enzyme was recorded at 108hours (1164.63U/mg pro...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4804723</comments>
            <pubDate>Tue, 26 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4804723</guid>        </item>
        <item>
            <title>lux-Marking and application of carbofuran degrader Burkholderia cepacia PCL3.</title>
            <link>http://www.medworm.com/index.php?rid=4804722&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21549227%26dopt%3DAbstract</link>
            <description>Authors: Plangklang P, Reugnsang A
    A luxAB-mutant of the carbofuran degrading bacterium Burkholderia cepacia PCL3 was successfully constructed with the capability to emit a luminescence signal of 1.6×10(-3)RLUcfu(-1). The mutant has a growth pattern and carbofuran degradation ability similar to PCL3 wild-type. The luminescent emission by PCL3:luxAB1 directly correlated with the metabolic activity of the cells. The optimal pH, temperature and n-decanal concentration for luminescence emission are 7.0, 35°C and 0.01%, respectively. PCL3:luxAB1 was used to assess the toxicity of carbofuran and carbofuran phenol in basal salt medium (BSM) in which the different sensitivity of the cells is dependent on the biomass concentration. With the luciferase system, the degradative fraction of the a...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4804722</comments>
            <pubDate>Tue, 26 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4804722</guid>        </item>
        <item>
            <title>Characterization of a newly isolated strain Rhodococcus erythropolis ZJB-09149 transforming 2-chloro-3-cyanopyridine to 2-chloronicotinic acid.</title>
            <link>http://www.medworm.com/index.php?rid=4804721&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21549865%26dopt%3DAbstract</link>
            <description>This study revealed that the nitrile hydratase (NHase) and amidase expressed in R. erythropolis ZJB-09149 are responsible for the conversion of 2-chloro-3-cyanopyridine. This is the first time to report on the biotransformation preparation of 2-chloronicotinic acid.
    PMID: 21549865 [PubMed - as supplied by publisher] (Source: New Biotechnology)</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4804721</comments>
            <pubDate>Tue, 26 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4804721</guid>        </item>
        <item>
            <title>DcHsp17.7, a small heat shock protein in carrot, is tissue-specifically expressed under salt stress and confers tolerance to salinity.</title>
            <link>http://www.medworm.com/index.php?rid=4804726&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21539946%26dopt%3DAbstract</link>
            <description>Authors: Song NH, Ahn YJ
    The expression and function of DcHsp17.7, a small heat shock protein in carrot (Daucus carota L.), were examined under salt stress, which is an exacerbating environmental condition due to water shortage and irrigation. DcHsp17.7 was constitutively expressed in leaf and stem tissues under normal growth conditions. Upon exposure to 300mM NaCl, the protein level of DcHsp17.7 increased dramatically in leaf tissue, but did not significantly change in stem tissue. Native-PAGE analysis showed tissue-specific oligomer formation. Under normal growth conditions, DcHsp17.7 was found in an approximately 240kDa complex in both tissues. However, NaCl treatment induced an additional approximately 160kDa complex containing DcHsp17.7. This occurred only in leaf tissue, suggesti...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4804726</comments>
            <pubDate>Thu, 21 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4804726</guid>        </item>
        <item>
            <title>Improved electrical wiring of microbes: anthraquinone-modified electrodes for biosensing of chlorinated hydrocarbons.</title>
            <link>http://www.medworm.com/index.php?rid=4804727&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21524722%26dopt%3DAbstract</link>
            <description>Authors: Aulenta F, Ferri T, Nicastro D, Majone M, Papini MP
    The present study reports the development of a novel bioelectrochemical sensor for trichloroethene (TCE), a common subsurface contaminant, based on the measurement of the electrical current resulting from the microbially catalysed reduction of TCE at anthraquinone (AQ)-modified electrodes. Firstly, we describe the development and electrochemical characterisation of AQ-modified electrodes, prepared via spontaneous or electrochemical reduction of AQ diazonium derivatives. Finally, the proof-of-principle of the bioelectrochemical sensor for TCE was evaluated, using a TCE-dechlorinating microbial culture as the biosensing element. The response of the bioelectrochemical sensor was measured either as the peak current in cyclic volt...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4804727</comments>
            <pubDate>Thu, 14 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4804727</guid>        </item>
        <item>
            <title>Antibody therapeutics - the evolving patent landscape biotechnology annual review 2011.</title>
            <link>http://www.medworm.com/index.php?rid=4804729&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21515427%26dopt%3DAbstract</link>
            <description>Authors: Petering J, McManamny P, Honeyman J
    The antibody patent landscape has evolved dramatically over the past 30 years, particularly in areas of technology relating to antibody modification to reduce immunogenicity in humans or improve antibody function. In some cases antibody techniques that were developed in the 1980s are still the subject of patent protection in the United States or Canada.
    PMID: 21515427 [PubMed - as supplied by publisher] (Source: New Biotechnology)</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4804729</comments>
            <pubDate>Mon, 11 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4804729</guid>        </item>
        <item>
            <title>Advances in the production and downstream processing of antibodies.</title>
            <link>http://www.medworm.com/index.php?rid=4804728&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21515428%26dopt%3DAbstract</link>
            <description>Authors: Chon JH, Zarbis-Papastoitsis G
    Sales of monoclonal antibody (mAbs) therapies exceeded $ 40 billion in 2010 and are expected to reach $ 70 billion by 2015. The majority of the approved antibodies are targeting cancer and autoimmune diseases with the top 5 grossing antibodies populating these two areas. In addition over 100 monoclonal antibodies are in Phase II and III of clinical development and numerous others are in various pre-clinical and safety studies. Commercial production of monoclonal antibodies is one of the few biotechnology manufacturing areas that has undergone significant improvements and standardization over the last ten years. Platform technologies have been established based on the structural similarities of these molecules and the regulatory requirements. Thes...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4804728</comments>
            <pubDate>Mon, 11 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4804728</guid>        </item>
        <item>
            <title>Rendered-protein hydrolysates for microbial synthesis of cyanophycin biopolymer.</title>
            <link>http://www.medworm.com/index.php?rid=4804730&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21501699%26dopt%3DAbstract</link>
            <description>Authors: Solaiman DK, Garcia RA, Ashby RD, Piazza GJ, Steinbüchel A
    Cyanophycin is a poly(arginyl-aspartate) biopolymer produced and stored intracellularly by bacteria. Cyanophycin has been proposed as a renewable replacement for petrochemical-based industrial products. An abundant source of amino acids and nitrogen such as in the form of protein hydrolysates is needed for the biosynthesis of cyanophycin. Rendered proteins are largely used as a feed supplement in animal husbandry and aquaculture. New uses would expand the market size of this class of protein coproducts. We prepared and thoroughly characterized the hydrolysates of meat and bone meal, and proceeded to demonstrate for the first time that these hydrolysates could be used in the fermentative production of cyanophycin. Usin...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4804730</comments>
            <pubDate>Thu, 07 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4804730</guid>        </item>
        <item>
            <title>Differentiation of mouse induced pluripotent stem cells into neurons using conditioned medium of dorsal root ganglia.</title>
            <link>http://www.medworm.com/index.php?rid=4804732&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21477670%26dopt%3DAbstract</link>
            <description>Authors: Kitazawa A, Shimizu N
    Mouse induced pluripotent stem (iPS) cells are known to have the ability to differentiate into various cell lineages including neurons in vitro. We have reported that chick dorsal root ganglion (DRG)-conditioned medium (CM) promoted the differentiation of mouse embryonic stem (ES) cells into motor neurons. We investigated the formation of undifferentiated iPS cell colonies and the differentiation of iPS cells into neurons using DRG-CM. When iPS cells were cultured in DMEM containing leukemia inhibitory factor (LIF), the iPS cells appeared to be maintained in an undifferentiated state for 19 passages. The number of iPS cell colonies (200μm in diameter) was maximal at six days of cultivation and the colonies were maintained in an undifferentiated state, bu...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4804732</comments>
            <pubDate>Tue, 05 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4804732</guid>        </item>
        <item>
            <title>Recombinant proteins in rheumatology - recent advances.</title>
            <link>http://www.medworm.com/index.php?rid=4804740&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21473939%26dopt%3DAbstract</link>
            <description>Authors: Rothe A, Rubbert A
    New targeted anti-inflammatory drugs have revolutionized the therapeutic strategies in rheumatology. Recombinant DNA selection technologies have enabled the isolation and humanization of specific antibody fragments of any specificity that can be 'armed' to deliver effective anti-inflammatory 'payloads'. Antibodies and other targeted provide the opportunity to block key soluble mediators of inflammation in their milieu, or alternatively to block intracellular inflammation-triggering pathways by binding to an upstream cell-surface receptor. Designed proteins can be improved with respect to desired pharmacokinetic and pharmacodynamic effects. They facilitate the delivery of the required immunosuppressive effect. However, the individual extent of desired and und...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4804740</comments>
            <pubDate>Mon, 04 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4804740</guid>        </item>
        <item>
            <title>Single B cell antibody technologies.</title>
            <link>http://www.medworm.com/index.php?rid=4804739&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21473940%26dopt%3DAbstract</link>
            <description>Authors: Tiller T
    Monoclonal antibodies (mAbs) are arguably the most significant class of biologics for use as pharmaceuticals and diagnostics. Many technological concepts exist for the generation and identification of therapeutically relevant mAbs, including the isolation and cloning of immunoglobulin (Ig) encoding genes from single B-lineage cells. This review summarizes various single B cell approaches and describes their use for the discovery of mAbs with potential therapeutic values or in basic research.
    PMID: 21473940 [PubMed - as supplied by publisher] (Source: New Biotechnology)</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4804739</comments>
            <pubDate>Mon, 04 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4804739</guid>        </item>
        <item>
            <title>Antibodies in oncology.</title>
            <link>http://www.medworm.com/index.php?rid=4804738&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21473941%26dopt%3DAbstract</link>
            <description>Authors: Pillay V, Gan HK, Scott AM
    Monoclonal antibodies (mAbs) have become one of the largest classes of new therapeutic agents approved for use in oncology, and have revolutionised the treatment of many human malignancies. Clinically useful mAbs can function through several different mechanisms, including inhibition of tumour-related signalling, induction of apoptosis, inhibition of angiogenesis, enhancing host immune response against cancer and targeted delivery of payloads (such as toxins, cytotoxic agents or radioisotopes) to the tumour site. The increasing knowledge of key molecules and cellular pathways involved in tumour induction and progression has led to a rise in the proportion of therapeutic mAbs entering clinical trials. These mAbs consist of various conventional or reco...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4804738</comments>
            <pubDate>Mon, 04 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4804738</guid>        </item>
        <item>
            <title>Antibodies in infectious diseases: polyclonals, monoclonals and niche biotechnology.</title>
            <link>http://www.medworm.com/index.php?rid=4804737&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21473942%26dopt%3DAbstract</link>
            <description>Authors: Berry JD, Gaudet RG
    Antibody preparations have a long history of providing protection from infectious diseases. Although antibodies remain the only natural host-derived defense mechanism capable of completely preventing infection, as products, they compete against inexpensive therapeutics such as antibiotics, small molecule inhibitors and active vaccines. The continued discovery in the monoclonal antibody (mAb) field of leads with broadened cross neutralization of viruses and demonstrable synergy of antibody with antibiotics for bacterial diseases, clearly show that innovation remains. The commercial success of mAbs in chronic disease has not been paralleled in infectious diseases for several reasons. Infectious disease immunotherapeutics are limited in scope as endemic diseas...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4804737</comments>
            <pubDate>Mon, 04 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4804737</guid>        </item>
        <item>
            <title>Antibodies in metabolic diseases.</title>
            <link>http://www.medworm.com/index.php?rid=4804735&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21473944%26dopt%3DAbstract</link>
            <description>Authors: Ahrens B
    In the past century, incidences of chronic metabolic diseases, such as obesity and type II diabetes, have increased dramatically. Obesity and abnormal insulin level are associated with a wide variety of health problems including a markedly increased risk for type II diabetes, fatty liver, hepato-biliary and gallbladder diseases, cardiovascular pathologies, neurodegenerative disorders, asthma and a variety of cancers. The development of therapeutic antibodies has evolved over the past decades into a mainstay of therapeutic options for patients with inflammatory diseases and cancer, while other indication areas such as metabolic diseases have so far only been rarely addressed. Although therapeutic antibodies might have advantages over current type II diabetes treatments...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4804735</comments>
            <pubDate>Mon, 04 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4804735</guid>        </item>
        <item>
            <title>Pre-clinical strategies and safety issues in developing therapeutic monoclonal antibodies.</title>
            <link>http://www.medworm.com/index.php?rid=4804734&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21473945%26dopt%3DAbstract</link>
            <description>This article seeks to provide a systematic approach to identifying and addressing the pertinent risks relative to the characteristics of the particular mAb product before the first administration to human subjects.
    PMID: 21473945 [PubMed - as supplied by publisher] (Source: New Biotechnology)</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4804734</comments>
            <pubDate>Mon, 04 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4804734</guid>        </item>
        <item>
            <title>For inclusion in &quot;Antibodies: From Basics to Therapeutics&quot; Recombinant Antibody Libraries and Selection Technologies.</title>
            <link>http://www.medworm.com/index.php?rid=4804733&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21477669%26dopt%3DAbstract</link>
            <description>For inclusion in &quot;Antibodies: From Basics to Therapeutics&quot; Recombinant Antibody Libraries and Selection Technologies.
    N Biotechnol. 2011 Apr 5;
    Authors: Zhou H, Zhang YL, Lu G, Ji H, Rodi CP
    Active immunization has benefited human health perhaps more than any other biomedical advancement. Today, passive immunization is profoundly changing the practice of medicine by enabling antibody targeting of toxic, self, and other antigens not conducive to active immunization. Recombinant antibody libraries have contributed greatly to this progress and will continue to do so. The ability to construct and display a variety of antibody libraries, including naive, immune, semi-synthetic, and synthetic ones coupled with rapid screening and selection technologies, is in large measure responsibl...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4804733</comments>
            <pubDate>Mon, 04 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4804733</guid>        </item>
        <item>
            <title>Analysis of the antibody structure based on high-resolution crystallographic studies.</title>
            <link>http://www.medworm.com/index.php?rid=4804731&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21477671%26dopt%3DAbstract</link>
            <description>Authors: Narciso JE, Uy ID, Cabang AB, Chavez JF, Pablo JL, Padilla-Concepcion GP, Padlan EA
    High-resolution structures of liganded and unliganded antibody molecules were analyzed in terms of the interaction between the antibody with ligand, between the residues in the contact between the variable domains, and between the framework and the complementarity-determining regions of the antibody. The solvent accessibilities of the residues in the variable domains were also analyzed. The structural information is useful in the engineering of antibodies for therapeutic and other purposes.
    PMID: 21477671 [PubMed - as supplied by publisher] (Source: New Biotechnology)</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4804731</comments>
            <pubDate>Mon, 04 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4804731</guid>        </item>
        <item>
            <title>Establishing a knowledge trail from molecular experiments to clinical trials.</title>
            <link>http://www.medworm.com/index.php?rid=4804741&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21473938%26dopt%3DAbstract</link>
            <description>Authors: Yong MY, González-Beltrán A, Begent R
    During the development cycle of a new antibody therapy, the therapeutic agent will be tested on subsequently more biologically complex models. New experiments' designs are based upon data gathered from prior models. New researchers who inherit the data and researchers from groups with different culture or expertise are often called upon to interpret these data. Experiments which are not recorded consistently or employ ambiguous terminology can make interpreting these results difficult. The researcher who had originally collected the data may not be at hand to correct any misunderstanding or offer clarification and data can be unknowingly misused. This introduces an element of risk into the therapy development process. We have developed a...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4804741</comments>
            <pubDate>Sun, 03 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4804741</guid>        </item>
        <item>
            <title>Therapeutic Applications of Antibodies - Antibodies in Non-Infectious Neurodegenerative Diseases.</title>
            <link>http://www.medworm.com/index.php?rid=4804736&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21473943%26dopt%3DAbstract</link>
            <description>Authors: Krishnamurthy PK, Sigurdsson EM
    Neurodegenerative diseases such as Alzheimer's disease (AD), Parkinson's disease, Huntington's disease (HD) or amyotrophic lateral sclerosis (ALS) are all characterized histologically by the presence of deposits of misfolded proteins, tau and amyloid, -synuclein, huntingtin or superoxide dismutase respectively. Currently these illnesses do not have any disease modifying treatment options. A novel therapeutic strategy that is being pursued is immunomodulation, which is using the body's immune system to target the self proteins that are deposited. Most of these promising approaches are still in preclinical development whilst some have progressed to Phase III clinical trials. As new insights are gained, it is hoped that these immunotherapies will b...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4804736</comments>
            <pubDate>Sun, 03 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4804736</guid>        </item>
        <item>
            <title>CDC19 encoding pyruvate kinase is important for high-temperature tolerance in Saccharomyces cerevisiae.</title>
            <link>http://www.medworm.com/index.php?rid=4804742&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21459167%26dopt%3DAbstract</link>
            <description>Authors: Benjaphokee S, Koedrith P, Auesukaree C, Asvarak T, Sugiyama M, Kaneko Y, Boonchird C, Harashima S
    Use of thermotolerant strains is a promising way to reduce the cost of maintaining optimum temperatures in the fermentation process. Here we investigated genetically a Saccharomyces cerevisiae strain showing a high-temperature (41°C) growth (Htg(+)) phenotype and the result suggested that the Htg(+) phenotype of this Htg(+) strain is dominant and under the control of most probably six genes, designated HTG1 to HTG6. As compared with a Htg(-) strain, the Htg(+) strain showed a higher survival rate after exposure to heat shock at 48°C. Moreover, the Htg(+) strain exhibited a significantly high content of trehalose when cultured at high temperature and stronger resistance to Congo...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4804742</comments>
            <pubDate>Thu, 31 Mar 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4804742</guid>        </item>
        <item>
            <title>Improving lipid production from bagasse hydrolysate with Trichosporon fermentans by response surface methodology.</title>
            <link>http://www.medworm.com/index.php?rid=4804745&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21458601%26dopt%3DAbstract</link>
            <description>Authors: Huang C, Wu H, Li RF, Zong MH
    Oleaginous yeast Trichosporon fermentans was proved to be able to use sulphuric acid-treated sugar cane bagasse hydrolysate as substrate to grow and accumulate lipid. Activated charcoal was shown as effective as the more expensive resin Amberlite XAD-4 for removing the inhibitors from the hydrolysate. To further improve the lipid production, response surface methodology (RSM) was used and a 3-level 4-factor Box-Behnken design was adopted to evaluate the effects of C/N ratio, inoculum concentration, initial pH and fermentation time on the cell growth and lipid accumulation of T. fermentans. Under the optimum conditions (C/N ratio 165, inoculum concentration 11%, initial pH 7.6 and fermentation time 9 days), a lipid concentration of 15.8g/L, which i...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4804745</comments>
            <pubDate>Wed, 30 Mar 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4804745</guid>        </item>
        <item>
            <title>Innovative approaches for effective selection of lipase-producing microorganisms as whole cell catalysts for biodiesel production.</title>
            <link>http://www.medworm.com/index.php?rid=4804744&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21458602%26dopt%3DAbstract</link>
            <description>Authors: Ciudad G, Reyes I, Azócar L, Briones R, Jorquera M, Wick LY, Navia R
    The high cost of commercial lipases limits their industrial application in the production of biodiesel or fatty acid methyl esters (FAME). This disadvantage has encouraged the search for lipase-producing microorganisms (LPMs) as potential whole cell catalysts for FAME production. The aim of this study, therefore, was to evaluate innovative procedures for easy selection and testing of LPMs as a low-cost whole cell catalyst, based on catalytic performance, methanol tolerance and physico-chemical cell surface properties. The latter (in particular the cell surface hydrophobicity and charge) were analyzed because of their crucial role in microbial adhesion to surfaces and the concomitant increase in cell immobili...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4804744</comments>
            <pubDate>Wed, 30 Mar 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4804744</guid>        </item>
        <item>
            <title>Expression of a human cytochrome P4502E1 in Nicotiana tabacum enhances tolerance and remediation of γ-hexachlorocyclohexane.</title>
            <link>http://www.medworm.com/index.php?rid=4804743&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21458603%26dopt%3DAbstract</link>
            <description>Authors: Singh S, Sherkhane PD, Kale SP, Eapen S
    Lindane (γ-hexachlorocyclohexane), a persistent organo-chlorine insecticide widely used in developing countries, has a negative effect as a polluting agent of soil and surface waters. Plants can be used for remediation of organic pollutants and their efficiency can be enhanced by introduction of heterologous genes. Mammalian cytochrome P4502E1 (CYP2E1), an important monooxygenase is involved in the degradation of a wide range of xenobiotics including environmental pollutants/herbicides and pesticides. Here, we report the development of transgenic tobacco plants expressing human CYP2E1 and the efficacy of plants for remediation of lindane. Transgenic tobacco plants with CYP2E1 showed enhanced tolerance to lindane when grown in hydroponic...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4804743</comments>
            <pubDate>Wed, 30 Mar 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4804743</guid>        </item>
        <item>
            <title>Sequential anaerobic/aerobic digestion of waste activated sludge: analysis of the process performance and kinetic study.</title>
            <link>http://www.medworm.com/index.php?rid=4804746&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21453800%26dopt%3DAbstract</link>
            <description>Authors: Tomei MC, Rita S, Mininni G
    Sequential anaerobic-aerobic digestion was applied to waste activated sludge (WAS) of a full scale wastewater treatment plant. The study was performed with the objective of testing the sequential digestion process on WAS, which is characterized by worse digestibility in comparison with the mixed sludge. Process performance was evaluated in terms of biogas production, volatile solids (VS) and COD reduction, and patterns of biopolymers (proteins and polysaccharides) in the subsequent digestion stages. VS removal efficiency of 40%, in the anaerobic phase, and an additional removal of 26%, in the aerobic one, were observed. For total COD removal efficiencies of 35% and 25% for anaerobic and aerobic stage respectively, were obtained. Kinetics of VS degra...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4804746</comments>
            <pubDate>Mon, 28 Mar 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4804746</guid>        </item>
        <item>
            <title>Fungicides degradation in an organic biomixture: impact on microbial diversity.</title>
            <link>http://www.medworm.com/index.php?rid=4804747&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21439413%26dopt%3DAbstract</link>
            <description>Authors: Coppola L, Comitini F, Casucci C, Milanovic V, Monaci E, Marinozzi M, Taccari M, Ciani M, Vischetti C
    Biological systems are being developed all over EU countries to protect water-bodies from pesticide contamination at farm level. A laboratory experiment was carried out to test the efficiency of a mixture of compost and straw in bio-degrading different mixtures of fungicides usually applied in vineyards. At the same time the effects of fungicide applications on microbial community of biomixture were also evaluated. Results showed that the biomixture had a good capability of degrading pesticides. Indeed, at the end of the experiment (112 days), the concentration of most of the pesticides was close to complete degradation. Denaturing gradient gel electrophoresis (DGGE) analysis ...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4804747</comments>
            <pubDate>Wed, 23 Mar 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4804747</guid>        </item>
        <item>
            <title>Production and characterization of exopolysaccharides and antioxidant from Paenibacillus sp. TKU023.</title>
            <link>http://www.medworm.com/index.php?rid=4642076&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21402186%26dopt%3DAbstract</link>
            <description>Authors: Wang CL, Huang TH, Liang TW, Fang CY, Wang SL
    Using squid pen powder (SPP) as the sole C/N source, Paenibacillus sp. TKU023 produced exopolysaccharides (EPS) and antioxidant. With medium containing 1.5% SPP, 0.1% K(2)HPO(4), and 0.05% MgSO(4)·7H(2)O, pH 7.23, the culture was incubated at 37°C in liquid (50mL/250mL) for five days. The resultant culture supernatant had higher EPS productivity (4.55g/L). The crude EPS were isolated by centrifugation, methanol precipitation and deproteinization. The characterization of the EPS demonstrated that it was mainly composed of glucose and maltose. In addition, the culture supernatant incubated for four days by using baffled base flask showed the strongest antioxidant activities and the highest total phenolic content, but maximum EPS pr...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4642076</comments>
            <pubDate>Mon, 21 Mar 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4642076</guid>        </item>
        <item>
            <title>Biotechnological valorization of low-cost sugar-based media for bacteriocin production by Leuconostoc mesenteroides E131.</title>
            <link>http://www.medworm.com/index.php?rid=4642073&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21419881%26dopt%3DAbstract</link>
            <description>Authors: Metsoviti M, Paramithiotis S, Drosinos EH, Skandamis PN, Galiotou-Panayotou M, Papanikolaou S
    The aim of the present study was to evaluate the suitability of low cost carbon sources for bacteriocin production by Leuconostoc mesenteroides strain E131. For this purpose, inexpensive sugars deriving from a sugar refinery plant (glucose, fructose and sucrose) as well as waste molasses were utilized as carbon sources in submerged shake-flask experiments and the kinetic response of the microorganism was evaluated. Interestingly, for the case of molasses, non-negligible decolorization-detoxification (up to ∼27%) of the residue was performed together with the production of bacteriocin. In all instances the initial concentration of sugars employed was adjusted at 20 and 30g/L, therefo...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4642073</comments>
            <pubDate>Wed, 16 Mar 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4642073</guid>        </item>
        <item>
            <title>In vitro determination of the contraceptive spermicidal activity of essential oil of Trachyspermum ammi (L.) Sprague ex Turrill fruits.</title>
            <link>http://www.medworm.com/index.php?rid=4642077&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21396489%26dopt%3DAbstract</link>
            <description>This study was conducted to determine the spermicidal and contraceptive efficacy of essential oil of Trachyspermum ammi on human sperm in vitro. Chemical compositions of the oil were analyzed by GC-MS. Nearly 30 compounds representing 91.39% of the total oil were identified. The minimum effective dose (MED) of essential oil of T. ammi that induced instant immobilization of human spermatozoa in vitro was 125μg/mL. The motility was also irreversible. All of the human sperms were found to be non viable within 10min at this concentration. The activity of acrosomal enzyme was reduced and a significant releases of 5'-nucleotidase into the surrounding medium was noted after treatment with MED concentration of essential oil, indicating the plasma membrane degradation of the sperm. The maximum num...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4642077</comments>
            <pubDate>Tue, 15 Mar 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4642077</guid>        </item>
        <item>
            <title>QuikChange Shuffling: a Convenient and Robust Method for Site-directed Mutagenesis and Random Recombination of Homologous Genes.</title>
            <link>http://www.medworm.com/index.php?rid=4642075&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21402187%26dopt%3DAbstract</link>
            <description>Authors: An Y, Chen L, Sun S, Lv A, Wu W
    Here we describe a robust method, termed QuikChange shuffling, for efficient site-directed mutagenesis and random recombination of homologous genes. The homologous genes are fragmented, and the random fragments are reassembled in a self-priming polymerase reaction to obtain chimeric genes. The product is then mixed with linearized vector and two pairs of complementary mutagenic primers, followed by assembly of the chimeric genes and linearized vector through QuikChange-like amplification to introduce recombinant plasmids with a site-directed mutation. The method, which can yield 100% chimeric genes after library construction, is more convenient and efficient than current DNA shuffling methods.
    PMID: 21402187 [PubMed - as supplied by publishe...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4642075</comments>
            <pubDate>Fri, 11 Mar 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4642075</guid>        </item>
        <item>
            <title>Cloning and optimized expression of a GH-11 xylanase from Fusarium oxysporum in Pichia pastoris.</title>
            <link>http://www.medworm.com/index.php?rid=4642074&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21402188%26dopt%3DAbstract</link>
            <description>Authors: Moukouli M, Topakas E, Christakopoulos P
    The endo-1,4-β-xylanase gene xyn11a from Fusarium oxysporum, member of the fungal glycosyl hydrolase (GH) family 11, was cloned and expressed in Pichia pastoris. The mature xylanase gene, which results after the excision of one intron and the secreting signal peptide, was placed under the control of an alcohol oxidase promoter (AOX1) in the plasmid pPICZαC. The final construction was integrated into the genome of the methylotrophic yeast P. pastoris X33 and the ability to produce xylanase activity was evaluated in flask cultures. Recombinant P. pastoris efficiently secreted xylanase into the medium and produced high level of enzymatic activity (110 U/ml) after 216h of growth, under methanol induction. In order to achieve higher enzyme...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4642074</comments>
            <pubDate>Fri, 11 Mar 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4642074</guid>        </item>
        <item>
            <title>Maximization of fructose esters synthesis by response surface methodology.</title>
            <link>http://www.medworm.com/index.php?rid=4580623&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21356336%26dopt%3DAbstract</link>
            <description>Authors: Neta NS, Peres AM, Teixeira JA, Rodrigues LR
    Enzymatic synthesis of fructose fatty acid ester was performed in organic solvent media, using a purified lipase from Candida antartica B immobilized in acrylic resin. Response surface methodology with a central composite rotatable design based on five levels was implemented to optimize three experimental operating conditions (temperature, agitation and reaction time). A statistical significant cubic model was established. Temperature and reaction time were found to be the most significant parameters. The optimum operational conditions for maximizing the synthesis of fructose esters were 57.1°C, 100rpm and 37.8h. The model was validated in the identified optimal conditions to check its adequacy and accuracy, and an experimental est...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4580623</comments>
            <pubDate>Sat, 26 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4580623</guid>        </item>
        <item>
            <title>An efficient and reproducible method for regeneration of whole plants from mature seeds of a high yielding Indica rice (Oryza sativa L.) variety PAU 201.</title>
            <link>http://www.medworm.com/index.php?rid=4580624&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21352959%26dopt%3DAbstract</link>
            <description>In this report we established a reproducible plant regeneration system through somatic embryogenesis. The explants used for regeneration were embryogenic calli derived from mature seeds cultured on callus induction media. For callus induction mature seeds were cultured on MS medium containing 30g/l sucrose combined with 560mg/l proline and 1.5-3.5mg/l 2,4-D and 0.5-1.5mg/l Kin. For plant regeneration, embryogenic calli were transferred to MS medium containing 30g/l sucrose, supplemented with 1.0-3.0mg/l BAP, 0.5-1.5mg/l Kin and 0.5-1.5mg/l NAA. The highest frequency of callus induction (44.4%) was observed on the MS medium supplemented with 2.5mg/l 2,4-D, 0.5mg/l Kin, 560mg/l proline and 30g/l sucrose. The highest frequency of shoot regeneration (42.5%) was observed on the MS medium supple...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4580624</comments>
            <pubDate>Wed, 23 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4580624</guid>        </item>
        <item>
            <title>Efficient and reproducible mammalian cell bioprocesses without probes and controllers ?</title>
            <link>http://www.medworm.com/index.php?rid=4525805&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21338722%26dopt%3DAbstract</link>
            <description>Authors: Tissot S, Oberbek A, Reclari M, Dreyer M, Hacker DL, Baldi L, Farhat M, Wurm FM
    Bioprocesses for recombinant protein production with mammalian cells are typically controlled for several physicochemical parameters including the pH and dissolved oxygen concentration (DO) of the culture medium. Here we studied whether these controls are necessary for efficient and reproducible bioprocesses in an orbitally shaken bioreactor (OSR). Mixing, gas transfer, and volumetric power con- sumption (P(v)) were determined in both a 5-L OSR and a 3-L stirred-tank bioreactor (STR). The two cultivation systems had a similar mixing intensity, but the STR had a lower volumetric mass transfer coefficient of oxygen (k(L)a) and a higher P than the OSR. Recombinant CHO cell lines expressing either tumo...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4525805</comments>
            <pubDate>Fri, 18 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4525805</guid>        </item>
        <item>
            <title>Investigation of Charged Polymer Influence on Green Fluorescent Protein Thermal Stability.</title>
            <link>http://www.medworm.com/index.php?rid=4525807&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21334469%26dopt%3DAbstract</link>
            <description>Authors: Novaes LC, Mazzola PG, Pessoa A, Penna TC
    Methods of stabilization and formulation of proteins is an important in both the biopharmaceutical and biocatalysis industry. Polymers are often used as modifiers of characteristics of biological macromolecules in order to improve the biochemical activity and stability of proteins or drug bioavailability. Green fluorescent protein (GFP) shows remarkable structural stability and high fluorescence; its stability can be directly related to its fluorescence output, among other characteristics. GFP is stable under increasing temperatures, and its thermal denaturation is highly reproducible. Relative thermal stability was undertaken by incubation of GFP at varying temperatures and GFP fluorescence was used as a reporter for unfolding. At 80...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4525807</comments>
            <pubDate>Thu, 17 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4525807</guid>        </item>
        <item>
            <title>Characterization of a fungistatic substance produced by Aspergillus flavus isolated from soil and its significance in nature.</title>
            <link>http://www.medworm.com/index.php?rid=4525806&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21334470%26dopt%3DAbstract</link>
            <description>Authors: Chen YT, Lin MJ, Yang CH, Ko WH
    A fungus capable of using vegetable tissues for multiplication in soil was isolated and identified as Aspergillus flavus based on morphological characteristics and sequence similarity of ITS and 28S. When grown in liquid medium prepared from the same vegetable tissues used in soil amendment, the isolate of A. flavus produced a substance capable of preventing disease development of black leaf spot of mustard cabbage caused by Alternaria brassicicola and inhibiting the germination of A. brassicicola conidia. The inhibitory substance was fungistatic, and was very stable under high temperature and high or low pH value. It was soluble in ethanol or methanol, moderately soluble in water, and insoluble in acetone, ethyl acetate or ether. The inhibitor ...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4525806</comments>
            <pubDate>Thu, 17 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4525806</guid>        </item>
        <item>
            <title>Production of poly(3-hydroxybutyrate) and poly(3-hydroxybutyrate-co-4-hydroxybutyrate) by Ralstonia eutropha from soybean oil.</title>
            <link>http://www.medworm.com/index.php?rid=4525808&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21333767%26dopt%3DAbstract</link>
            <description>Authors: Park DH, Kim BS
    High-yield production of polyhydroxyalkanoates (PHAs) by Ralstonia eutropha KCTC 2662 was investigated using soybean oil and γ-butyrolactone as carbon sources. In flask culture, it was shown that R. eutropha KCTC 2662 accumulated PHAs during the growth phase. The optimum carbon to nitrogen ratio (C/N ratio) giving the highest cell and PHA yield was 20 g-soybean oil/g-(NH(4))(2)SO(4). The 4-hydroxybutyrate (4HB) fraction in the copolymer was not strongly affected by the C/N ratio. In a 2.5-L fermentor, a homopolymer of poly(3-hydroxybutyrate) [P(3HB)] was produced from soybean oil as the sole carbon source by batch and fed-batch cultures of R. eutropha with dry cell weights of 15∼32g/L, PHA contents of 78∼83 wt%, and yields of 0.80∼0.82 g-PHA/g-soybean oi...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4525808</comments>
            <pubDate>Wed, 16 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4525808</guid>        </item>
        <item>
            <title>Use of whey lactose from dairy industry for economical kefiran production by Lactobacillus kefiranofaciens in mixed cultures with yeasts.</title>
            <link>http://www.medworm.com/index.php?rid=4525813&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21315193%26dopt%3DAbstract</link>
            <description>Authors: Cheirsilp B, Radchabut S
    To evaluate the feasibility of producing kefiran industrially, whey lactose, a by-product from dairy industry, was used as a low cost carbon source. Because the accumulation of lactic acid as a by-product of Lactobacillus kefiranofaciens inhibited cell growth and kefiran production, the kefir grain derived and non-derived yeasts were screened for their abilities to reduce lactic acid and promote kefiran production in a mixed culture. Six species of yeasts were examined: Torulaspora delbrueckii IFO 1626; Saccharomyces cerevisiae IFO 0216; Debaryomyces hansenii TISTR 5155; Saccharomyces exiguus TISTR 5081; Zygosaccharomyces rouxii TISTR 5044; and Saccharomyces carlsbergensis TISTR 5018. The mixed culture of L. kefiranofaciens with S. cerevisiae IFO 0216 ...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4525813</comments>
            <pubDate>Tue, 15 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4525813</guid>        </item>
        <item>
            <title>Significant improvement of Geobacillus thermoleovorans CCR11 thermoalkalophilic lipase production using Response Surface Methodology.</title>
            <link>http://www.medworm.com/index.php?rid=4525812&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21315194%26dopt%3DAbstract</link>
            <description>Authors: Sánchez-Otero MG, Ruiz-López II, Avila-Nieto DE, Oliart-Ros RM
    The medium optimization for the production of the Geobacillus thermoleovorans CCR11 thermoalkalophilic lipase was carried out in shake flask cultures using safflower high oleic oil. In the first step of optimization, a two level fractional factorial design allowed the identification of the concentration of nutrient broth and temperature as the main variables significantly affecting lipase production (P&amp;lt;0.05). In a second step, a D-optimal design was applied to determine the variables optimal values, defined as those yielding maximal lipase production in shaken flasks, thus demonstrating that the optimal concentration of nutrient broth was 3.8g/l and the optimal culture temperature was 39.5°C. The model was ex...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4525812</comments>
            <pubDate>Tue, 15 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4525812</guid>        </item>
        <item>
            <title>Induction of hypocrellin production by Triton X-100 under submerged fermentation with Shiraia sp. SUPER-H168.</title>
            <link>http://www.medworm.com/index.php?rid=4525810&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21324385%26dopt%3DAbstract</link>
            <description>Authors: Cai Y, Liao X, Liang X, Ding Y, Sun J, Zhang D
    Hypocrellins are important photodynamic therapy compounds for cancer disease. The effect of surfactants on hypocrellin production of Shiraia sp. SUPER-H168 was evaluated under submerged fermentation condition. The production of hypocrellins could reach 780.6mg/l with the addition of Triton X-100, confirmed by color reaction, high performance liquid chromatography, electrospray ionization mass spectrometry and nuclear magnetic resonance experiments. According to our observation, treatment of the culture at the beginning of the fermentation was most effective, and the yield of hypocrellins was much lower with the addition of Triton X-100 during the log phase and stationary phase. Shiraia sp. SUPER-H168 could not produce hypocrellin ...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4525810</comments>
            <pubDate>Sun, 13 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4525810</guid>        </item>
        <item>
            <title>High-level production of extracellular lipase by Yarrowia lipolytica mutants from methyl oleate.</title>
            <link>http://www.medworm.com/index.php?rid=4525809&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21324386%26dopt%3DAbstract</link>
            <description>Authors: Darvishi F, Destain J, Nahvi I, Thonart P, Zarkesh-Esfahani H
    The yeast Yarrowia lipolytica degrades efficiently low-cost hydrophobic substrates for the production of various added-value products such as lipases. To obtain yeast strains producing high levels of extracellular lipase, Y. lipolytica DSM3286 was subjected to mutation using ethyl methanesulfonate (EMS) and ultraviolet (UV) light. Twenty mutants were selected out of 1600 mutants of Y. lipolytica treated with EMS and UV based on lipase production ability on selective medium. A new industrial medium containing methyl oleate was optimized for lipase production. In the 20L bioreactor containing new industrial medium, one UV mutant (U6) produced 356U/mL of lipase after 24h, which is about 10.5-fold higher than that produ...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4525809</comments>
            <pubDate>Sun, 13 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4525809</guid>        </item>
        <item>
            <title>Biocatalytic synthesis and antitumor activities of novel silybin-acylated derivatives with dicarboxylic acids.</title>
            <link>http://www.medworm.com/index.php?rid=4525811&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21320648%26dopt%3DAbstract</link>
            <description>Authors: Theodosiou E, Loutrari H, Stamatis H, Roussos C, Kolisis FN
    Novel silybin-acylated derivatives with dicarboxylic acids were prepared in various organic solvents using immobilized Candida antarctica lipase B (Novozym 435(®)). The reaction parameters affecting the silybin conversion, such as the nature of the organic solvent and the acyl donor used were investigated. The antiproliferative effects of silybin monoesters, and their ability to modulate the secretion of vascular endothelial growth factor (VEGF) were estimated using K562 human lymphoblastoma cells and compared to the parental compound. The synthesized esters retained the biological function of silybin and in some cases were more effective, indicating that target biotransformation may generate novel compounds with imp...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4525811</comments>
            <pubDate>Sat, 12 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4525811</guid>        </item>
        <item>
            <title>Improvement of Bacillus thuringiensis bioinsecticides production by sporeless and sporulating strains using response surface methodology.</title>
            <link>http://www.medworm.com/index.php?rid=4471357&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21310269%26dopt%3DAbstract</link>
            <description>Authors: Khedher SB, Kamoun A, Jaoua S, Zouari N
    Statistical experimental designs, involving a Plackett-Burman design followed by a rotatable central composite design were used to optimize the culture medium constituents for Bacillus thuringiensis bioinsecticides production. This was carried out by using firstly an asporogenic strain and extrapolated to some sporeless and sporulating strains. Initial screening of production parameters was performed and the variables with statistically significant effects on delta-endotoxin production were identified: glucose, glycerol, yeast extract and MnSO(4). These variables were selected for further optimization by response surface methodology. The obtained results revealed that the optimum culture medium for delta-endotoxin production consists of ...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4471357</comments>
            <pubDate>Mon, 07 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4471357</guid>        </item>
        <item>
            <title>The impact of the EU regulatory constraint of transgenic crops on farm income.</title>
            <link>http://www.medworm.com/index.php?rid=4471358&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21272674%26dopt%3DAbstract</link>
            <description>Authors: Park J, McFarlane I, Phipps R, Ceddia G
    World population and the need for nutritious food continue to grow. For 14 years farmers from a range of countries across the globe have been accessing transgenic technologies either to reduce crop production costs, increase yield and/or to exploit a range of rotational benefits. In 2009 134Mha of transgenic crops was grown. The arable area of the EU 27 is approximately 102Mha; however, only about 0.1Mha of transgenic crops, mainly maize in Spain, is grown in the EU. This is in part due to limited approvals before the establishment of a moratorium on the cultivation of transgenic crops. In this paper we estimate the revenue foregone by EU farmers, based on the potential hectarages of IR and HT transgenic crops that have been economically...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4471358</comments>
            <pubDate>Tue, 25 Jan 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4471358</guid>        </item>
        <item>
            <title>Mixed culture of Oleaginous Yeast Rhodotorula glutinis and Microalga Chlorella vulgaris for Lipids Production from Industrial Wastes and Its Use as Biodiesel Feedstock.</title>
            <link>http://www.medworm.com/index.php?rid=4404459&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21255692%26dopt%3DAbstract</link>
            <description>Authors: Cheirsilp B, Suwannarat W, Niyomdecha R
    A mixed culture of oleaginous yeast Rhodotorula glutinis and microalga Chlorella vulgaris was performed to enhance lipids production from industrial wastes. These included effluent from seafood processing plant and molasses from sugar cane plant. In the mixed culture, the yeast grew faster and the lipids production was higher than that in the pure cultures. This could be because microalga acted as an oxygen generator for yeast, while yeast provided CO(2) to microalga and both carried out the production of lipids. The optimal conditions for lipids production by the mixed culture were as follows: ratio of yeast to microalga at 1:1; initial pH at 5.0; molasses concentration at 1%; shaking speed at 200rpm; and light intensity at 5.0 klux und...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4404459</comments>
            <pubDate>Tue, 18 Jan 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4404459</guid>        </item>
        <item>
            <title>Formation of acrylamide from glucans and asparagine.</title>
            <link>http://www.medworm.com/index.php?rid=4404465&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21252006%26dopt%3DAbstract</link>
            <description>Authors: Tsutsumiuchi K, Watanabe Y, Watanabe M, Hibino M, Kambe M, Okajima N, Negishi H, Miwa J, Taniguchi H
    Model foods consisting of carbohydrates, asparagine (Asn), albumin, and sodium chloride were heated at 180°C for various times, and the levels of acrylamide (AA) in these foods were determined by LC/MS/MS. When glucans such as β-cyclodextrin (β-CD), starch, and cellulose were used as carbohydrates in the above model, the levels of AA formed were approximately the same as or much higher than that observed in the glucose model. Glucans were heated in the absence of Asn for 1 hr, and their degradation products were analyzed for sugar components by HPAEC-PAD and for volatile compounds by GC/MS. The amounts of glucose detected in the glucan models, however, were too low to consid...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4404465</comments>
            <pubDate>Mon, 17 Jan 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4404465</guid>        </item>
        <item>
            <title>Purification, characterization and thermal inactivation kinetics of a non-regioselective thermostable lipase from a genotypically identified extremophilic Bacillus subtilis NS 8.</title>
            <link>http://www.medworm.com/index.php?rid=4404466&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21238617%26dopt%3DAbstract</link>
            <description>Authors: Olusesan AT, Azura LK, Forghani B, Bakar FA, Mohamed AK, Radu S, Manap MY, Saari N
    Thermostable lipase produced by a genotypically identified extremophilic Bacillus subtilis NS 8 was purified 500-fold to homogeneity with a recovery of 16% by ultrafiltration, DEAE-Toyopearl 650M and Sephadex G-75 column. The purified enzyme showed a prominent single band with a molecular weight of 45kDa. The optimum pH and temperature for activity of lipase were 7.0 and 60°C, respectively. The enzyme was stable in the pH range between 7 and 9 and temperature range between 40 and 70°C. It showed high stability with half-lives of 273.38min at 60°C, 51.04min at 70°C and 41.58min at 80°C. The D-values at 60, 70 and 80°C were 788.70, 169.59 and 138.15min, respectively. The enzyme's enthalpy, e...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4404466</comments>
            <pubDate>Fri, 14 Jan 2011 00:00:00 +0100</pubDate>
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        <item>
            <title>The effects of Korean propolis against foodborne pathogens and transmission electron microscopic examination.</title>
            <link>http://www.medworm.com/index.php?rid=4404471&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21232643%26dopt%3DAbstract</link>
            <description>This study was performed to evaluate the effects of Korean propolis against foodborne pathogens and spores of Bacillus cereus and to investigate the antimicrobial activity against B. cereus structure by transmission electron microscopy (TEM). The antimicrobial effects of the Korean propolis were tested against foodborne pathogens including Gram-positive (B. cereus, Listeria monocytogenes and Staphylococcus aureus) and Gram-negative (Salmonella typhimurium, Escherichia coli and Pseudomonas fluorescence) bacteria by agar diffusion assay. Gram-positive bacteria were more sensitive than were Gram-negative bacteria. The vegetative cells of B. cereus were the most sensitive among the pathogens tested with minimum inhibitory concentration (MIC) of 0.036mg/μl of propolis on agar medium. Based on ...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4404471</comments>
            <pubDate>Tue, 11 Jan 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4404471</guid>        </item>
        <item>
            <title>An alkali-thermotolerant extracellular protease from a newly isolated Streptomyces sp. DP2.</title>
            <link>http://www.medworm.com/index.php?rid=4404470&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21232644%26dopt%3DAbstract</link>
            <description>Authors: Bajaj BK, Sharma P
    Of six alkalitolerant, extracellular protease producing bacterial strains isolated, DP2 displayed maximum activity. This organism was designated as Streptomyces sp. DP2 and identified as Streptomyces ambofaciens. Maximum protease yield was observed after 48hours of submerged fermentation using various carbon and nitrogen sources. Fructose was found to be the best substrate for protease production, followed by maltose, lactose and wheat bran. Mustard cake is reported for the first time as the most ideal nitrogen source although soybean meal also gave comparable yield. The protease produced by Streptomyces sp. DP2 exhibited extensive activity over a broad pH range (4-12) with maximum activity at pH 8, and was active over a broad range of elevated temperatures ...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4404470</comments>
            <pubDate>Tue, 11 Jan 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4404470</guid>        </item>
        <item>
            <title>Cellulase production in a new mutant strain of Penicillium decumbens ML-017 by solid state fermentation with rice bran.</title>
            <link>http://www.medworm.com/index.php?rid=4404469&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21232645%26dopt%3DAbstract</link>
            <description>Authors: Liu Y, Luo Z, Long C, Wang H, Long M, Hu Z
    To produce cellulolytic enzyme efficiently, Penicillium decumbens strain L-06 was used to prepare mutants with ethyl methane sulfonate (EMS) and UV-irradiation. A mutant strain ML-017 is shown to have a higher cellulase activity than others. Box-Behnken's design (BBD) and response surface methodology (RSM) were adopted to optimize the conditions of cellulase (filter paper activity, FPA) production in strain ML-017 by solid-state fermentation (SSF) with rice bran as the substrate. And the result shows that the initial pH, moisture content and culture temperature all have significant effect on the production of cellulose. The optimized condition shall be initial pH 5.7, moisture content 72% and culture temperature 30°C. The maximum cel...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4404469</comments>
            <pubDate>Tue, 11 Jan 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4404469</guid>        </item>
        <item>
            <title>Hyper production of alkali stable xylanase in lesser duration by Bacillus pumilus SV-85S using wheat bran under solid state fermentation.</title>
            <link>http://www.medworm.com/index.php?rid=4404468&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21232646%26dopt%3DAbstract</link>
            <description>Authors: Nagar S, Mittal A, Kumar D, Kumar L, Kuhad RC, Gupta VK
    High level production of an extracellular cellulase-poor alkali stable xylanase has been conceded from newly isolated Bacillus pumilus SV-85S under solid state fermentation using wheat bran as a substrate. Optimization of the fermentation conditions enhanced the enzyme production to 73,000±1000IU/g dry substrate, which was 13.8-fold higher than unoptimized conditions (5300IU/g). The enzyme titre was highest after 48h of incubation at 30°C with 1:3 ratios of substrate to moistening agent using wheat bran as a carbon source. The enzyme could be produced in significant levels by using either tap water or distilled water alone as a moistening agent. An elevated production of xylanase by B. pumilus SV-85S in the presence of ...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4404468</comments>
            <pubDate>Tue, 11 Jan 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4404468</guid>        </item>
        <item>
            <title>Surrogate antigens as targets for proteome-wide binder selection.</title>
            <link>http://www.medworm.com/index.php?rid=4404467&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21232647%26dopt%3DAbstract</link>
            <description>Authors: Gustavsson E, Ek S, Steen J, Kristensson M, Algenäs C, Uhlén M, Wingren C, Ottosson J, Hober S, Borrebaeck CA
    In the past decade, many initiatives were taken for the development of antibodies for proteome-wide studies, as well as characterisation and validation of clinically relevant disease biomarkers. Phage display offers many advantages compared to antibody generation by immunisation because it is an unlimited resource of affinity reagents without batch-to-batch variation and is also amendable for high throughput in contrast to conventional hybridoma technology. One of the major bottlenecks to proteome-wide binder selection is the limited supply of suitable target antigens representative of the human proteome. Here, we provide proof of principle of using easily accessible...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4404467</comments>
            <pubDate>Tue, 11 Jan 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4404467</guid>        </item>
        <item>
            <title>Bioconversion of Saccharum spontaneum (wild sugarcane) hemicellulosic hydrolysate into ethanol by mono and co-cultures of Pichia stipitis NCIM3498 and thermotolerant Saccharomyces cerevisiae-VS(3).</title>
            <link>http://www.medworm.com/index.php?rid=4338537&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21185411%26dopt%3DAbstract</link>
            <description>Authors: Chandel AK, Singh OV, Narasu ML, Rao LV
    The lignocellulosic biomass is a low-cost renewable resource for eco-benign liquid fuel 'ethanol'. To resolve the hydrolysis of mixed sugars in lignocellulosic substrate Saccharum spontaneum, the microbial co-cultures of Pichia stipitis NCIM 3498 and thermotolerant Saccharomyces cerevisiae-VS(3) were analyzed for efficient bioconversion of mixed sugars into ethanol. Among the hydrolysis conditions, the acid hydrolysis released maximum sugars along with furans, phenolics and acetic acid. The acidic hydrolysate was detoxified and fermented by monocultures of P. stipitis NCIM3498 (P.S.) and thermotolerant S. cerevisiae VS(3) (S.C.), and co-culture of P.S. (7.5mL) and S.C. (2.5mL). Before the fermentation of hemicellulose acid hydrolysate, b...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4338537</comments>
            <pubDate>Thu, 23 Dec 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4338537</guid>        </item>
        <item>
            <title>Cyclic nucleotides as affinity tools: Phosphorothioate cAMP analogues address specific PKA subproteomes.</title>
            <link>http://www.medworm.com/index.php?rid=4276931&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21147280%26dopt%3DAbstract</link>
            <description>Authors: Hanke SE, Bertinetti D, Badel A, Schweinsberg S, Genieser HG, Herberg FW
    cAMP is a general second messenger controlling distinct targets in eukaryotic cells. In a (sub)proteomic approach, two classes of phosphorothioate cAMP affinity tools were used to isolate and to identify signalling complexes of the main cAMP target, cAMP dependent protein kinase (PKA). Agonist analogues (here: Sp-cAMPS) bind to the regulatory subunits of PKA (PKA-R), together with their interaction partners, and cause dissociation of a holoenzyme complex comprising PKA-R and catalytic subunits of PKA (PKA-C). Antagonist analogues (here: Rp-cAMPS) bind to the holoenzyme without dissociating the complex and were developed to identify interaction partners that bind to the entire complex or to PKA-C. More tha...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4276931</comments>
            <pubDate>Fri, 10 Dec 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4276931</guid>        </item>
        <item>
            <title>Utilization of heat-dried Pseudomonas aeruginosa biomass for voltammetric determination of Pb(II).</title>
            <link>http://www.medworm.com/index.php?rid=4276932&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21144915%26dopt%3DAbstract</link>
            <description>Authors: Yüce M, Nazır H, Dönmez G
    In this research, thermally dried Pseudomonas aeruginosa cells were used as a biological material for the construction of a microbial biosensor. The preparation, optimization and application of the developed microbial biosensor, which analyzed Pb(II), are presented. The method was based on stripping of adsorbed metal ions from the modified electrode surface. Modified carbon paste electrodes were preconcentrated at open circuit, and then electrochemically measured by using cyclic voltammetry (CV) and differential pulse stripping voltammetry (DPSV) techniques. It was found that the thermally dried cells were capable of adsorbing Pb(II) ions from aqueous solutions and could determine the ions prominently at optimum experimental conditions. Many import...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4276932</comments>
            <pubDate>Tue, 07 Dec 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4276932</guid>        </item>
        <item>
            <title>Characterization of statistically produced xylanase for enrichment of fruit juice clarification process.</title>
            <link>http://www.medworm.com/index.php?rid=4218827&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21093618%26dopt%3DAbstract</link>
            <description>Authors: Dhiman SS, Garg G, Sharma J, Mahajan R
    Critical factors for xylanase production of Bacillus stearothermophilus under batch fermentation and for clarification of citrus fruit juice using this xylanase were optimized through central composite design of response surface methodology. Statistical approach resulted in an increase of 1.19-fold in xylanase yield over conventional method. Model equation for juice clarification included independent variables viz. temperature, incubation time and enzyme dose to study the dependent variables such as yield, acidic neutralityand filterabilityetc. Coefficient of determination, R(2) for enzyme production model and for different juice properties were in accordance with the linearity of the model. On the basis of the contour plots the optimum e...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4218827</comments>
            <pubDate>Wed, 17 Nov 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4218827</guid>        </item>
        <item>
            <title>A Statistical approach for the enhanced production of alkaline protease showing fibrinolytic activity from a newly isolated Gram-negative Bacillus sp. strain AS- S20-I.</title>
            <link>http://www.medworm.com/index.php?rid=4185781&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21078421%26dopt%3DAbstract</link>
            <description>Authors: Mukherjee AK, Rai SK
    An alkaline-fibrinolytic protease-producing bacterial strain (AS-S20-I) isolated from a soil sample in Assam was a Gram-negative rod and grown at temperatures ranging from 25 to 55°C, and pH 6.5 to 11.0. Taxonomic identification of isolated strain by polyphasic approach (phenotypic characterization, chemotaxonomic properties, and ribotyping data of the strain) suggested that it belongs to the genus Bacillus, for which the name Bacillus sp. strain AS-S20-I (MTCC 8961) was proposed. The initial screening by using Placket-Burman design demonstrated that amongst the tested factors, casein, ammonium sulphate and pH of the medium significantly (p&amp;lt;0.05) enhanced the protease (fibrinolytic enzyme) yield in submerged fermentation. Further optimization of fibrin...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4185781</comments>
            <pubDate>Fri, 12 Nov 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4185781</guid>        </item>
        <item>
            <title>Improvement of a phiC31 integrase-based gene delivery system that confers high and continuous transgene expression.</title>
            <link>http://www.medworm.com/index.php?rid=4185783&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21075223%26dopt%3DAbstract</link>
            <description>Authors: Watanabe S, Nakamura S, Sakurai T, Akasaka K, Sato M
    PhiC31 integrase-based gene delivery has been developed. However, the expression of integrated transgenes is often suppressed by a negative position effect. To improve this system, we constructed a new phiC31 integrase-based expression vector that contains attB, an expression unit placed in reverse orientation with two sea urchin-derived Ars-insulators to avoid position effects. In vitro and in vivo transfection experiments revealed that this new system produces higher levels of transgene expression as well as continued gene expression. Thus, the present gene delivery system will facilitate reverse genetics-based molecular biological studies.
    PMID: 21075223 [PubMed - as supplied by publisher] (Source: New Biotechnology)</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4185783</comments>
            <pubDate>Thu, 11 Nov 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4185783</guid>        </item>
        <item>
            <title>Generation of B. nigra-B. rapa chromosome addition stocks: Cytology and microsatellite markers (SSRs) based characterization.</title>
            <link>http://www.medworm.com/index.php?rid=4185782&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21075224%26dopt%3DAbstract</link>
            <description>Authors: Kapoor R, Banga SS, Banga SK, Kaur G
    To improve B. nigra, the B-genome donor for B. juncea through selective introgression of useful variation from A-genome chromosomes, B. nigra-B. rapa chromosome addition stocks were successfully synthesized for the first time. Resynthesized B. juncea was used as B-genome donor species and A-genome addition stocks were developed by hybridizing sesquidiploid plant (ABB) as female using B. nigra as the male parent. Various cycles of backcrossing and/or selfing were utilized to isolate plants carrying addition of three A-genome chromosomes in the background of B. nigra. These chromosome addition stocks were characterized by chromosome counts, pollen and seed fertility and chromosome specific microsatellite (SSRs) markers. The chromosome number ...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4185782</comments>
            <pubDate>Thu, 11 Nov 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4185782</guid>        </item>
        <item>
            <title>Loss of Xenopus tropicalis EMSY causes impairment of gastrulation and upregulation of p53.</title>
            <link>http://www.medworm.com/index.php?rid=4153369&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21056705%26dopt%3DAbstract</link>
            <description>Authors: Rana AA, Roper SJ, Palmer EA, Smith JC
    EMSY interacts directly with BRCA2 and links the BRCA2 pathway to sporadic breast and ovarian cancer. It also interacts with BS69 and HP1b, both of which are involved in chromatin remodeling, and with NIF-1 and DBC-1 in the regulation of nuclear receptor-mediated transcription. Here we investigate the function of EMSY during amphibian development, and in doing so provide the first loss-of-function analysis of this protein. Injection of Xenopus tropicalis embryos with antisense morpholino oligonucleotides targeting XtEMSY impairs gastrulation movements, disrupts dorsal structures, and kills embryos by tailbud stages. Consistent with these observations, regional markers such as Xbra, Chd, Gsc, Shh, Sox3 and Sox17 are downregulated. In contr...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4153369</comments>
            <pubDate>Thu, 04 Nov 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4153369</guid>        </item>
        <item>
            <title>The potential of brewer's spent grain to improve the production of α-amylase by Bacillus sp. KR-8104 in submerged fermentation system.</title>
            <link>http://www.medworm.com/index.php?rid=4107967&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20970528%26dopt%3DAbstract</link>
            <description>Authors: Hashemi M, Shojaosadatic SA, Razavi SH, Mousavi SM
    Brewer's spent grain (BSG) was used as a solid substrate for the production of α-amylase by Bacillus sp. KR-8104 in a submerged fermentation system. The production of α-amylase was maximized through statistical optimization of the BSG concentration and incubation time using the Doehlert experimental design. The highest tested amount of BSG (5% (w/v) in the optimization process resulted in a 5.1 fold enhancement of the response. Subsequently, we studied the role of the water-soluble and -insoluble fractions of BSG on the production of α-amylase. The results revealed that whole BSG had a greater effect on the production of α-amylase than each fraction had separately. Finally, when we examined the potential of BSG to replace ...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4107967</comments>
            <pubDate>Tue, 19 Oct 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4107967</guid>        </item>
        <item>
            <title>A novel organic solvent tolerant protease from a newly isolated Geomicrobium sp. EMB2 (MTCC 10310): Production optimization by response surface methodology.</title>
            <link>http://www.medworm.com/index.php?rid=4107966&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20970529%26dopt%3DAbstract</link>
            <description>Authors: Karan R, Singh SP, Kapoor S, Khare SK
    Thirty eight haloalkaliphilic bacterial strains were isolated from Sambhar Salt Lake, India and screened for their ability to secrete haloalkaliphilic proteases. Among them, a moderately halophilic, mesophilic and alkaliphilic potent strain Geomicrobium sp. EMB2 produced an extracellular protease which was remarkably stable in organic solvents, salt, surfactants, detergents and alkaline pH. Statistically based experimental designs were applied to study the interactions and optimization of medium constituents for efficient protease production by Geomicrobium sp. EMB2. An overall 20-fold increase in protease production was achieved in the optimized medium (721 U/ml) as compared with the unoptimized medium (37 U/ml). The high production level...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4107966</comments>
            <pubDate>Tue, 19 Oct 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4107966</guid>        </item>
        <item>
            <title>Improved Mannan-degrading Enzymes Production by Aspergillus niger through Medium Optimization.</title>
            <link>http://www.medworm.com/index.php?rid=4107965&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20970530%26dopt%3DAbstract</link>
            <description>Authors: Mohamad SN, Ramanan RN, Mohamad R, Ariff AB
    The effect of different carbon and nitrogen sources on the production of mannan-degrading enzymes, focussing on β-mannanase, by Aspergillus niger was investigated using shake flask culture. The β-mannanase activity obtained during growth of A. niger on guar gum (1,495 nkat mL(-1)) was much higher than those observed on other carbon substrates, locust bean gum (1,148 nkat mL(-1)), α-cellulose (10.7 nkat mL(-1)), glucose (8.8 nkat mL(-1)) and carboxymethylcellulose (4.6 nkat mL(-1)). For fermentation using guar gum as a carbon source, bacteriological peptone gave the highest β-mannanase activity (1,744 nkat mL(-1)) followed by peptone from meat (1,168 nkat mL(-1)), yeast extract (817 nkat mL(-1)), ammonium sulphate (241 nkat mL(-1)...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4107965</comments>
            <pubDate>Tue, 19 Oct 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4107965</guid>        </item>
        <item>
            <title>Array comparative genome hybridization in patients with developmental delay: two example cases.</title>
            <link>http://www.medworm.com/index.php?rid=4107968&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20969982%26dopt%3DAbstract</link>
            <description>Authors: Hancarova M, Drabova J, Zmitkova Z, Vlckova M, Hedvicakova P, Novotna D, Vlckova Z, Vejvalkova S, Marikova T, Sedlacek Z
    Developmental delay is often a predictor of mental retardation or autism, two relatively frequent developmental disorders severely affecting intellectual and social functioning. The causes of these conditions remain unknown in most patients. They have a strong genetic component, but the specific genetic defects can only be identified in a fraction of patients. Recent developments in genomics supported the establishment of the causal link between copy number variants in the genomes of some patients and their affection. One of the techniques suitable for this analysis is array comparative genome hybridization, which can be used both for detailed mapping of chr...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4107968</comments>
            <pubDate>Mon, 18 Oct 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4107968</guid>        </item>
        <item>
            <title>&quot;4D Biology for Health and Disease&quot; Workshop Report.</title>
            <link>http://www.medworm.com/index.php?rid=4088456&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20951846%26dopt%3DAbstract</link>
            <description>&quot;4D Biology for Health and Disease&quot; Workshop Report.
    N Biotechnol. 2010 Oct 14;
    Authors: Abrahams JP, Apweiler R, Balling R, Bertero MG, Bujnicki JM, Chayen NE, Chène P, Corthals GL, Dyląg T, Förster F, Heck AJ, Henderson PJ, Herwig R, Jehenson P, Kokalj SJ, Laue E, Legrain P, Martens L, Migliorini C, Musacchio A, Podobnik M, Schertler GF, Schreiber G, Sixma TK, Smit AB, Stuart D, Svergun D, Taussig MJ
    The &quot;4D Biology Workshop for Health and Disease&quot;, held on 16-17(th) of March 2010 in Brussels, aimed at finding the best organising principles for large scale proteomics, interactomics and structural genomics/biology initiatives, and setting the vision for future high throughput research and large-scale data gathering in biological and medical science. Major conclusions of the...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4088456</comments>
            <pubDate>Wed, 13 Oct 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4088456</guid>        </item>
        <item>
            <title>Production of diacylglycerols from glycerol monooleate and ethyl oleate through free and immobilized lipase-catalyzed consecutive reactions.</title>
            <link>http://www.medworm.com/index.php?rid=4088455&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20951847%26dopt%3DAbstract</link>
            <description>Authors: Jin J, Li D, Zhu XM, Adhikari P, Lee KT, Lee JH
    The ability of free and immobilized lipase on production of diacylglycerols (DAG) by transesterification of glycerol monooleate (GMO) and ethyl oleate was investigated. Among three free lipases such as lipase G (Penicillium cyclopium), lipase AK (Pseudomonas fluorescens) and lipase PS (Pseudomonas cepacia), lipase PS exhibited the highest DAG productivity, and the DAG content gradually increased up to 24 hrs reaction and then remained steady. The comparative result for DAG productivity between free lipase PS and immobilized lipases (lipase PS-D and Lipozyme RM IM) during 9 times of 24hours reaction indicated that total DAG production was higher in immobilized lipase PS-D (183.5mM) and Lipozyme RM IM (309.5mM) than free lipase PS ...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4088455</comments>
            <pubDate>Wed, 13 Oct 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4088455</guid>        </item>
        <item>
            <title>Identification of diacylglycerol and triacylglycerol containing 11,12,13-trihydroxy-9,14-octadecadienoic acid in Castor Oil.</title>
            <link>http://www.medworm.com/index.php?rid=4088454&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20951848%26dopt%3DAbstract</link>
            <description>We report here the identification of acylglycerols containing a triOH18:2 fatty acid in castor oil. The structure of this novel fatty acid was proposed as 11,12,13-trihydroxy-9,14-octadecadienoic acid by the mass spectrometry of the lithiated adducts of acylglycerols in the HPLC fractions of castor oil. The fragmentation pathways of the lithiated adduct of 11,12,13-trihydroxy-9,14-octadecadienoic acid were proposed. We also proposed the biosynthetic pathways of polyhydroxy fatty acids in castor.
    PMID: 20951848 [PubMed - as supplied by publisher] (Source: New Biotechnology)</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4088454</comments>
            <pubDate>Wed, 13 Oct 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4088454</guid>        </item>
        <item>
            <title>A novel extracellular protease from Pseudomonas aeruginosa MCM B-327: Enzyme production and its partial characterization.</title>
            <link>http://www.medworm.com/index.php?rid=4088457&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20951241%26dopt%3DAbstract</link>
            <description>Authors: Zambare V, Nilegaonkar S, Kanekar P
    The focus of this study was on production, purification and characterization of dehairing protease by Pseudomonas aeruginosa MCM B-327, isolated from vermicompost pit soil. Optimum protease activity, 395UmL(-1), was observed in the medium containing soyabean meal and tryptone, at pH 7 and 30°C. The crude enzyme exhibited dehairing activity. As compared to chemical method, enzymatic method of dehairing showed reduction in COD, TDS and TSS by 34.28%, 37.32% and 51.58% respectively. Zymogram of crude enzyme on native-PAGE presented two bands with protease activity of molecular weights of 56 and 67kDa. Both proteases showed dehairing activity. Out of these, 56kDa protease (PA02) was purified 3.05-folds with 2.71% recovery. The enzyme was active...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4088457</comments>
            <pubDate>Tue, 12 Oct 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4088457</guid>        </item>
        <item>
            <title>Penicillium oxalicum SAE(M)-51: a mutagenised strain for enhanced production of chitin deacetylase for bioconversion to chitosan.</title>
            <link>http://www.medworm.com/index.php?rid=4062988&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20920617%26dopt%3DAbstract</link>
            <description>Authors: Pareek N, Vivekanand V, Dwivedi P, Singh RP
    A novel chitin deacetylase (CDA) producing strain Penicillium oxalicum ITCC 6965 was isolated from residual materials of sea food processing industries. Strain following mutagenesis using ethidium bromide (EtBr) and microwave irradiation had resulted into a mutant P. oxalicum SAE(M)-51 having improved levels of chitin deacetylase (210.71±1.65Ul(-1)) as compared to the wild type strain (108.26±1.98Ul(-1)). Maximum enzyme production was achieved in submerged fermentation following 144 hours of incubation with notably improved productivity of 1.46±0.82Ul(-1)h(-1) as compared to the wild type strain (0.75±0.53Ul(-1)h(-1)). Scanning electron micrographs of mutant and wild type strains had revealed distinct morphological features. Eval...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4062988</comments>
            <pubDate>Thu, 07 Oct 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4062988</guid>        </item>
        <item>
            <title>Nutritional regulation of protease production by the feather-degrading bacterium Chryseobacterium sp. kr6.</title>
            <link>http://www.medworm.com/index.php?rid=4062987&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20920618%26dopt%3DAbstract</link>
            <description>Authors: Riffel A, Daroit DJ, Brandelli A
    The effects of nutritional conditions on growth and protease production by the feather-degrading Chryseobacterium sp. kr6 were investigated. Higher growth was observed on feather-containing or tryptone (TR) medium when compared to casein (CA) or glucose-nitrogen (GN) base medium. Protease production occurred during growth on feather-containing and TR media, whereas no protease activity was detected on CA or GN medium, indicating that protease production is not constitutive, depending on the presence of specific complex nitrogen sources. Supplementation of whole feathers (WF) medium with glucose (WFG) or NH(4)Cl (WFN) did not result in major differences in growth and protease production, whereas soluble protein was lower in supplemented media. G...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4062987</comments>
            <pubDate>Thu, 07 Oct 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4062987</guid>        </item>
        <item>
            <title>Editorial.</title>
            <link>http://www.medworm.com/index.php?rid=4062983&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20933623%26dopt%3DAbstract</link>
            <description>Authors: Arber W
    
    PMID: 20933623 [PubMed - as supplied by publisher] (Source: New Biotechnology)</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4062983</comments>
            <pubDate>Thu, 07 Oct 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4062983</guid>        </item>
        <item>
            <title>Finding Stable Cellulase and Xylanase: Evaluation of the Synergistic Effect of pH and Temperature.</title>
            <link>http://www.medworm.com/index.php?rid=4062978&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20937420%26dopt%3DAbstract</link>
            <description>Authors: Farinas CS, Loyo MM, Junior AB, Tardioli PW, Neto VB, Couri S
    Ethanol from lignocellulosic biomass has been recognized as one of the most promising alternatives for the production of renewable and sustainable energy. However, one of the major bottlenecks holding back its commercialization is the high costs of the enzymes needed for biomass conversion. In this work, we studied the enzymes produced from a selected strain of Aspergillus niger under solid state fermentation. The cellulase and xylanase enzymatic cocktail was characterized in terms of pH and temperature by using response surface methodology. Thermostability and kinetic parameters were also determined. The statistical analysis of pH and temperature effects on enzymatic activity showed a synergistic interaction of the...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4062978</comments>
            <pubDate>Thu, 07 Oct 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4062978</guid>        </item>
        <item>
            <title>pH catalyzed pretreatment of corn bran for enhanced enzymatic arabinoxylan degradation.</title>
            <link>http://www.medworm.com/index.php?rid=4062984&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20933622%26dopt%3DAbstract</link>
            <description>This study examined the optimization of pretreatment of corn bran for enzymatic hydrolysis through statistic modeling. A low pH pretreatment (pH 2, 150°C, 65min) boosted the enzymatic release of xylose and glucose and maximized biomass solubilization. With more acidic pretreatment followed by enzymatic hydrolysis the total xylose release was maximized (at pH 1.3) reaching ∼50% by weight of the original amount present in destarched corn bran, but the enzyme catalyzed xylose release was maximal at approx. pH 2. The total glucose release peaked at pretreatment of approx. pH 1.5 with an enzymatic release of approx. 68% by weight of the original amounts present in destarched corn bran. For arabinose the enzymatic release was negatively affected by the acidic pretreatment as labile arabinosyl...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4062984</comments>
            <pubDate>Tue, 05 Oct 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4062984</guid>        </item>
        <item>
            <title>Involvement of low molecular mass soluble acyl-CoA-binding protein in seed oil biosynthesis.</title>
            <link>http://www.medworm.com/index.php?rid=4062981&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20933624%26dopt%3DAbstract</link>
            <description>Authors: Yurchenko OP, Weselake RJ
    Acyl-CoA-binding protein (ACBP), a low molecular mass (m) (∼10kDa) soluble protein ubiquitous in eukaryotes, plays an important housekeeping role in lipid metabolism by maintaining the intracellular acyl-CoA pool. ACBP has been shown to be involved in lipid biosynthesis and transport, gene expression, and membrane biogenesis. In plants, low m ACBP and high m ACBPs participate in response mechanisms to biotic and abiotic factors, acyl-CoA transport in phloem, and biosynthesis of structural and storage lipids. In light of current research on modification of seed oil, an insight into mechanisms of substrate trafficking within lipid biosynthetic pathways is crucial for developing rational strategies for the production of specialty oils with the desired ...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4062981</comments>
            <pubDate>Tue, 05 Oct 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4062981</guid>        </item>
        <item>
            <title>Expression of anti-sclerotinia scFv in transgenic B. napus enhances tolerance against stem rot.</title>
            <link>http://www.medworm.com/index.php?rid=4062985&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20933110%26dopt%3DAbstract</link>
            <description>The objective of the current study was to generate recombinant pathogen specific antibody (scFv)-expressing transgenic Brassica napus plants with increased tolerance to the phytopathogenic fungus, Sclerotinia sclerotiorum. Transgenic canola (B. napus) lines expressing S. sclerotiorum-specific scFv antibody showed a significant level of tolerance towards S. sclerotiorum as compared to their non-transformed counterparts. Both incidence and progression of S. sclerotiorum-induced disease symptoms were reduced in plants expressing the recombinant scFv.
    PMID: 20933110 [PubMed - as supplied by publisher] (Source: New Biotechnology)</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4062985</comments>
            <pubDate>Mon, 04 Oct 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4062985</guid>        </item>
        <item>
            <title>Purification and Characterization of Intracellular Lipase from the Polyunsaturated Fatty Acid-Producing Fungus Mortierella alliacea.</title>
            <link>http://www.medworm.com/index.php?rid=4062986&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20932946%26dopt%3DAbstract</link>
            <description>Authors: Jermsuntiea W, Aki T, Toyoura R, Iwashita K, Kawamoto S, Ono K
    Previous studies on an arachidonic acid-producing fungus, Mortierella alliacea YN-15, suggested that its intracellular lipase plays an important role in the metabolism of exogenous and storage lipids. The lipase purified in this study through acetone precipitation and three-step chromatography was estimated to be about 11 kDa in size by SDS-PAGE and mass spectrometry, and it tended to form large aggregates in aqueous solution. The purified lipase retained its activity over wide ranges of pH (2-12) and temperature (20-80°C). Its activity was enhanced by the Ca(2+) ion and reduced by some heavy metal ions, such as Zn(2+) and Hg(2+), and diethylpyrocarbonate. Among the various substrates tested, monoacylglycerols con...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4062986</comments>
            <pubDate>Sun, 03 Oct 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4062986</guid>        </item>
        <item>
            <title>Strategies to identify microRNA targets: New advances.</title>
            <link>http://www.medworm.com/index.php?rid=4062989&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20888440%26dopt%3DAbstract</link>
            <description>Authors: Jin H, Tuo W, Lian H, Liu Q, Zhu XQ, Gao H
    MicroRNAs (miRNAs) are small regulatory RNA molecules functioning to modulate gene expression at the post-transcriptional level, and playing an important role in many developmental and physiological processes. Ten thousand miRNAs have been discovered in various organisms. Although considerable progress has been made in computational methodology to identify miRNA targets, most predicted miRNA targets may be false positive. Due to the lack of effective tools to identify miRNA targets, the study of miRNAs is seriously retarded. In recent years, some molecular cloning strategies of miRNA targets have been developed, including RT-PCR using miRNAs as endogenous primers, labeled miRNA pull-down assay (LAMP) and RNA ligase-mediated amplificat...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4062989</comments>
            <pubDate>Thu, 30 Sep 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4062989</guid>        </item>
        <item>
            <title>Biochemical monitoring in fenugreek to develop functional food and medicinal plant variants.</title>
            <link>http://www.medworm.com/index.php?rid=4003606&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20851781%26dopt%3DAbstract</link>
            <description>Authors: Thomas JE, Bandara M, Lee EL, Driedger D, Acharya S
    Many plants used as functional foods or for medicinal purposes have been criticized for their inconsistent physiological effects. Variation in genotype and environmental conditions under which plants are produced can contribute to this inconsistency in biochemical composition. Fenugreek (Trigonella foenum-graecum L.) is a medicinal plant that not only can lower blood glucose and cholesterol levels in animals, but also can be used as a forage crop for livestock feed. Seed content for the bioactive compounds diosgenin, galactomannan and 4-hydroxyisoleucine was characterized for ten fenugreek genotypes under rainfed and irrigated conditions. High and low seed yielding genotype/environment combinations were identified that posses...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4003606</comments>
            <pubDate>Mon, 20 Sep 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4003606</guid>        </item>
        <item>
            <title>Ethical arguments relevant to the use of GM crops.</title>
            <link>http://www.medworm.com/index.php?rid=4003968&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20850572%26dopt%3DAbstract</link>
            <description>Authors: Weale A
    The Nuffield Council on Bioethics (NCOB) has published two reports (1999 and 2004) on the social and ethical issues involved in the use of genetically modified crops. This presentation summarises their core ethical arguments. Five sets of ethical concerns have been raised about GM crops: potential harm to human health; potential damage to the environment; negative impact on traditional farming practice; excessive corporate dominance; and the 'unnaturalness' of the technology. The NCOB examined these claims in the light of the principle of general human welfare, the maintenance of human rights and the principle of justice. It concluded in relation to the issue of 'unnaturalness' that GM modification did not differ to such an extent from conventional breeding that it is ...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4003968</comments>
            <pubDate>Thu, 16 Sep 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4003968</guid>        </item>
        <item>
            <title>Cell free expression put on the spot: advances in repeatable protein arraying from DNA (DAPA).</title>
            <link>http://www.medworm.com/index.php?rid=4003900&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20850573%26dopt%3DAbstract</link>
            <description>Authors: Stoevesandt O, Vetter M, Kastelic D, Palmer EA, He M, Taussig MJ
    We have previously described the 'DNA array to protein array' (DAPA) method for microarraying of proteins expressed by cell-free systems in situ on the array surface. In this technique, a DNA array on one slide acts as the template for generating a protein array on a second slide, mediated by a cell free lysate between the two juxtaposed slides. Here we explore the feature of the repeatability of the technology, in which the same DNA array is reused several times, and use the method to generate a microarray of over 120 diverse proteins. The capabilities of DAPA technology in comparison with other protein array methods are discussed.
    PMID: 20850573 [PubMed - as supplied by publisher] (Source: New Biotechnology...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4003900</comments>
            <pubDate>Thu, 16 Sep 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4003900</guid>        </item>
        <item>
            <title>Isolation and characterization of temperature and alkaline stable bioflocculant from Agrobacterium sp. M-503.</title>
            <link>http://www.medworm.com/index.php?rid=4004076&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20849992%26dopt%3DAbstract</link>
            <description>Authors: Li Q, Liu HL, Qi QS, Wang FS, Zhang YZ
    A bacterium isolated from activated sludge of propylene epoxide wastewater was identified as Agrobacterium sp. M-503. It was confirmed to produce bioflocculant with excellent flocculation activity. The yield of the bioflocculant reached 14.9g/l in batch cultivation with a carbon source conversion of 74.5%. This bioflocculant was temperature and alkaline stable, retaining almost all flocculation activity after being treated at 121Â°C for 20 minutes or at pH 12.0. It consisted of neutral sugar, uronic acid, aminosugar and protein in weight ratios of 85.0:9.9:2.1:3.0. The active polysaccharide fraction of the bioflocculant was purified to homogeneity by ethanol precipitation, DEAE ion-exchange and gel chromatography. Analysis of the purifi...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4004076</comments>
            <pubDate>Wed, 15 Sep 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4004076</guid>        </item>
        <item>
            <title>Purification and biochemical characterization of a nattokinase by conversion of shrimp shell with Bacillus subtilis TKU007.</title>
            <link>http://www.medworm.com/index.php?rid=4004024&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20849993%26dopt%3DAbstract</link>
            <description>Authors: Wang SL, Wu YY, Liang TW
    BSN1, a nattokinase, was purified from the culture supernatant of Bacillus subtilis TKU007 with shrimp shell wastes as the sole carbon/nitrogen source. The BSN1 was purified to homogeneity by three-step procedure with a 515-fold increase in specific activity and 12% recovery. The molecular masses of BSN1 determined by SDS-PAGE and gel filtrations were approximately 30kDa and 28kDa, respectively. The results of peptide mass mapping showed that four tryptic peptides of BSN1 were identical to the nattokinase from B. subtilis (GenBank accession number gi14422313) with 37% sequence coverage. The N-terminal amino acid sequence of the first 12 amino acids of BSN1 was AQSVPYGISQIK. The optimum pH, optimum temperature, pH stability, and thermal stability of BSN...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
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            <pubDate>Wed, 15 Sep 2010 23:00:00 +0100</pubDate>
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            <title>Assessment of Protein Domain Fusions in Human Protein Interaction Networks Prediction: application to the human kinetochore model.</title>
            <link>http://www.medworm.com/index.php?rid=4003828&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20851221%26dopt%3DAbstract</link>
            <description>Authors: Morilla I, Lees JG, Reid AJ, Orengo C, Ranea JA
    In order to understand how biological systems function it is necessary to determine the interactions and associations between proteins. Some proteins, involved in a common biological process and encoded by separate genes in one organism, can be found fused within a single protein chain in other organisms. By detecting these triplets, a functional relationship can be established between the un-fused proteins. Here we use a domain fusion prediction method to predict these protein interactions for the human interactome. We observed that gene fusion events are more related to physical interaction between proteins than to other weaker functional relationships such as participation in a common biological pathway. These results suggest ...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
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            <pubDate>Wed, 15 Sep 2010 23:00:00 +0100</pubDate>
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            <title>Development and evaluation of data-driven designed tags (DDTs) for controlling protein solubility.</title>
            <link>http://www.medworm.com/index.php?rid=3973432&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20837175%26dopt%3DAbstract</link>
            <description>Authors: Hirose S, Kawamura Y, Mori M, Yokota K, Noguchi T, Goshima N
    Production of proteins is an important issue in protein science and pharmaceutical studies. Numerous protein expression systems using living cells and cell-free methods have been developed to date. In these systems, a promising strategy for improving the success rate of obtaining soluble proteins is the attachment of various tags into target proteins based on empirical rules. This paper presents a method for production of data-driven designed tags (DDTs) based on highly frequent sequence property patterns in an experimentally assessed protein solubility dataset in a wheat germ cell-free system. We constructed seven proteins combined with 12 kinds of DDTs (six for enhancing solubility and six for insolubility) at the ...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3973432</comments>
            <pubDate>Thu, 09 Sep 2010 23:00:00 +0100</pubDate>
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            <title>In Vitro Protein Expression: An Emerging Alternative to Cell-Based Approaches.</title>
            <link>http://www.medworm.com/index.php?rid=3934085&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20804874%26dopt%3DAbstract</link>
            <description>Authors: He M
    Protein expression remains a bottleneck in the production of proteins. Due to a number of advantages, cell-free translation is emerging as an alternative to cell-based methods for generation of proteins. Recent advances have led to many novel applications of cell-free systems in biotechnology, proteomics and fundamental biological research. This special issue of New Biotechnology describes recent advances in cell free protein expression systems and their applications.
    PMID: 20804874 [PubMed - as supplied by publisher] (Source: New Biotechnology)</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3934085</comments>
            <pubDate>Thu, 26 Aug 2010 23:00:00 +0100</pubDate>
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            <title>Challenges and Responsibilities for Public Sector Scientists.</title>
            <link>http://www.medworm.com/index.php?rid=3915806&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20800704%26dopt%3DAbstract</link>
            <description>Authors: Van Montagu M
    Current agriculture faces the challenge of doubling food production to meet the food needs of a population expected to reach 9 billion by mid-century while maintaining soil and water quality and conserving biodiversity. These challenges are more overwhelming for the rural poor, who are the custodians of environmental resources and at the same time particularly vulnerable to environmental degradation. Solutions have to come from concerted actions by different segments of society in which public sector science plays a fundamental role. Public sector scientists are at the root of all the present generation of GM crop traits under cultivation and more will come with the new knowledge that is being generated by systems biology. To speed up innovation, molecular biolog...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3915806</comments>
            <pubDate>Tue, 24 Aug 2010 23:00:00 +0100</pubDate>
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            <title>Wheat germ cell-free protein production system for post-genomic research.</title>
            <link>http://www.medworm.com/index.php?rid=3915805&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20800705%26dopt%3DAbstract</link>
            <description>Authors: Madono M, Sawasaki T, Morishita R, Endo Y
    Genomic information becomes useful knowledge only when the structures and functions of gene products are understood. In spite of a vast array of analytical tools developed for biological studies in recent years, producing proteins at will is still a bottleneck in post-genomic studies. The cell-free protein production system we developed using wheat embryos has enabled us to produce high quality proteins for genome-wide functional and structural analyses and at the same time circumvent almost all the limitations, such as biohazards and costs, that have hampered conventional cell-free protein synthesis systems. In the present article, we introduce examples of our new wheat germ cell-free protein production system and its application to f...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3915805</comments>
            <pubDate>Tue, 24 Aug 2010 23:00:00 +0100</pubDate>
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            <title>In the cauldron of cell-free synthesis of membrane proteins: playing with new surfactants.</title>
            <link>http://www.medworm.com/index.php?rid=3915804&amp;cid=s_37002_70_f&amp;fid=37002&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20800706%26dopt%3DAbstract</link>
            <description>Authors: Park KH, Billon-Denis E, Dahmane T, Lebaupain F, Pucci B, Breyton C, Zito F
    Cell-free protein synthesis is a well-known technique for the roles it has played in deciphering the genetic code and in the beginnings of signal sequence studies. Since then, many efforts have been made to optimise this technique and, recently, to adapt it to membrane protein production with yields compatible with structural investigations. The versatility of the method allows membrane proteins to be obtained directly stabilised in surfactant micelles or inserted in a lipidic environment (proteoliposome, bicelle, nanodisc) at the end of synthesis. Among the surfactants used, non-detergent ones such as fluorinated surfactants proved to be a good alternative in terms of colloidal stability and preservat...</description>
            <author>New Biotechnology</author>
            <type>journals</type>
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            <pubDate>Tue, 24 Aug 2010 23:00:00 +0100</pubDate>
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