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        <title>Microbial Cell Factories 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 'Microbial Cell Factories' source.</description>
        <link><![CDATA[http://www.medworm.com/rss/search.php?qu=Microbial+Cell+Factories&t=Microbial+Cell+Factories&s=Search&f=source]]></link>
        <lastBuildDate>Mon, 06 Feb 2012 21:32:18 +0100</lastBuildDate>
        <item>
            <title>IcsA autotransporter passenger promotes increased fusion protein expression on the cell surface</title>
            <link>http://www.medworm.com/index.php?rid=5664674&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F11%2F1%2F20</link>
            <description>Conclusions:
The export mechanism of autotransporters is not well understood but accumulating evidence suggest a critical role for the native effector or alpha domain in facilitating its own export via interactions with the translocation or beta domain. This is the first report directly comparing expression of heterologous proteins fused to the full length IcsA autotransporter and fusion to the beta domain alone. Protein expression and surface presentation of the fusion proteins were dramatically improved when fused to IcsA rather than IcsAbeta. Future studies involved in designing autotransporters as cell surface display vehicles would benefit from including the native alpha domain. This work also provides further evidence for a key interaction between the autotransporter alpha and beta d...</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5664674</comments>
            <pubDate>Tue, 07 Feb 2012 02:08:30 +0100</pubDate>
            <guid isPermaLink="false">5664674</guid>        </item>
        <item>
            <title>A strategy of gene overexpression based on tandem repetitive promoters in Escherichia coli</title>
            <link>http://www.medworm.com/index.php?rid=5664675&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F11%2F1%2F19</link>
            <description>Conclusions:
The transcription strength of the MCPtacs promoter cluster can be greatly improved by increasing the tandem repeats number of the core-tac-promoter. By integrating the desired gene together with the MCPtacs promoter cluster into the chromosome of E. coli, we can achieve high and stale overexpression with only a small size. This strategy has an application potential in many fields and can be extended to other bacteria. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5664675</comments>
            <pubDate>Mon, 06 Feb 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5664675</guid>        </item>
        <item>
            <title>Deciphering the role of Paenibacillus strain Q8 in the organic matter recycling in the acid mine drainage of Carnoules</title>
            <link>http://www.medworm.com/index.php?rid=5657256&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F11%2F1%2F16</link>
            <description>Conclusions:
AMDs have been studied for years especially with regard to interactions between bacteria and the inorganic compartment hosting them. To date, no study reported the role of microorganisms in the recycling of the organic matter. The present work suggests that the strain Q8 might play an important role in the community by recycling the scarce organic matter (cellulose, hemicellulose, starch...), especially when the conditions change. Furthermore, function-based screening of a Q8 DNA library allowed to assign an amylolytic function to a gene previously unknown. AMDs could be considered as a reservoir of genes with potential biotechnological properties. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5657256</comments>
            <pubDate>Fri, 03 Feb 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5657256</guid>        </item>
        <item>
            <title>Transcriptome profiling of a curdlan-producing Agrobacterium reveals conserved regulatory mechanisms of exopolysaccharide biosynthesis</title>
            <link>http://www.medworm.com/index.php?rid=5657255&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F11%2F1%2F17</link>
            <description>Conclusions:
This study identifies several mechanisms regulating the synthesis of curdlan, an EPS with numerous applications. These mechanisms are potential metabolic engineering targets for improving the industrial production of curdlan from Agrobacterium sp. ATCC 31749. Furthermore, many of the genes identified in this study are highly conserved across microbial genomes, and we propose that the molecular elements identified in this study may serve as universal regulators of microbial EPS synthesis. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5657255</comments>
            <pubDate>Fri, 03 Feb 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5657255</guid>        </item>
        <item>
            <title>Starmerella bombicola influences the metabolism of Saccharomyces cerevisiae at pyruvate decarboxylase and alcohol dehydrogenase level during mixed wine fermentation</title>
            <link>http://www.medworm.com/index.php?rid=5657254&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F11%2F1%2F18</link>
            <description>Conclusion:
In mixed fermentation, S. bombicola immobilized cells greatly affected the fermentation behavior of S. cerevisiae and the analytical composition of wine. The influence of S. bombicola on S. cerevisiae was not limited to a simple additive contribution. Indeed, its presence caused metabolic modifications during S. cerevisiae fermentation causing variation in the gene expression and enzymatic activity of alcohol deydrogenase and pyruvate decarboxilase. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5657254</comments>
            <pubDate>Fri, 03 Feb 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5657254</guid>        </item>
        <item>
            <title>The major secreted protein Msp1/p75 is O-glycosylated in Lactobacillus rhamnosus GG</title>
            <link>http://www.medworm.com/index.php?rid=5657257&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F11%2F1%2F15</link>
            <description>Conclusions:
In this study we have provided the first evidence of protein O-glycosylation in the probiotic L rhamnosus GG. The major secreted protein Msp1 is glycosylated with a ConA reactive glycan at the serine residues at 106 and 107. Glycosylation is not required for the peptidoglycan hydrolase activity of Msp1 nor for Akt activation capacity in epithelial cells, but appears to be important for its stability and protection against proteases. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5657257</comments>
            <pubDate>Wed, 01 Feb 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5657257</guid>        </item>
        <item>
            <title>One-step generation of error-prone PCR libraries using Gateway(R) technology</title>
            <link>http://www.medworm.com/index.php?rid=5657258&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F11%2F1%2F14</link>
            <description>Conclusions:
The one-step method enables producing epPCR libraries of as high complexity and quality as does the regular, two-step, protocol for half the amount of work. In addition, it contributes to preserve the original complexity of the epPCR product. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5657258</comments>
            <pubDate>Mon, 30 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5657258</guid>        </item>
        <item>
            <title>Exploiting the Campylobacter jejuni protein glycosylation system for glycoengineering vaccines and diagnostic tools directed against brucellosis</title>
            <link>http://www.medworm.com/index.php?rid=5636022&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F11%2F1%2F13</link>
            <description>Conclusion:
Bacterial engineered glycoproteins show promising applications for the development on an array of diagnostics and immunoprotective opportunities in the future. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5636022</comments>
            <pubDate>Wed, 25 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5636022</guid>        </item>
        <item>
            <title>Combined effects of agitation and aeration on the chitinolytic enzymes production by the Antarctic fungus Lecanicillium muscarium CCFEE 5003</title>
            <link>http://www.medworm.com/index.php?rid=5625307&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F11%2F1%2F12</link>
            <description>Conclusions:
This work demonstrated the attitude of L. muscarium CCFEE 5003 to grow in bench-top bioreactor; outlined the strong influence of aeration and agitation on its growth and enzyme production and identified the optimal conditions for possible production at the industrial level. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5625307</comments>
            <pubDate>Mon, 23 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5625307</guid>        </item>
        <item>
            <title>Low-mutation-rate, reduced-genome Escherichia coli: An improved host for faithful maintenance of engineered genetic constructs</title>
            <link>http://www.medworm.com/index.php?rid=5617570&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F11%2F1%2F11</link>
            <description>Conclusions:
By eliminating stress-inducible error-prone DNA-polymerases, the genome of the mobile genetic element-free E. coli strain MDS42 was further stabilized. The resulting strain represents an improved host in various synthetic and molecular biological applications, allowing more stable production of growth-inhibiting biomolecules. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5617570</comments>
            <pubDate>Fri, 20 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5617570</guid>        </item>
        <item>
            <title>Small surfactant-like peptides can drive soluble proteins into active aggregates</title>
            <link>http://www.medworm.com/index.php?rid=5604550&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F11%2F1%2F10</link>
            <description>Conclusions:
This study shows that the surfactant-like peptides L6KD and it derivatives can act as a pull-down handler for converting soluble proteins into active aggregates, much like 18A and ELK16. These peptide-mediated protein aggregations might have important implications for protein aggregation in vivo, and can be explored for production of functional biopolymers with detergent or other interfacial activities. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5604550</comments>
            <pubDate>Wed, 18 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5604550</guid>        </item>
        <item>
            <title>Robust, small-scale cultivation platform for Streptomyces coelicolor</title>
            <link>http://www.medworm.com/index.php?rid=5604551&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F11%2F1%2F9</link>
            <description>Conclusion:
We observed good agreement of the physiological data obtained in the developed MTP platform with bench-scale. Hence, the described MTP-based screening platform has a high potential for investigation of secondary metabolite biosynthesis in Streptomycetes and other filamentous bacteria and the use may significantly reduce the workload and costs. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5604551</comments>
            <pubDate>Tue, 17 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5604551</guid>        </item>
        <item>
            <title>Extracellular Overexpression of Recombinant Thermobifida fusca cutinase by Alpha-hemolysin Secretion System in E. coli BL21(DE3)</title>
            <link>http://www.medworm.com/index.php?rid=5594078&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F11%2F1%2F8</link>
            <description>Conclusions:
In the present study, T. fusca cutinase was successfully secreted to the culture media by alpha-hemolysin secretion system. This is the first report of cutinase being efficiently secreted by this pathway. Due to the limited cases of successful expression of industrial enzyme by E. coli alpha-hemolysin secretion system, our study further explored the utilization of this pathway in industrial enzymes. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5594078</comments>
            <pubDate>Thu, 12 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5594078</guid>        </item>
        <item>
            <title>Host cell and expression engineering for development of an E. coli ketoreductase catalyst: Enhancement of formate dehydrogenase activity for regeneration of NADH</title>
            <link>http://www.medworm.com/index.php?rid=5594079&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F11%2F1%2F7</link>
            <description>Conclusions:
Expression engineering of C. boidinii FDH is an important strategy to optimize E. coli whole-cell reductase catalysts that employ intracellular formate oxidation for regeneration of NADH. Increased FDH-activity was reflected by higher reduction yields of D-xylose and o-chloroacetophenone conversions provided that mass transfer limitations were overcome. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5594079</comments>
            <pubDate>Wed, 11 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5594079</guid>        </item>
        <item>
            <title>Casein phosphopeptides drastically increase secretion of extracellular proteins in Aspergillus awamori. Proteomics studies reveal changes in the secretory pathway</title>
            <link>http://www.medworm.com/index.php?rid=5594081&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F11%2F1%2F5</link>
            <description>Conclusions:
In summary, CPPs cause a reprogramming of cellular metabolism leading to massive secretion of extracellular proteins. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5594081</comments>
            <pubDate>Tue, 10 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5594081</guid>        </item>
        <item>
            <title>A novel expression system for production of soluble prion proteins in E.coli</title>
            <link>http://www.medworm.com/index.php?rid=5594080&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F11%2F1%2F6</link>
            <description>Expression of eukaryotic proteins in Escherichia coli is challenging, especially when they contain disulfide bonds. Since the discovery of the prion protein (PrP) and its role in transmissible spongiform encephalopathies, the need to obtain large quantities of the recombinant protein for research purposes has been essential. Currently, production of recombinant PrP is achieved by refolding protocols. Here, we show that the co-expression of two different PrP with the human Quiescin Sulfhydryl OXidase (QSOX), a human chaperone with thiol/disulfide oxidase activity, in the cytoplasm of E. coli produces soluble recombinant PrP. The structural integrity of the soluble PrP has been confirmed by nuclear magnetic resonance spectroscopy, demonstrating that properly folded PrP can be easily expresse...</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5594080</comments>
            <pubDate>Tue, 10 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5594080</guid>        </item>
        <item>
            <title>Engineered Trx2p industrial yeast strain protects glycolysis and fermentation proteins from oxidative carbonylation during biomass propagation</title>
            <link>http://www.medworm.com/index.php?rid=5577125&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F11%2F1%2F4</link>
            <description>Conclusions:
The identified proteins suggest that the fermentative capacity detriment observed under industrial conditions in T73 wine commercial strain results from the oxidative carbonylation of specific glycolytic and fermentation enzymes. Indeed, increased thioredoxin levels enhance the performance of key fermentation enzymes such as Adh1p, which consequently increases fermentative capacity. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5577125</comments>
            <pubDate>Mon, 09 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5577125</guid>        </item>
        <item>
            <title>The new pLAI (lux regulon based auto-inducible) expression system for recombinant protein production in Escherichia coli</title>
            <link>http://www.medworm.com/index.php?rid=5569750&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F11%2F1%2F3</link>
            <description>Conclusion:
Coupling gene expression to cell density using cell-to-cell communication provides a promising approach for recombinant protein production. The system allows the control of expression of the target recombinant gene independently from external inducers or drastic changes in metabolic conditions and enabling tight regulation of expression . (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5569750</comments>
            <pubDate>Thu, 05 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5569750</guid>        </item>
        <item>
            <title>Improved production of biohydrogen in light-powered Escherichia coli by co-expression of proteorhodopsin and heterologous hydrogenase</title>
            <link>http://www.medworm.com/index.php?rid=5569751&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F11%2F1%2F2</link>
            <description>Conclusion:
Here, we report for the first time the potential application of proteorhodopsin for the production of biohydrogen, a promising alternative fuel. We showed that H2 production was enhanced by the co-expression of proteorhodopsin and [NiFe]-hydrogenase in recombinant E. coli BL21(DE3) in a light intensity-dependent manner. These results demonstrate that E. coli can be applied as light-powered cell factories for biohydrogen production by introducing proteorhodopsin. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5569751</comments>
            <pubDate>Wed, 04 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5569751</guid>        </item>
        <item>
            <title>Laboratory evolution of copper tolerant yeast strains</title>
            <link>http://www.medworm.com/index.php?rid=5569752&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F11%2F1%2F1</link>
            <description>Conclusions:
Following evolution, both Candida and Saccharomyces cells were able to proliferate up to 2.5 g * L-1 CuSO4 and to accumulate high amounts of intracellular copper. The comparison of yeasts differing in their robustness, allowed highlighting physiological and molecular determinants of natural and acquired copper tolerance. We observed that different mechanisms contribute to confer metal tolerance: the control of copper uptake, changes in the levels of enzymes involved in oxidative stress response and changes in the copper-binding proteome. However, copper elicits different physiological and molecular reactions in yeasts with different backgrounds. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5569752</comments>
            <pubDate>Tue, 03 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5569752</guid>        </item>
        <item>
            <title>Heterologous expression of Pycnoporus cinnabarinus cellobiose dehydrogenase in Pichia pastoris and involvement in saccharification processes</title>
            <link>http://www.medworm.com/index.php?rid=5550307&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F113</link>
            <description>Conclusions:
We demonstrate that CDH offers an attractive tool for saccharification process enhancement due to gluconic acid production from raw lignocellulosic material. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5550307</comments>
            <pubDate>Wed, 28 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5550307</guid>        </item>
        <item>
            <title>Comparative one-factor-at-a-time, response surface (statistical) and bench-scale bioreactor level optimization of thermoalkaline protease production from a psychrotrophic Pseudomonas putida SKG-1 isolate</title>
            <link>http://www.medworm.com/index.php?rid=5550306&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F114</link>
            <description>Conclusions:
The optimization of fermentation variables using conventional, statistical approaches and aeration/agitation at fermentor level resulted in ~13.5 folds increase (882 Uml-1) in protease production compared to un-optimized conditions (65 Uml-1). This is the highest level of thermoalkaline protease reported so far by any psychrotrophic bacterium. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5550306</comments>
            <pubDate>Wed, 28 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5550306</guid>        </item>
        <item>
            <title>The order of expression is a key factor in the production of active transglutaminase in Escherichia coli by co-expression with its pro-peptide</title>
            <link>http://www.medworm.com/index.php?rid=5534297&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F112</link>
            <description>Conclusions:
Our results indicated that the pro-peptide can assist correct folding of the TGase inter-molecularly in E. coli, and expression of pro-peptide prior to that of TGase was essential for the production of active TGase. The co-expression strategy based on optimizing the order of gene expression could be useful for the expression of other functional proteins that are synthesized as a precursor. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5534297</comments>
            <pubDate>Fri, 23 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5534297</guid>        </item>
        <item>
            <title>Reassessment of hydrogen tolerance in Caldicellulosiruptor saccharolyticus</title>
            <link>http://www.medworm.com/index.php?rid=5534298&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F111</link>
            <description>Conclusion:
C. saccharolyticus is able to grow and produce hydrogen at high PH2, hence eliminating the need of gas sparging in its cultures. Under this condition, it has a unique ability to fine tune its metabolism by maintaining the glycolytic flux through regulating GAPDH activity and redistribution of pyruvate flux. Concerning the later, xylose-rich feedstock should be preferred over the sucrose-rich one for better H2 yield. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5534298</comments>
            <pubDate>Wed, 21 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5534298</guid>        </item>
        <item>
            <title>The O-mannosylation and production of recombinant APA (45/47 KDa) protein from Mycobacterium tuberculosis in Streptomyces lividans is affected by culture conditions in shake flasks</title>
            <link>http://www.medworm.com/index.php?rid=5520962&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=%24%7Bitem.link%7D</link>
            <description>Conclusions:
The shear and/or oxygenation parameters determine the bacterial morphology, the productivity, and the O-mannosylation of rAPA in S. lividans. As demonstrated here, culture conditions have to be carefully controlled in order to obtain recombinant O-glycosylated proteins with similar &quot;quality&quot; in bacteria, particularly, if the protein activity depends on the glycosylation pattern. Furthermore, it will be an interesting exercise to determine the effect of shear and oxygen in shake flasks, to obtain evidences that may be useful in scaling-up these processes to bioreactors. Another approach will be using lab-scale bioreactors under well-controlled conditions, and study the impact those on rAPA productivity and quality. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5520962</comments>
            <pubDate>Tue, 20 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5520962</guid>        </item>
        <item>
            <title>Production in yeast of pseudotype virus-like particles harboring functionally active antibody fragments neutralizing the cytolytic activity of vaginolysin</title>
            <link>http://www.medworm.com/index.php?rid=5513027&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F109</link>
            <description>Conclusions:
Recombinant scFv-Fc proteins were expressed in yeast with low efficiency. New approach to display the scFv-Fc molecules on the surface of pseudotype VLPs was successful and allowed generation of multivalent scFv-Fc proteins with high VLY-neutralizing potency. Our study demonstrated for the first time that large recombinant antibody molecule fused with hamster polyomavirus VP2 protein and co-expressed with VP1 protein in the form of pseudotype VLPs was properly folded and exhibited strong antigen-binding activity. The current study broadens the potential of recombinant VLPs as a highly efficient carrier for functionally active complex proteins. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5513027</comments>
            <pubDate>Thu, 15 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5513027</guid>        </item>
        <item>
            <title>A novel cold-active beta-D-galactosidase from the  Paracoccus sp. 32d - gene cloning, purification and characterization</title>
            <link>http://www.medworm.com/index.php?rid=5501820&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F108</link>
            <description>Conclusions:
A novel bgaL gene was isolated from Paracoccus sp. 32d encoded a novel cold-active beta-D-galactosidase. An E. coli expression system has enabled efficient production of soluble form of BgaL Paracoccus sp. 32d. The amino acid sequence analysis of the BgaL enzyme revealed notable differences in comparison to the result of the amino acid sequences analysis of well-characterized cold-active beta-D-galactosidases belonging to Glycoside Hydrolase Family 2. Finally, the enzymatic properties of Paracoccus sp. 32d beta-D-galactosidase shows its potential for being applied to development of a new industrial biocatalyst for efficient lactose hydrolysis in milk. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5501820</comments>
            <pubDate>Tue, 13 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5501820</guid>        </item>
        <item>
            <title>Heterologous overexpression of Glomerella cingulata FAD-dependent glucose dehydrogenase in Escherichia coli and Pichia pastoris</title>
            <link>http://www.medworm.com/index.php?rid=5501822&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F106</link>
            <description>Conclusions:
The heterologous expression of active GDH was greatly favoured in the eukaryotic host. The efficient expression in P. pastoris facilitates the production of genetically engineered GDH variants for electrochemical-, physiological- and structural studies. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5501822</comments>
            <pubDate>Mon, 12 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5501822</guid>        </item>
        <item>
            <title>High-yield production of biologically active recombinant protein in shake flask culture by combination of enzyme-based glucose delivery and increased oxygen transfer</title>
            <link>http://www.medworm.com/index.php?rid=5501821&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F107</link>
            <description>This report describes the combined use of an enzyme-based glucose release system (EnBase(R)) and high-aeration shake flask (Ultra Yield FlaskTM). The benefit of this combination is demonstrated by over 100-fold improvement in the active yield of recombinant alcohol dehydrogenase expressed in E. coli. Compared to Terrific Broth and ZYM-5052 autoinduction medium, the EnBase system improved yield mainly through increased productivity per cell. Four-fold increase in oxygen transfer by the Ultra Yield Flask contributed to higher cell density with EnBase but not with the other tested media, and consequently the product yield per ml of EnBase culture was further improved. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5501821</comments>
            <pubDate>Mon, 12 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5501821</guid>        </item>
        <item>
            <title>Enhanced expression of membrane proteins in E. coli with a PBAD promoter mutant: synergies with chaperone pathway engineering strategies</title>
            <link>http://www.medworm.com/index.php?rid=5493038&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F105</link>
            <description>Conclusions:
Our system, which combines a downregulated version of the tightly repressed PBAD promoter with a TF-deficient host may prove a valuable alternative to T7-based expression for the production of membrane proteins that have so far remained elusive targets. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5493038</comments>
            <pubDate>Fri, 09 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5493038</guid>        </item>
        <item>
            <title>The Impact of Phosphate Scarcity on Pharmaceutical Protein Production in S. cerevisiae: Linking Transcriptomic Insights to Phenotypic Responses</title>
            <link>http://www.medworm.com/index.php?rid=5483946&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F104</link>
            <description>Conclusions:
Our study underlines the dynamic character of adaptive responses of cells towards a change in their nutrient access. The gradual decrease of the phosphate supply resulted in a step-wise modulated phenotypic response, thereby alternating the specific productivity and the secretory flux. Our work emphasizes the importance of reduced phosphate supply for improved secretory production of heterologous proteins. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5483946</comments>
            <pubDate>Wed, 07 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5483946</guid>        </item>
        <item>
            <title>A thermostable GH45 endoglucanase from yeast: impact of its atypical multimodularity on activity</title>
            <link>http://www.medworm.com/index.php?rid=5483947&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F103</link>
            <description>Conclusions:
The present study has revealed the specific features of the first characterized endo beta-1,4 glucanase from yeast, whose thermostability is promising for biotechnological applications related to the saccharification of lignocellulosic biomass such as consolidated bioprocessing. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5483947</comments>
            <pubDate>Tue, 06 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5483947</guid>        </item>
        <item>
            <title>Synthesis of an antiviral drug precursor from chitin using a saprophyte as a whole-cell catalyst</title>
            <link>http://www.medworm.com/index.php?rid=5483948&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F102</link>
            <description>Conclusions:
This study is a proof of concept for the possibility to engineer in a filamentous fungus a bacterial enzyme cascade, which is fully functional. Furthermore, it provides the basis for the development of a process for NeuNAc production as well as a general prospective design for production processes that use saprophytes as whole-cell catalysts. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5483948</comments>
            <pubDate>Mon, 05 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5483948</guid>        </item>
        <item>
            <title>Biological activities of histidine-rich peptides; merging Biotechnology and Nanomedicine</title>
            <link>http://www.medworm.com/index.php?rid=5465796&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F101</link>
            <description>Histidine-rich peptides are commonly used in recombinant protein production as purification tags, allowing the one-step affinity separation of the His-tagged proteins from the extracellular media or cell extracts. Genetic engineering makes feasible the post-purification His-tag removal by inserting, between the tag and the main protein body, a target site for trans-acting proteases or a self-proteolytic peptide with regulatable activities. However, for technical ease, His tags are often not removed and the fusion proteins eventually used in this form. In this commentary, we revise the powerful biological properties of histidine-rich peptides as endosomolytic agents and as architectonic tags in nanoparticle formation, for which they are exploited in drug delivery and other nanomedical appli...</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5465796</comments>
            <pubDate>Fri, 02 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5465796</guid>        </item>
        <item>
            <title>Evaluation of toxic effects of several carboxylic acids on bacterial growth by toxicodynamic modelling.</title>
            <link>http://www.medworm.com/index.php?rid=5448025&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F100</link>
            <description>Conclusions:
The effect of several organic acids on the growth of different bacteria was accurately studied and perfectly characterized by a bivariate equation which combines the basis of dose-response theory with microbial growth kinetics (secondary model). The toxicity of carboxylic acids was lower with the increase of the molecular weight of these chemicals. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5448025</comments>
            <pubDate>Fri, 25 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5448025</guid>        </item>
        <item>
            <title>Microbial production of hyaluronic acid: Current state, challenges, and perspectives</title>
            <link>http://www.medworm.com/index.php?rid=5418596&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F99</link>
            <description>Hyaluronic acid (HA) is a natural and linear polymer composed of repeating disaccharide units of beta-1, 3-N-acetyl glucosamine and beta-1, 4-glucuronic acid with a molecular weight up to 6 million Daltons. With excellent viscoelasticity, high moisture retention capacity, and high biocompatibility, HA finds a wide-range of applications in medicine, cosmetics, and nutraceuticals.Traditionally HA was extracted from rooster combs, and now it is mainly produced via streptococcal fermentation. Recently the production of HA via recombinant systems has received increasing interest due to the avoidance of potential toxins. This work summarizes the research history and current commercial market of HA, and then deeply analyzes the current state of microbial production of HA by Streptococcus zooepide...</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5418596</comments>
            <pubDate>Wed, 16 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5418596</guid>        </item>
        <item>
            <title>Improvement of antibiotic activity of Xenorhabdus bovienii by medium optimization using response surface methodology</title>
            <link>http://www.medworm.com/index.php?rid=5418597&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F98</link>
            <description>Conclusions:
To the best of our knowledge, there are no reports on antibiotic production of X. boviebii by medium optimization using RSM. The results strongly support the use of RSM for medium optimization. The optimized medium not only resulted in a 37.8% increase of antibiotic activity, but also reduced the numbers of experiments. The chosen method of medium optimization was efficient, simple and less time consuming. This work will be useful for the development of X. bovienii cultivation process for efficient antibiotic production on a large scale, and for the development of more advanced control strategies on plant diseases. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5418597</comments>
            <pubDate>Mon, 14 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5418597</guid>        </item>
        <item>
            <title>The acid-tolerant L-arabinose isomerase from the mesophilic Shewanella sp ANA-3 is highly active at low temperatures</title>
            <link>http://www.medworm.com/index.php?rid=5397568&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F96</link>
            <description>Conclusions:
Here we reported the purification and the biochemical characterization of the novel Shewanella sp. ANA-3 L-arabinose isomerase. Determination of the biochemical properties demonstrated that this enzyme was highly active at low temperatures. The generated T268K mutant displays an increase of the enzyme stability essentially at low pH. These features seem to be very attractive for the bioconversion of D-galactose into D-tagatose at low temperature which is very interesting from industrial point of view. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5397568</comments>
            <pubDate>Thu, 10 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5397568</guid>        </item>
        <item>
            <title>Dehydratase Mediated 1-Propanol Production in Metabolically Engineered Escherichia coli</title>
            <link>http://www.medworm.com/index.php?rid=5397567&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F97</link>
            <description>Conclusions:
We have successfully established a new pathway for 1-propanol production by shunting the carbon flux from glycolysis. To our knowledge, it is the first time that this pathway has been utilized to produce 1-propanol in E. coli. The work presented here forms a basis for further improvement in production. We speculate that dragging more carbon flux towards methylglyoxal by manipulating glycolytic pathway and eliminating competing pathways such as lactate generation can further enhance the production of 1-propanol. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5397567</comments>
            <pubDate>Thu, 10 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5397567</guid>        </item>
        <item>
            <title>A novel esterase gene cloned from a metagenomic library from neritic sediments of the South China Sea</title>
            <link>http://www.medworm.com/index.php?rid=5397569&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F95</link>
            <description>Background:
Marine microbes are a large and diverse group, which are exposed to a wide variety of pressure, temperature, salinity, nutrient availability and other environmental conditions. They provide a huge potential source of novel enzymes with unique properties that may be useful in industry and biotechnology. To explore the lipolytic genetic resources in the South China Sea, 23 sediment samples were collected in the depth (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5397569</comments>
            <pubDate>Wed, 09 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5397569</guid>        </item>
        <item>
            <title>Molecular cloning, expression and biochemical characterisation of a cold-adapted novel recombinant chitinase from Glaciozyma antarctica PI12.</title>
            <link>http://www.medworm.com/index.php?rid=5376628&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F94</link>
            <description>Conclusion:
By taking advantage of its high activity at low temperatures and its acidic pH optimum, this recombinant chitinase will be valuable in various biotechnological applications under low temperature and acidic pH conditions. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5376628</comments>
            <pubDate>Fri, 04 Nov 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5376628</guid>        </item>
        <item>
            <title>Self-assembling, protein-based intracellular bacterial organelles: emerging vehicles for encapsulating, targeting and delivering therapeutical cargoes</title>
            <link>http://www.medworm.com/index.php?rid=5376630&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F92</link>
            <description>Many bacterial species contain intracellular nano- and micro-compartments consisting of self-assembling proteins that form protein-only shells. These structures are built up by combinations of a reduced number of repeated elements, from 60 repeated copies of one unique structural element self-assembled in encapsulins of 24 nm to 10,000-20,000 copies of a few protein species assembled in a organelle of around 100-150 nm in cross-section. However, this apparent simplicity does not correspond to the structural and functional sophistication of some of these organelles. They package, by not yet definitely solved mechanisms, one or more enzymes involved in specific metabolic pathways, confining such reactions and sequestering or increasing the inner concentration of unstable, toxics or volatile ...</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5376630</comments>
            <pubDate>Thu, 03 Nov 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5376630</guid>        </item>
        <item>
            <title>Protein trafficking, ergosterol biosynthesis and membrane physics impact recombinant protein secretion in Pichia pastoris</title>
            <link>http://www.medworm.com/index.php?rid=5376629&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F93</link>
            <description>Conclusions:
The current study presents a systems biotechnology-based strategy for the engineering of the industrially important yeast P. pastoris combining the use of host specific DNA microarray technologies and physiological studies under well defined environmental conditions. Such studies allowed for the identification of novel targets related with protein trafficking and ergosterol biosynthesis for improved recombinant protein production. Nevertheless, further studies will be required to elucidate the precise mechanisms whereby membrane biogenesis and composition impact on protein secretion in P. pastoris. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5376629</comments>
            <pubDate>Thu, 03 Nov 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5376629</guid>        </item>
        <item>
            <title>Development of a cultivation process for the enhancement of human interferon alpha 2b production in the oleaginous yeast, Yarrowia lipolytica</title>
            <link>http://www.medworm.com/index.php?rid=5376632&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F90</link>
            <description>Conclusion:
Y. lipolytica, a generally regarded as safe (GRAS) microorganism is one of the most promising non conventional yeasts for the production of biologically active therapeutic proteins under the control of hydrophobic substrate-inducible promoter. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5376632</comments>
            <pubDate>Wed, 02 Nov 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5376632</guid>        </item>
        <item>
            <title>Modifications of the metabolic pathways of lipid and triglyceride production in microalgae</title>
            <link>http://www.medworm.com/index.php?rid=5376631&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F91</link>
            <description>Microalgae have presented themselves as a strong candidate to replace diminishing oil reserves as a source of lipids for biofuels. Here we describe successful modifications of terrestrial plant lipid content which increase productivity overall or shift the balance of lipid production towards lipid varieties more useful for biofuel production. Our discussion ranges from the biosynthetic pathways and rate limiting steps of triacylglyceride formation to enzymes required for the formation of triacylglycerides containing exotic lipids. Secondarily, we discuss techniques for genetic engineering and modification of microalgae which can be combined with insights gained from research in higher plants to aid in the creation of production strains of microalgae. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5376631</comments>
            <pubDate>Wed, 02 Nov 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5376631</guid>        </item>
        <item>
            <title>Comparative genomics study of polyhydroxyalkanoates (PHA) and ectoine relevant genes from Halomonas sp. TD01 revealed extensive horizontal gene transfer events and co-evolutionary relationships</title>
            <link>http://www.medworm.com/index.php?rid=5376634&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F88</link>
            <description>Conclusions:
The accessibility of genome information would facilitate research on the genetic engineering of halophilic bacteria including Halomonas sp. TD01. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5376634</comments>
            <pubDate>Tue, 01 Nov 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5376634</guid>        </item>
        <item>
            <title>Simultaneous cell growth and ethanol production from cellulose by an engineered yeast consortium displaying a functional mini-cellulosome</title>
            <link>http://www.medworm.com/index.php?rid=5376633&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F89</link>
            <description>Conclusions:
This report represents a significant step towards the goal of cellulosic ethanol production. This engineered yeast consortium displaying a functional mini-cellulosome demonstrated not only the ability to grow on the released sugars from PASC but also a 3-fold higher ethanol production than a similar yeast consortium secreting only the three cellulases. The use of more complex cellulosomal structures may further improve the overall efficiency for ethanol production. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5376633</comments>
            <pubDate>Tue, 01 Nov 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5376633</guid>        </item>
        <item>
            <title>Significance of CO2 donor on the production of succinic acid by Actinobacillus succinogenes ATCC 55618</title>
            <link>http://www.medworm.com/index.php?rid=5376635&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F87</link>
            <description>Conclusions:
Besides the high dissolved CO2 concentration, the excessive addition of MgCO3 was beneficial to promote the succinic acid synthesis. This was the first report investigating the replaceable of gaseous CO2 in the fermentation of succinic acid. The results obtained in this study may be useful for reducing the cost of succinic acid fermentation process. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5376635</comments>
            <pubDate>Mon, 31 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5376635</guid>        </item>
        <item>
            <title>Heterologous Protein Display on the Cell Surface of Lactic Acid Bacteria Mediated by the S-Layer Protein</title>
            <link>http://www.medworm.com/index.php?rid=5376636&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F86</link>
            <description>Conclusion:
The LcsB region can be used as a functional scaffold to target the heterologous proteins to the cell surfaces of lactic acid bacteria in vitro and in vivo, and has also the potential for biotechnological application. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5376636</comments>
            <pubDate>Fri, 28 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5376636</guid>        </item>
        <item>
            <title>A fast approach to determine a fed batch feeding profile for recombinant Pichia pastoris strains</title>
            <link>http://www.medworm.com/index.php?rid=5356055&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F85</link>
            <description>Conclusion:
In this study, we show that a fast approach to determine a minimal set of strain characteristic parameters based on easy-to-do batch cultivations with methanol pulses is generally applicable for different P. pastoris strains and that dynamic fed batch strategies can be designed on the specific substrate uptake rate without running the risk of methanol accumulation. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5356055</comments>
            <pubDate>Thu, 27 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5356055</guid>        </item>
        <item>
            <title>Characterization of DNA polymerase beta from Danio rerio by overexpression in E. coli using the in vivo/in vitro compatible pIVEX plasmid</title>
            <link>http://www.medworm.com/index.php?rid=5344048&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F84</link>
            <description>Conclusions:
Our characterization of pol beta from a model fish organism contributes to the study of the function and evolution of DNA polymerases, which are emerging as important cellular targets for chemical intervention in the development of anticancer agents. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5344048</comments>
            <pubDate>Fri, 21 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5344048</guid>        </item>
        <item>
            <title>Regulation of mtl operon promoter of Bacillus subtilis: Requirements of its use in expression vectors</title>
            <link>http://www.medworm.com/index.php?rid=5344049&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F83</link>
            <description>Conclusions:
The mtl operon promoter (PmtlA) is a strong promoter that reached a maximum of 13,000 Miller units with lacZ as a reporter on low copy plasmids. It is tightly regulated by just one copy of the mtlR gene on the chromosome and subject to CCR. CCR can be switched off by mutations in MtlR and the glucose transporter. These properties and the low costs of the inducers, i.e. mannitol and glucitol, make the promoter ideal for designing regulated expression systems. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5344049</comments>
            <pubDate>Thu, 20 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5344049</guid>        </item>
        <item>
            <title>Actinoplanes teichomyceticus ATCC 31121 as a cell factory for producing teicoplanin</title>
            <link>http://www.medworm.com/index.php?rid=5331400&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F82</link>
            <description>Conclusions:
Since the cost and the quality of teicoplanin production depend mainly on the fermentation process, we developed a robust and scalable fermentation process by using an industrial medium in which a complex composition can be modulated by the combined addition of suitable precursors. This work was performed in the wild-type strain ATCC 31121, which has a clear genetic background. This is important for starting a rational improvement program and also helps to better control teicoplanin production during process and strain development. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5331400</comments>
            <pubDate>Tue, 18 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5331400</guid>        </item>
        <item>
            <title>Growth independent rhamnolipid production from glucose using the non-pathogenic Pseudomonas putida KT2440</title>
            <link>http://www.medworm.com/index.php?rid=5331402&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F80</link>
            <description>Conclusions:
A functional alternative to the pathogenic rhamnolipid producer P. aeruginosa was constructed and characterized. P. putida KT24C1 pVLT31_rhlAB featured the highest yield and titer reported from heterologous rhamnolipid producers with glucose as carbon source. Notably, rhamnolipid production was uncoupled from biomass formation, which allows optimal distribution of resources towards rhamnolipid synthesis. The results are discussed in the context of rational strain engineering by using the concepts of synthetic biology like chassis cells and orthogonality, thereby avoiding the complex regulatory programs of rhamnolipid production existing in the natural producer P. aeruginosa. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5331402</comments>
            <pubDate>Mon, 17 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5331402</guid>        </item>
        <item>
            <title>Microalgae as bioreactors for bioplastic production</title>
            <link>http://www.medworm.com/index.php?rid=5331401&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F81</link>
            <description>Solar-powered polyester production is proved feasible by causing microalgae to express enzymes borrowed from specialized bacteria, to result in biosynthesis of poly-3-hydroxybutyrate. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5331401</comments>
            <pubDate>Mon, 17 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5331401</guid>        </item>
        <item>
            <title>Co-production of GroELS discriminates between intrinsic and thermally-induced recombinant protein aggregation during substrate quality control</title>
            <link>http://www.medworm.com/index.php?rid=5311619&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F79</link>
            <description>Conclusions:
From the analysis of protein yield, solubility and biological activity of the four model proteins produced alone or along the chaperones, we conclude that GroELS impacts on yield and quality of aggregation-prone proteins with intrinsic determinants but not on thermally induced protein aggregation. No effective modifications of protein solubility have been observed, but significant stabilization of small (encapsulable) substrates and moderate chaperone-induced degradation of larger (excluded) polypeptides. These findings indicate that the activities of this chaperone pair in the context of actively producing recombinant bacteria discriminate between intrinsic and thermally-induced protein aggregation, and that the side effects of GroELS overproduction might be determined by sub...</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5311619</comments>
            <pubDate>Wed, 12 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5311619</guid>        </item>
        <item>
            <title>Heterologous expression, biochemical characterization, and overproduction of alkaline alpha-amylase from Bacillus alcalophilus in Bacillus subtilis</title>
            <link>http://www.medworm.com/index.php?rid=5294081&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F77</link>
            <description>Conclusions:
This is the first report concerning the heterologous expression of alkaline alpha-amylase in B. subtilis, and the obtained results make it feasible to achieve the industrial production of alkaline alpha-amylase with the recombinant B. subtilis. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5294081</comments>
            <pubDate>Fri, 07 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5294081</guid>        </item>
        <item>
            <title>An in silico Characterization of Microbial Electrosynthesis for Metabolic Engineering of Biochemicals</title>
            <link>http://www.medworm.com/index.php?rid=5294082&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F76</link>
            <description>Conclusions:
The results in this paper provide a systematic understanding of the benefits and limitations of bioelectrochemical techniques for biochemical production and highlight how electrical enhancement can impact cellular metabolism and biochemical production. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5294082</comments>
            <pubDate>Mon, 03 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5294082</guid>        </item>
        <item>
            <title>Real-Time Monitoring of Intracellular Wax Ester Metabolism</title>
            <link>http://www.medworm.com/index.php?rid=5269812&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F75</link>
            <description>Conclusions:
The monitoring system showed correlation between wax ester synthesis pattern and luminescent signal. The system shows potential for real-time screening purposes and studies on bacterial wax esters, revealing new aspects to dynamics and role of wax ester metabolism in bacteria. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5269812</comments>
            <pubDate>Fri, 30 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5269812</guid>        </item>
        <item>
            <title>Anti-biofilm Activity of an Exopolysaccharide from a Sponge-associated Strain of Bacillus licheniformis</title>
            <link>http://www.medworm.com/index.php?rid=5269813&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F74</link>
            <description>Conclusion:
The polysaccharide isolated from sponge-associated B. licheniformis has several features that provide a tool for better exploration of novel anti-biofilm compounds. Inhibiting biofilm formation of a wide range of bacteria without affecting their growth appears to represent a special feature of the polysaccharide described in this report. Further research on such surface-active compounds might help developing new classes of anti-biofilm molecules with broad spectrum activity and more in general will allow exploring of new functions for bacterial polysaccharides in the environment. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5269813</comments>
            <pubDate>Tue, 27 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5269813</guid>        </item>
        <item>
            <title>Yeast processing bodies and stress granules: self-assembly ribonucleoprotein particles</title>
            <link>http://www.medworm.com/index.php?rid=5257740&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F73</link>
            <description>Processing bodies (PBs) and stress granules (SGs) are two highly conserved cytoplasmic ribonucleoprotein foci that contain translationally repressed mRNAs together with proteins from the mRNA metabolism. Interestingly, they also share some common features with other granules, including the prokaryotic inclusion bodies. Although the function of PBs and SGs remains elusive, major advances have been done in unraveling their composition and assembly by using the yeast Saccharomyces cerevisae. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5257740</comments>
            <pubDate>Sat, 24 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5257740</guid>        </item>
        <item>
            <title>Optimisation of surface expression using the AIDA autotransporter</title>
            <link>http://www.medworm.com/index.php?rid=5218268&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F72</link>
            <description>Conclusions:
A number of parameters in recombinant protein production were seen to influence the surface expression of the model protein with respect both to the productivity and to the display on the individual cell. The choice of medium and the cell design to remove proteolytic cleavage were however the most important. Both fed-batch and batch processing can be successfully used, but prolonged batch processing is probably only possible if the chosen strain has a low acetic acid production. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5218268</comments>
            <pubDate>Wed, 14 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5218268</guid>        </item>
        <item>
            <title>Engineering Strategy of Yeast Metabolism for Higher Alcohol Production</title>
            <link>http://www.medworm.com/index.php?rid=5204913&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F70</link>
            <description>Conclusions:
The metabolic simulation demonstrated that the poor productivity of S. cerevisiae was improved by the introduction of E. coli genes to compensate the structural difference. This suggested that gene supplementation is a promising strategy for the metabolic engineering of S. cerevisiae to produce higher alcohols which should be the next challenge for the synthetic bioengineering of S. cerevisiae for the efficient production of higher alcohols. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5204913</comments>
            <pubDate>Thu, 08 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5204913</guid>        </item>
        <item>
            <title>Enzyme production by filamentous fungi: Analysis of the secretome of Trichoderma reesei grown on unconventional carbon source</title>
            <link>http://www.medworm.com/index.php?rid=5156669&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F68</link>
            <description>Conclusions:
: This study not only provides a catalogue of the prevalent proteins secreted by T. reesei in the two media, but the results also suggest that production of hydrolytic enzymes using unconventional carbon sources, such as components in spent hydrolysates, deserves further attention in the future. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5156669</comments>
            <pubDate>Mon, 22 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5156669</guid>        </item>
        <item>
            <title>Catabolic regulation analysis of Escherichia coli 
and its crp, mlc, mgsA, pgi and ptsG mutants</title>
            <link>http://www.medworm.com/index.php?rid=5117886&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F67</link>
            <description>${item.shortDescription} (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5117886</comments>
            <pubDate>Wed, 10 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5117886</guid>        </item>
        <item>
            <title>Expanding the molecular toolbox for Lactococcus lactis: construction of an inducible thioredoxin gene fusion expression system</title>
            <link>http://www.medworm.com/index.php?rid=5117887&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F66</link>
            <description>${item.shortDescription} (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5117887</comments>
            <pubDate>Mon, 08 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5117887</guid>        </item>
        <item>
            <title>Heterologous production of active Ribonuclease Inhibitor in Escherichia coli by redox state control and chaperonin coexpression</title>
            <link>http://www.medworm.com/index.php?rid=5106254&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F65</link>
            <description>${item.shortDescription} (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5106254</comments>
            <pubDate>Sun, 07 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5106254</guid>        </item>
        <item>
            <title>Overproduction of Bacillus amyloliquefaciens extracellular glutamyl-endopeptidase as a result of ectopic multi-copy insertion of an efficiently-expressed mpr gene into the Bacillus subtilis chromosome</title>
            <link>http://www.medworm.com/index.php?rid=5103045&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F64</link>
            <description>${item.shortDescription} (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5103045</comments>
            <pubDate>Thu, 04 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5103045</guid>        </item>
        <item>
            <title>Extracellular secretion of a recombinant therapeutic peptide by Bacillus halodurans utilizing a modified flagellin type III secretion system.</title>
            <link>http://www.medworm.com/index.php?rid=5094740&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F62</link>
            <description>${item.shortDescription} (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5094740</comments>
            <pubDate>Wed, 03 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5094740</guid>        </item>
        <item>
            <title>Polyphosphate - an ancient energy source and active metabolic regulator</title>
            <link>http://www.medworm.com/index.php?rid=5094739&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F63</link>
            <description>${item.shortDescription} (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5094739</comments>
            <pubDate>Wed, 03 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5094739</guid>        </item>
        <item>
            <title>1,3-propanediol dehydrogenases in Lactobacillus reuteri: impact on central metabolism and 3-hydroxypropionaldehyde production</title>
            <link>http://www.medworm.com/index.php?rid=5094741&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F61</link>
            <description>${item.shortDescription} (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5094741</comments>
            <pubDate>Tue, 02 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5094741</guid>        </item>
        <item>
            <title>Post-production protein stability: trouble beyond the cell factory</title>
            <link>http://www.medworm.com/index.php?rid=5085473&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F60</link>
            <description>${item.shortDescription} (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5085473</comments>
            <pubDate>Sun, 31 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5085473</guid>        </item>
        <item>
            <title>Morphology engineering - Osmolality and its effect on Aspergillus niger morphology and productivity</title>
            <link>http://www.medworm.com/index.php?rid=5076874&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F58</link>
            <description>${item.shortDescription} (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5076874</comments>
            <pubDate>Thu, 28 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5076874</guid>        </item>
        <item>
            <title>Retinoid production using metabolically engineered Escherichia coli with a two-phase culture system</title>
            <link>http://www.medworm.com/index.php?rid=5076873&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F59</link>
            <description>${item.shortDescription} (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5076873</comments>
            <pubDate>Thu, 28 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5076873</guid>        </item>
        <item>
            <title>Endotoxin-free purification for the isolation of Bovine Viral Diarrhoea Virus E2 protein from insoluble inclusion body aggregates</title>
            <link>http://www.medworm.com/index.php?rid=5068874&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F57</link>
            <description>${item.shortDescription} (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5068874</comments>
            <pubDate>Mon, 25 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5068874</guid>        </item>
        <item>
            <title>Functional identification in Lactobacillus reuteri of a
PocR-like transcription factor regulating glycerol utilization
and vitamin B12 synthesis</title>
            <link>http://www.medworm.com/index.php?rid=5048889&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F55</link>
            <description>${item.shortDescription} (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5048889</comments>
            <pubDate>Wed, 20 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5048889</guid>        </item>
        <item>
            <title>Identification and characterization of a new true lipase isolated through metagenomic approach</title>
            <link>http://www.medworm.com/index.php?rid=5035708&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F54</link>
            <description>Conclusions:
The combination of the use of a fat-contaminated soil, enrichment of prokaryotic DNA and a three-step screening strategy led to a high number of lipase-producing clones in the metagenomic library. The most notable properties of the new lipase that was isolated and characterized were a high specific activity against long chain triacylglycerols, activity and stability over a wide range of pH values, good thermal stability and stability in water-miscible organic solvents and at high salt concentrations. These characteristics suggest that this lipase has potential to perform well in biocatalytic processes, such as for hydrolysis and synthesis reactions involving long-chain triacylglycerols and fatty acid esters. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5035708</comments>
            <pubDate>Thu, 14 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5035708</guid>        </item>
        <item>
            <title>The role of Cra in regulating acetate excretion and osmotic tolerance in E. coli K-12 and E. coli B at high density growth</title>
            <link>http://www.medworm.com/index.php?rid=4992076&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F52</link>
            <description>Conclusions:
The transcriptional changes caused by the deletion of cra gene did not affect the activity of the central carbon metabolism, suggesting that Cra does not act alone; rather it interacts with other pleiotropic regulators to create a network of metabolic effects. An unexpected outcome of this work is the finding that cra deletion caused transcription inhibition of the bet operon in E. coli K-12 (JM109) but did not affect this operon transcription in E. coli B (BL21). This property, together with the insensitivity to high glucose concentrations, makes this the E. coli B (BL21) strain more resistant to environmental changes. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4992076</comments>
            <pubDate>Wed, 29 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4992076</guid>        </item>
        <item>
            <title>Optimizing HIV-1 protease production in Escherichia coli as fusion protein</title>
            <link>http://www.medworm.com/index.php?rid=4992075&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F53</link>
            <description>Conclusions:
By using this optimized expression and purification procedure fairly large amounts of good-quality HIV-1Pr recombinant enzyme can be produced at the lab-scale and thus used for further biochemical studies. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4992075</comments>
            <pubDate>Wed, 29 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4992075</guid>        </item>
        <item>
            <title>Enhanced biosurfactant production through cloning of three genes and role of esterase in biosurfactant release</title>
            <link>http://www.medworm.com/index.php?rid=4975036&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F49</link>
            <description>Conclusion:
The attributes of enhanced biosurfactant and esterase production by hyper-producing recombinant strains have many utilities from industrial viewpoint. This study for the first time has shown a possible association between biosurfactant production and esterase activity in any Bacillus species. Biosurfactant-esterase complex has been found to have powerful emulsification properties, which shows promising bioremediation, hydrocarbon biodegradation and pharmaceutical applications. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4975036</comments>
            <pubDate>Sun, 26 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4975036</guid>        </item>
        <item>
            <title>Modeling and measuring intracellular fluxes of secreted recombinant protein in Pichia pastoris with a novel 34S labeling procedure</title>
            <link>http://www.medworm.com/index.php?rid=4967955&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F47</link>
            <description>Conclusions:
A novel 34S labeling procedure that enables in vivo quantification of intracellular fluxes of recombinant protein under &quot;production like&quot; conditions is described. Subsequent sensitivity analysis of the fluxes by using MATLAB, indicate the most promising approaches for strain improvement towards increased secretion. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4967955</comments>
            <pubDate>Sat, 25 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4967955</guid>        </item>
        <item>
            <title>Virus-like particle production with yeast: ultrastructural and immunocytochemical insights into Pichia pastoris producing high levels of the Hepatitis B surface antigen</title>
            <link>http://www.medworm.com/index.php?rid=4967954&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F48</link>
            <description>Conclusions:
It is concluded that high level production and intrinsic slow HBsAg VLP assembly kinetics are leading to retention and accumulation of the antigen in the endoplasmic reticulum where it assembles at least partly into defined lamellar structures. Further transport of HBsAg to the Golgi apparatus is impaired thus leading to secretory pathway disfunction and the formation of an extended endoplasmic reticulum which bulges into irregular cloud-shaped formations. As VLPs were not found within the cells it is concluded that the VLP assembly process must take place during down-stream processing after detergent-mediated disassembly of HBsAg lamellas and subsequent reassembly of HBsAg into spherical VLPs. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4967954</comments>
            <pubDate>Sat, 25 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4967954</guid>        </item>
        <item>
            <title>Quantitative transcript analysis of the inducible expression system pSIP: comparison of the overexpression of Lactobacillus spp. beta-galactosidases in Lactobacillus plantarum</title>
            <link>http://www.medworm.com/index.php?rid=4959529&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F46</link>
            <description>Conclusion:
The use of identical expression strategies for highly similar genes led to very different mRNA levels. The data indicate that this difference is primarily caused by translational effects that are likely to affect both mRNA synthesis rates and mRNA stability. These translational effects thus seem to be a dominant determinant for the success of gene expression efforts in lactobacilli. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4959529</comments>
            <pubDate>Tue, 21 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4959529</guid>        </item>
        <item>
            <title>Statistics-based model for prediction of chemical biosynthesis yield from Saccharomyces cerevisiae</title>
            <link>http://www.medworm.com/index.php?rid=4951733&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F45</link>
            <description>Background:
The robustness of Saccharomyces cerevisiae in facilitating industrial-scale production of ethanol extends its utilization as a platform to synthesize other metabolites, both native and of heterologous origins. Metabolic engineering strategies, typically via pathway overexpression and deletion, continue to play a key role for optimizing the conversion efficiency of substrates into the desired products. However, chemical production titer or yield remains difficult to predict based on reaction stoichiometry and mass balance. We sampled a large space of data of chemical production from S. cerevisiae, and developed a statistics-based model to calculate production yield using input variables that represent the number of enzymatic steps in the key biosynthetic pathway of interest, met...</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4951733</comments>
            <pubDate>Mon, 20 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4951733</guid>        </item>
        <item>
            <title>Biotechnological applications of recombinant single-domain antibody fragments</title>
            <link>http://www.medworm.com/index.php?rid=4920497&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F44</link>
            <description>Conclusions:
Beside the necessary task of updating, this work analyses in detail some applicative aspects of the single-domain antibodies that have been overseen in the past, such as their efficacy as co-crystallization chaperones, protein aggregation controllers, enzyme activity tuners, and the specificities of the unconventional single-domain fragments. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4920497</comments>
            <pubDate>Wed, 08 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4920497</guid>        </item>
        <item>
            <title>A Novel Method to Prepare L-Arabinose from Xylose Mother Liquor by Yeast-mediated Biopurification</title>
            <link>http://www.medworm.com/index.php?rid=4910791&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F43</link>
            <description>Conclusion:
Yeast-mediated biopurification provides a dynamic method to prepare high purity of L-arabinose from the feedstock solution xylose mother liqour, with cost-effective and high-performance properties. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4910791</comments>
            <pubDate>Mon, 06 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4910791</guid>        </item>
        <item>
            <title>Streamlined Protein Expression and Purification Using Cleavable Self-Aggregating Tags</title>
            <link>http://www.medworm.com/index.php?rid=4891979&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F42</link>
            <description>Conclusions:
This tested single step purification is capable of producing proteins with high quantity and purity. It can greatly reduce the cost and time, and thus provides application potentials for both industrial scale up and laboratorial usage. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4891979</comments>
            <pubDate>Wed, 01 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4891979</guid>        </item>
        <item>
            <title>A Novel Family VII Esterase with Industrial Potential from Compost Metagenomic Library</title>
            <link>http://www.medworm.com/index.php?rid=4882892&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F41</link>
            <description>Conclusions:
The high stability of EstCS2 in organic solvents and its activity towards esters of ketoprofen and tertiary alcohols, and in polyurethane suggests that it has potential uses for many applications in biotransformation and bioremediation. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4882892</comments>
            <pubDate>Sat, 28 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4882892</guid>        </item>
        <item>
            <title>The effects of disruption of phosphoglucose isomerase gene on carbon utilisation and cellulase production in Trichoderma reesei Rut-C30</title>
            <link>http://www.medworm.com/index.php?rid=4861689&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F40</link>
            <description>Conclusions:
The ability to grow in media with glucose as the sole carbon source indicated that Trichoderma Deltapgi1 mutants were able to use the pentose phosphate pathway. But, they did not increase the expression of gpdh. Morphological characteristics were the result of the pgi1 deletion. Deletion of pgi1 in Rut-C30 increased cellulase production, but only under repressing conditions. This increase resulted partly from the deletion itself and partly from a genetic interaction with the cre1-1 mutation. The lower cellulase activity of these mutants in media with lactose could be attributed to a reduced ability to hydrolyse this sugar but not to an effect on the expression of xyr1. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4861689</comments>
            <pubDate>Mon, 23 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4861689</guid>        </item>
        <item>
            <title>Design of an efficient medium for heterologous protein production in Yarrowia lipolytica: case of human interferon alpha 2b</title>
            <link>http://www.medworm.com/index.php?rid=4847514&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F38</link>
            <description>Conclusion:
We have designed an efficient medium for large scale production of heterologous proteins by Y. lipolytica. The optimized medium GNY is suitable for the production of hIFN alpha2b with the advantage that no complex nitrogen sources with non-defined composition were required. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4847514</comments>
            <pubDate>Thu, 19 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4847514</guid>        </item>
        <item>
            <title>Metabolic regulation of Escherichia coli and its phoB and phoR genes knockout mutants under phosphate and nitrogen limitations as well as at acidic condition</title>
            <link>http://www.medworm.com/index.php?rid=4847513&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F39</link>
            <description>Conclusion:
The present result shows the complicated nature of the metabolic regulation for the fermentation characteristics upon phosphate limitation, acidic condition, and nitrogen limitation based on the transcript levels of selected genes. The result implies that the regulations under phosphate limitation, acidic condition, and nitrogen limitation, which occur typically at the late growth phase of the batch culture, are interconnected through RpoS and RpoD together with Pho genes. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4847513</comments>
            <pubDate>Thu, 19 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4847513</guid>        </item>
        <item>
            <title>Overexpression of human virus surface glycoprotein precursors induces cytosolic unfolded protein response in Saccharomyces cerevisiae</title>
            <link>http://www.medworm.com/index.php?rid=4840182&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F37</link>
            <description>Conclusions:
Inefficient translocation of MuHN and MeH precursors through ER membrane is a bottleneck for high-level expression in yeast. Overexpression of these recombinant proteins induces the UPR's cytosolic counterpart, the UPR-Cyto, which represent a subset of proteins involved in the heat-shock response. The involvement of eEF1A may explain the mechanism by which only large chaperones, but not small Hsps are upregulated during this stress response. Our study highlights important differences between viral surface protein expression in yeast and mammalian cells at the first stage of secretory pathway. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4840182</comments>
            <pubDate>Wed, 18 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4840182</guid>        </item>
        <item>
            <title>Improved Triacylglycerol Production in Acinetobacter baylyi ADP1 by Metabolic Engineering</title>
            <link>http://www.medworm.com/index.php?rid=4840183&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F36</link>
            <description>Conclusions:
In silico predictions of beneficial gene deletions were verified experimentally. The chosen single and multiple gene deletions affected beneficially the natural triacylglycerol metabolism of A. baylyi ADP1. This study demonstrates the importance of single gene deletions in triacylglycerol metabolism, and proposes Acinetobacter sp. ADP1 as a model system for bioenergetic studies regarding metabolic engineering. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4840183</comments>
            <pubDate>Tue, 17 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4840183</guid>        </item>
        <item>
            <title>Suppressing glucose uptake and acetic acid production increases membrane protein overexpression in Escherichia coli</title>
            <link>http://www.medworm.com/index.php?rid=4840184&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F35</link>
            <description>Conclusions:
The use of mutants that reduce the specific substrate uptake rate seems to be a versatile tool for overcoming some of the difficulties in the production of integral membrane spanning proteins. A set of strains with mutations in the glucose uptake system and with a lower acetic acid formation were able to produce three out of five membrane proteins that it was not possible to produce with the corresponding wild type. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4840184</comments>
            <pubDate>Mon, 16 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4840184</guid>        </item>
        <item>
            <title>Optimization of production of the anti-keratin 8 single-chain Fv TS1-218 in Pichia pastoris using design of experiments</title>
            <link>http://www.medworm.com/index.php?rid=4828338&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F34</link>
            <description>Conclusion:
The results demonstrated that design of experiments can be utilized for a rapid optimization of initial culture conditions and that P. pastoris is highly capable of producing and secreting functional single-chain antibody fragments at temperatures as low as 11 degrees C. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4828338</comments>
            <pubDate>Sun, 15 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4828338</guid>        </item>
        <item>
            <title>Strain engineering for improved expression of recombinant proteins in bacteria</title>
            <link>http://www.medworm.com/index.php?rid=4828339&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F32</link>
            <description>Protein expression in Escherichia coli represents the most facile approach for the preparation of non-glycosylated proteins for analytical and preparative purposes. So far, the optimization of recombinant expression has largely remained a matter of trial and error and has relied upon varying parameters, such as expression vector, media composition, growth temperature and chaperone co-expression. Recently several new approaches for the genome-scale engineering of E. coli to enhance recombinant protein expression have been developed. These methodologies now enable the generation of optimized E. coli expression strains in a manner analogous to metabolic engineering for the synthesis of low-molecular-weight compounds. In this short review, we provide an overview of strain engineering approache...</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4828339</comments>
            <pubDate>Fri, 13 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4828339</guid>        </item>
        <item>
            <title>Reducing conditions are the key for efficient production of active ribonuclease inhibitor in Escherichia coli</title>
            <link>http://www.medworm.com/index.php?rid=4812423&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F31</link>
            <description>Conclusions:
DTT highly improved both, periplasmic and cytoplasmic accumulation and activity of RI at low synthesis rate, i.e. in constructs harbouring weak recombinant synthesis rate stipulating genetic elements together with cultivation at low temperature. In a stirred bioreactor environment RI folding was strongly improved by repeated pulse addition of DTT at low aeration conditions. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4812423</comments>
            <pubDate>Mon, 09 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4812423</guid>        </item>
        <item>
            <title>Characterization of a cryptic plasmid pSM429 and its application for heterologous expression in psychrophilic Pseudoalteromonas</title>
            <link>http://www.medworm.com/index.php?rid=4788494&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F30</link>
            <description>Conclusions:
Plasmid pSM429 was isolated and characterized, and the regions essential for plasmid replication and stability were determined, helping the development of pSM429-based shuttle vectors. The shuttle vectors pWD and its derivatives could be used as cloning vectors for Pseudoalteromonas, offering new perspectives in the genetic manipulation of Pseudoalteromonas strains. With the aid of pWD-derived vector and its host, the erythromycin resistance gene and the cd gene of a cold-adapted protein were successfully expressed, indicating that the potential use of this system for recombinant protein production, especially for cold-adapted proteins. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4788494</comments>
            <pubDate>Wed, 04 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4788494</guid>        </item>
        <item>
            <title>Lactococcus lactis M4, a potential host for the expression of heterologous proteins</title>
            <link>http://www.medworm.com/index.php?rid=4753240&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F28</link>
            <description>Conclusions:
Based on the 16S rRNA gene molecular analysis, eight Gram-positive cocci milk isolates were identified as L. lactis subsp. lactis. One of the strains, L. lactis M4 was able to maintain transformed low molecular weight plasmid vectors and expressed the GFP gene. This strain has the potential to be developed into a new lactococcal host for the expression of heterologous proteins. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4753240</comments>
            <pubDate>Mon, 25 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4753240</guid>        </item>
        <item>
            <title>Evaluation of the Pichia pastoris expression system for the production of GPCRs for structural analysis</title>
            <link>http://www.medworm.com/index.php?rid=4742092&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F24</link>
            <description>Conclusion:
Compared to insect cells, P. pastoris is easier to handle, can be grown at lower cost, and can be expressed quicker at a large scale. Yeast, P. pastoris, and insect cells are all effective expression systems for GPCRs. The results of the present study strongly suggested that protein expression in P. pastoris can be applied to the structural and biochemical studies of GPCRs. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4742092</comments>
            <pubDate>Thu, 21 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4742092</guid>        </item>
        <item>
            <title>A reduction in growth rate of Pseudomonas putida KT2442 counteracts productivity advances in medium-chain-length polyhydroxyalkanoate production from gluconate</title>
            <link>http://www.medworm.com/index.php?rid=4742091&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F25</link>
            <description>Conclusions:
The study illustrates that the recruitment of a pleiotropic mutation, whose effects might reach deep into physiological regulation, effectively makes P. putida KT2440 and KT2442 two different strains in terms of mcl-PHA production. The differences include the onset of mcl-PHA production (nitrogen limitation) and the resulting strain performance (growth rate). It remains difficult to predict a priori where such major changes might occur, as illustrated by the comparable behavior on octanoate. Consequently, experimental data on mcl-PHA production acquired for P. putida KT2442 cannot always be extrapolated to KT2440 and vice versa, which potentially reduces the body of available knowledge for each of these two model strains for mcl-PHA production substantially. (Source: Microbial...</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4742091</comments>
            <pubDate>Thu, 21 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4742091</guid>        </item>
        <item>
            <title>Production of Nalpha-acetylated thymosin alpha1 in Escherichia coli</title>
            <link>http://www.medworm.com/index.php?rid=4742090&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F26</link>
            <description>Conclusions:
The present data demonstrate that Nalpha-acetylated Talpha1 can be efficiently produced in recombinant E. coli. This bioprocess could be used as an alternative to chemosynthesis for the production of Talpha1. The described methodologies may also be helpful for the biosynthesis of similar peptides. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4742090</comments>
            <pubDate>Thu, 21 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4742090</guid>        </item>
        <item>
            <title>Single cell analysis applied to antibody fragment production with Bacillus megaterium: development of advanced physiology and bioprocess state estimation tools</title>
            <link>http://www.medworm.com/index.php?rid=4719476&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F23</link>
            <description>Conclusions:
It was possible to distinguish between live, metabolic active, depolarized, dormant, and dead cells and to discriminate between high and low productive cells. The methods were shown suitable tools for process monitoring at single cell level allowing a better process understanding, increase robustness and form a firm basis for physiology-based analysis and optimization with general application for bioprocess development. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4719476</comments>
            <pubDate>Thu, 14 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4719476</guid>        </item>
        <item>
            <title>Surface display of salmonella epitopes in Escherichia coli and Staphylococcus carnosus</title>
            <link>http://www.medworm.com/index.php?rid=4704082&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F22</link>
            <description>Conclusion:
Apart from the accumulated knowledge and the existence of a wealth of equipment and techniques, the results indicate the selection of E. coli for further studies for surface expression of salmonella antigens. Surface expression of the full length protein facing the cell environment was positively proven by standard analysis, and the FACS signal comparison to expression in Staphylococcus carnosus shows that the distribution of the surface protein on each cell was comparatively very narrow in E. coli, the E. coli outer membrane molecules can serve as an adjuvant for the surface antigenic proteins and multimeric forms of the SefA protein were detected which would probably be positive for the realisation of a strong antigenic property. The detection of specific and similar proteoly...</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4704082</comments>
            <pubDate>Sun, 10 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4704082</guid>        </item>
        <item>
            <title>A transferable heterogeneous two-hybrid system in Escherichia coli based on polyhydroxyalkanoates synthesis regulatory protein PhaR</title>
            <link>http://www.medworm.com/index.php?rid=4692817&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F21</link>
            <description>Conclusion:
beta-Galactosidase activity level precisely correlated with the interaction force of tested protein pairs, and very weak beta-galactosidase expression was detected throughout the control groups, which demonstrated the feasibility of this system for studying protein interactions. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4692817</comments>
            <pubDate>Fri, 08 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4692817</guid>        </item>
        <item>
            <title>GH10 xylanase D from Penicillium funiculosum: biochemical studies and xylooligosaccharide production</title>
            <link>http://www.medworm.com/index.php?rid=4683407&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F20</link>
            <description>Conclusion:
Because of its attractive properties XynD might be considered for biotechnological applications. Moreover, XOS hydrolysis suggested that XynD possess four catalytic subsites with a high energy of interaction with the substrate and a fifth subsite with a small energy of interaction, according to the GH10 xylanase literature data. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4683407</comments>
            <pubDate>Mon, 04 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4683407</guid>        </item>
        <item>
            <title>Genetic response to metabolic fluctuations: correlation between central carbon metabolism and DNA replication in Escherichia coli</title>
            <link>http://www.medworm.com/index.php?rid=4663488&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F19</link>
            <description>Conclusions:
The genetic correlation exists between central carbon metabolism and DNA replication in the model Gram-negative bacterium, E. coli. This link exists at the steps of initiation and elongation of DNA replication, indicating the important global correlation between metabolic status of the cell and the events leading to cell reproduction. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4663488</comments>
            <pubDate>Wed, 30 Mar 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4663488</guid>        </item>
        <item>
            <title>Evolution combined with genomic study elucidates genetic bases of isobutanol tolerance in Escherichia coli</title>
            <link>http://www.medworm.com/index.php?rid=4631143&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F18</link>
            <description>Conclusions:
We have discovered a set of genotypic adaptations that confer increased tolerance to exogenous isobutanol stress. Our results are immediately useful to further efforts to engineer more isobutanol tolerant host strains of E. coli for isobutanol production. We suggest that rpoS and post-transcriptional regulators, such as hfq, RNA helicases, and sRNAs may be interesting mutagenesis targets for future global phenotype engineering. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4631143</comments>
            <pubDate>Fri, 25 Mar 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4631143</guid>        </item>
        <item>
            <title>Antifoam addition to shake flask cultures of recombinant Pichia pastoris increases yield</title>
            <link>http://www.medworm.com/index.php?rid=4621752&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F17</link>
            <description>Conclusions:
We show that addition of a range of antifoaming agents to shake flask cultures of P. pastoris increases the total yield of the recombinant protein being produced. This is not only a simple method to increase the amount of protein in the culture, but our study also provides insight into how antifoams interact with microbial cell factories. Two mechanisms are apparent: one group of antifoams (Antifoam A, Antifoam C and J673A) increases the specific yield of GFP by increasing the total amount of protein produced and secreted per cell, whilst the second (P2000 or SB2121) increases the total yield by increasing the density of the culture. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4621752</comments>
            <pubDate>Tue, 22 Mar 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4621752</guid>        </item>
        <item>
            <title>A dynamic method based on the specific substrate uptake rate to set up a feeding strategy for Pichia pastoris</title>
            <link>http://www.medworm.com/index.php?rid=4544562&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F14</link>
            <description>Conclusions:
Our strategy describes a novel and fast approach to determine strain specific parameters of a recombinant Pichia pastoris strain to set up feeding profiles solely based on the specific substrate uptake rate. This approach is generic and will allow application to other products and other hosts. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4544562</comments>
            <pubDate>Thu, 03 Mar 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4544562</guid>        </item>
        <item>
            <title>Oxygen transfer rate during the production of alginate by Azotobacter vinelandii under oxygen-limited and non oxygen-limited conditions</title>
            <link>http://www.medworm.com/index.php?rid=4527459&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F13</link>
            <description>Conclusions:
Overall, our results showed that under oxygen-limited and non oxygen-limited conditions, alginate production and its molecular mass are linked to the OTRmax, independently of the DOT of the culture. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4527459</comments>
            <pubDate>Sun, 27 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4527459</guid>        </item>
        <item>
            <title>Multi-omics approach to study the growth efficiency and amino acid metabolism in Lactococcus lactis at various specific growth rates</title>
            <link>http://www.medworm.com/index.php?rid=4516832&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F12</link>
            <description>Conclusions:
The current study demonstrates advantages of the usage of strictly controlled continuous cultivation methods combined with multi-omics approach for quantitative understanding of amino acid and energy metabolism of Lactococcus lactis which is a valuable new knowledge for development of balanced growth media, gene manipulations for desired product formation etc. Moreover, collected dataset is an excellent input for developing metabolic models. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4516832</comments>
            <pubDate>Thu, 24 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4516832</guid>        </item>
        <item>
            <title>Efficient production of soluble recombinant single chain Fv fragments by a Pseudomonas putida strain KT2440 cell factory</title>
            <link>http://www.medworm.com/index.php?rid=4501242&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F11</link>
            <description>Conclusions:
Pseudomonas putida KT2440 is a good cell factory for the production of scFvs, and the broad host range constructs we have produced allow yield assessment in a number of different expression hosts when yields in one initially selected are insufficient. High cell density cultivation and further optimization and refinement of the KT2440 cell factory will achieve additional increases in the yields of scFvs. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4501242</comments>
            <pubDate>Mon, 21 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4501242</guid>        </item>
        <item>
            <title>High cell density cultivation of Escherichia coli K4 in a microfiltration bioreactor: a step towards improvement of chondroitin precursor production</title>
            <link>http://www.medworm.com/index.php?rid=4489094&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F10</link>
            <description>Conclusion:
The increase of capsular polysaccharide titre confirmed the validity of the proposed fermentation strategy and opened the way to the use of the microfiltration bioreactor for the biotechnological production of chondroitin. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4489094</comments>
            <pubDate>Wed, 16 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4489094</guid>        </item>
        <item>
            <title>Active protein aggregates induced by terminally attached self-assembling peptide ELK16 in Escherichia coli</title>
            <link>http://www.medworm.com/index.php?rid=4477165&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F9</link>
            <description>Conclusions:
This has been the first report where a terminally attached self-assembling beta peptide ELK16 can promote the formation of active inclusion bodies or active protein aggregates in E. coli. It has the potential to render E. coli and other recombinant hosts more efficient as microbial cell factories for protein production. Our observation might also provide hints for protein aggregation-related diseases. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4477165</comments>
            <pubDate>Tue, 15 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4477165</guid>        </item>
        <item>
            <title>Loosenin, a novel protein with cellulose-disrupting activity from Bjerkandera adusta.</title>
            <link>http://www.medworm.com/index.php?rid=4464205&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F8</link>
            <description>Conclusions:
LOOS1 is a new type of protein with disrupting activity on cellulose. LOOS1 binds polysaccharides, and given its enhancing properties on the action of hydrolytic enzymes, LOOS1 represents a potential additive in the production of fermentable sugars from lignocellulose. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4464205</comments>
            <pubDate>Fri, 11 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4464205</guid>        </item>
        <item>
            <title>Expression of an endotoxin-free S-layer/allergen fusion protein in gram-positive Bacillus subtilis 1012 for the potential application as vaccines for immunotherapy of atopic allergy</title>
            <link>http://www.medworm.com/index.php?rid=4459486&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F6</link>
            <description>Conclusions:
The impact of this study can be seen in the usage of a gram-positive organism for the production of pyrogen-free self-assembling recombinant S-layer/allergen fusion protein with great relevance for the development of vaccines for immunotherapy of atopic allergy. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4459486</comments>
            <pubDate>Thu, 10 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4459486</guid>        </item>
        <item>
            <title>Modification of genetic regulation of a heterologous chitosanase gene in  Streptomyces lividans TK24 leads to chitosanase production in the absence of chitosan</title>
            <link>http://www.medworm.com/index.php?rid=4459485&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F7</link>
            <description>Conclusions:
This new chitosanase production system is of interest for biotechnology as only common media components are used and enzyme of high degree of purity is obtained directly in the culture supernatant. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4459485</comments>
            <pubDate>Thu, 10 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4459485</guid>        </item>
        <item>
            <title>Xylitol production from xylose mother liquor: a novel strategy that combines the use of recombinant Bacillus subtilis and Candida maltosa</title>
            <link>http://www.medworm.com/index.php?rid=4445452&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F5</link>
            <description>Conclusion:
In this study, we developed a biological method for the purification of xylose from xylose mother liquor and subsequent preparation of xylitol by C. maltosa-mediated biohydrogenation of xylose. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4445452</comments>
            <pubDate>Mon, 07 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4445452</guid>        </item>
        <item>
            <title>Improving yeast strains using recyclable integration cassettes, for the production of plant terpenoids</title>
            <link>http://www.medworm.com/index.php?rid=4411266&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F4</link>
            <description>Conclusions:
Using the developed molecular tools, new yeast strains were generated with increased capacity to produce plant terpenoids. The approach taken and the durability of the strains allow successive rounds of improvement to maximize yields. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4411266</comments>
            <pubDate>Fri, 28 Jan 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4411266</guid>        </item>
        <item>
            <title>Transcriptional regulation of main metabolic pathways of cyoA, cydB, fnr, and fur gene knockout Escherichia coli in C-limited and N-limited aerobic continuous cultures</title>
            <link>http://www.medworm.com/index.php?rid=4405230&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F3</link>
            <description>Conclusion:
The present result demonstrated how the fermentation characteristics could be explained by the transcript levels of metabolic pathway genes as well as global regulators in relation to the knockout of such single genes as cyoA, cydB, fnr, and fur, and clarified the complex gene network regulation in relation to glycolysis, TCA cycle, respiration, and N-regulated pathways. The present result is quite important in understanding the metabolic regulation for metabolic engineering. Moreover, the present result may be useful in improving the specific glucose consumption rate and activation of the TCA cycle by modulating the respiratory chain genes and the related global regulators. The result obtained under N-limited condition may be useful for the heterologous protein production unde...</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4405230</comments>
            <pubDate>Thu, 27 Jan 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4405230</guid>        </item>
        <item>
            <title>Metabolic pathway engineering based on metabolomics confers acetic and formic acid tolerance to a recombinant xylose-fermenting strain of Saccharomyces cerevisiae</title>
            <link>http://www.medworm.com/index.php?rid=4330522&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F2</link>
            <description>Conclusions:
Our metabolomic approach revealed one of the molecular events underlying the response to acetic acid and focuses attention on the non-oxidative PPP as a target for metabolic engineering. An important challenge for metabolic engineering is identification of gene targets that have material importance. This study has demonstrated that metabolomics is a powerful tool to develop rational strategies to confer tolerance to stress through genetic engineering. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4330522</comments>
            <pubDate>Mon, 10 Jan 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4330522</guid>        </item>
        <item>
            <title>Pre-expression of a sulfhydryl oxidase significantly increases the yields of eukaryotic disulfide bond containing proteins expressed in the cytoplasm of E.coli</title>
            <link>http://www.medworm.com/index.php?rid=4322265&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F10%2F1%2F1</link>
            <description>Conclusions:
Our results show that the production of eukaryotic proteins with multiple disulfide bonds in the cytoplasm of E.coli is possible. The required exogenous components can be put onto a single plasmid vector allowing facile transfer between different prokaryotic strains. These results open up new avenues for the use of E.coli as a microbial cell factory. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4322265</comments>
            <pubDate>Fri, 07 Jan 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4322265</guid>        </item>
        <item>
            <title>Engineering building blocks for self-assembling protein nanoparticles</title>
            <link>http://www.medworm.com/index.php?rid=4300399&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F9%2F1%2F101</link>
            <description>Like natural viruses, manmade protein cages for drug delivery are to be ideally formed by repetitive subunits with self-assembling properties, mimicking viral functions and molecular organization. Naturally formed nanostructures (such as viruses, flagella or simpler protein oligomers) can be engineered to acquire specific traits of interest in biomedicine, for instance through the addition of cell targeting agents for desired biodistribution and specific delivery of associated drugs. However, fully artificial constructs would be highly desirable regarding finest tuning and adaptation to precise therapeutic purposes. Although engineering of protein assembling is still in its infancy, arising principles and promising strategies of protein manipulation point out the rational construction of n...</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4300399</comments>
            <pubDate>Thu, 30 Dec 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4300399</guid>        </item>
        <item>
            <title>Physiological responses to folate overproduction in Lactobacillus plantarum WCFS1</title>
            <link>http://www.medworm.com/index.php?rid=4264855&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F9%2F1%2F100</link>
            <description>Conclusion:
Folate overproduction leads to very little change in metabolite levels or overall transcript profile, while at the same time the growth rate is reduced drastically. This shows that Lactobacillus plantarum WCFS1 is unable to respond to this growth rate reduction, most likely because the growth-related transcripts and proteins are diluted by the enormous amount of gratuitous folate-related transcripts and proteins. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4264855</comments>
            <pubDate>Fri, 17 Dec 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4264855</guid>        </item>
        <item>
            <title>Large-scale production of magnetosomes by chemostat culture of Magnetospirillum gryphiswaldense at high cell density</title>
            <link>http://www.medworm.com/index.php?rid=4252684&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F9%2F1%2F99</link>
            <description>Conclusions:
Compared to previously reported methods, our culture technique with the MSR-1 strain significantly increased cell density, cell yield, and magnetosome yield in a shorter time window and thus reduced the cost of production. The cell density and magnetosome yield reported here are the highest so far achieved with a magnetotactic bacteria. Refinement of this technique will enable further increase of cell density and magnetosome yield. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4252684</comments>
            <pubDate>Sun, 12 Dec 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4252684</guid>        </item>
        <item>
            <title>High yield expression of leptospirosis vaccine candidates LigA and LipL32 in the methylotrophic yeast Pichia pastoris</title>
            <link>http://www.medworm.com/index.php?rid=4232828&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F9%2F1%2F98</link>
            <description>Conclusions:
The expression of LigANI and LipL32 in P. pastoris resulted in a significant increase in yield compared to expression in E. coli. In addition, the proteins were secreted, allowing for easy purification, and retained the antigenic characteristics of the native proteins, demonstrating their potential application as subunit vaccine candidates. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4232828</comments>
            <pubDate>Mon, 06 Dec 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4232828</guid>        </item>
        <item>
            <title>Two distinct regions in the model protein Peb1 are critical for its heterologous transport out of Escherichia coli</title>
            <link>http://www.medworm.com/index.php?rid=4224702&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F9%2F1%2F97</link>
            <description>Conclusions:
We propose that the localization of the model protein Peb1 in the growth medium of E. coli is due to active secretion by a still unknown pathway of E. coli. The secretion apparently is a two-step process involving a periplasmic step and the TAR regions. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4224702</comments>
            <pubDate>Thu, 02 Dec 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4224702</guid>        </item>
        <item>
            <title>Biosynthesis of chiral 3-hydroxyvalerate from single propionate-unrelated carbon sources in metabolically engineered E. coli</title>
            <link>http://www.medworm.com/index.php?rid=4205670&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F9%2F1%2F96</link>
            <description>Conclusions:
Our work represents the first report of direct microbial production of enantiomerically pure 3HV from a single carbon source. Continued engineering of host strains and pathway enzymes will ultimately lead to more economical production of chiral 3HV. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4205670</comments>
            <pubDate>Sat, 27 Nov 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4205670</guid>        </item>
        <item>
            <title>Differential proteomic analysis highlights metabolic strategies associated with balhimycin production in Amycolatopsis balhimycina chemostat cultivations</title>
            <link>http://www.medworm.com/index.php?rid=4202905&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F9%2F1%2F95</link>
            <description>Conclusion:
In the two chemostat conditions, used to generate biomass for proteomic analysis, mycelia grew with the same rate and with similar glucose-biomass conversion efficiencies. Global gene expression analysis revealed a differential metabolic adaptation, highlighting strategies for energetic supply and biosynthesis of metabolic intermediates required for biomass production and, in LP, for balhimycin biosynthesis. These data, confirming a relationship between primary metabolism and antibiotic production, could be used to increase antibiotic yield both by rational genetic engineering and fermentation processes improvement. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4202905</comments>
            <pubDate>Fri, 26 Nov 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4202905</guid>        </item>
        <item>
            <title>Dissection of an old protein reveals a novel application: domain D of Staphylococcus aureus Protein A (sSpAD) as a secretion - tag</title>
            <link>http://www.medworm.com/index.php?rid=4196490&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F9%2F1%2F92</link>
            <description>Conclusions:
In this work we present a new secretion tag that combines several advantages for the production of recombinant proteins in E. coli. Domain D of S. aureus protein A protects the protein of interest against N-terminal degradation, increases target protein solubility and enables a straight-forward purification of the recombinant protein using of IgG columns. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4196490</comments>
            <pubDate>Tue, 23 Nov 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4196490</guid>        </item>
        <item>
            <title>Fed-batch fermentation of GM-CSF-producing glycoengineered Pichia pastoris under controlled specific growth rate</title>
            <link>http://www.medworm.com/index.php?rid=4196489&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F9%2F1%2F93</link>
            <description>Conclusions:
Together, these data illustrate that the GlycoSwitch-Man5 P. pastoris is a robust production strain for homogenously N-glycosylated proteins. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4196489</comments>
            <pubDate>Tue, 23 Nov 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4196489</guid>        </item>
        <item>
            <title>Identification and characterization of a novel fumarase gene by metagenome expression cloning from marine microorganisms</title>
            <link>http://www.medworm.com/index.php?rid=4189682&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F9%2F1%2F91</link>
            <description>Conclusions:
We isolated a novel fumarase gene, fumF, from a sequence-based screen of a plasmid metagenomic library from uncultivated marine microorganisms. The properties of FumF protein may be ideal for the industrial production of L-malate under higher temperature conditions. The identification of FumF underscores the potential of marine metagenome screening for novel biomolecules. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4189682</comments>
            <pubDate>Tue, 23 Nov 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4189682</guid>        </item>
        <item>
            <title>Physiological characteristics of the extreme thermophile Caldicellulosiruptor saccharolyticus: an efficient hydrogen cell factory</title>
            <link>http://www.medworm.com/index.php?rid=4189684&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F9%2F1%2F89</link>
            <description>Global concerns about climate changes and their association with the use of fossil fuels have accelerated research on biological fuel production. Biological hydrogen production from hemicellulose-containing waste is considered one of the promising avenues. A major economical issue for such a process, however, is the low substrate conversion efficiency. Interestingly, the extreme thermophilic bacterium Caldicellulosiruptor saccharolyticus can produce hydrogen from carbohydrate-rich substrates at yields close to the theoretical maximum of the dark fermentation process (i.e., 4 mol H2/mol hexose). The organism is able to ferment an array of mono-, di- and polysaccharides, and is relatively tolerant to high partial hydrogen pressures, making it a promising candidate for exploitation in a biohy...</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4189684</comments>
            <pubDate>Mon, 22 Nov 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4189684</guid>        </item>
        <item>
            <title>Metabolic Response of Geobacter sulfurreducens towards Electron Donor/Acceptor Variation</title>
            <link>http://www.medworm.com/index.php?rid=4189683&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F9%2F1%2F90</link>
            <description>Conclusions:
We gained detailed insights into the metabolism of G. sulfurreducens cells under various electron donor/acceptor conditions using 13C-based metabolic flux analysis. Our results can be used for the development of G. sulfurreducens as a chassis for a variety of applications including bioremediation and renewable biofuel production. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4189683</comments>
            <pubDate>Mon, 22 Nov 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4189683</guid>        </item>
        <item>
            <title>Modeling and simulation of the main metabolism in Escherichia coli and its several single-gene knockout mutants with experimental verification</title>
            <link>http://www.medworm.com/index.php?rid=4182783&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F9%2F1%2F88</link>
            <description>Conclusions:
It was shown to be useful to simulate the main metabolism of E.coli for understanding metabolic changes inside the cell in response to specific pathway gene knockouts, considering the whole main metabolic pathways. The comparison of the simulation result with the experimental data indicates that the present model could simulate the effect of the specific gene knockouts to the changes in the metabolisms to some extent. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4182783</comments>
            <pubDate>Fri, 19 Nov 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4182783</guid>        </item>
        <item>
            <title>High-level production of animal-free recombinant transferrin from Saccharomyces cerevisiae</title>
            <link>http://www.medworm.com/index.php?rid=4175302&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F9%2F1%2F87</link>
            <description>Conclusions:
A Saccharomyces cerevisiae expression system has enabled the cGMP manufacture of an animal-free rTf for industrial cell culture application without the risk of prion and viral contamination, and provides a high-quality platform for the development of transferrin-based therapeutics. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4175302</comments>
            <pubDate>Wed, 17 Nov 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4175302</guid>        </item>
        <item>
            <title>Bioprocess Control in Microscale: Scalable Fermentations in Disposable and User-Friendly Microfluidic Systems</title>
            <link>http://www.medworm.com/index.php?rid=4162677&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F9%2F1%2F86</link>
            <description>Conclusion:
In microfluidic MTPs, pH-controlled batch as well as fed-batch fermentations were successfully performed. The liquid dosing as well as the biomass growth kinetics of the process-controlled fermentations agreed well both in the microscale and laboratory scale. In conclusion, a user-friendly and disposable microfluidic system could be established which allows scaleable, fully controlled and fully monitored fermentations in working volumes below 1 milliliter. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4162677</comments>
            <pubDate>Sat, 13 Nov 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4162677</guid>        </item>
        <item>
            <title>Improved vanillin production in baker's yeast through in silico design</title>
            <link>http://www.medworm.com/index.php?rid=4142519&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F9%2F1%2F84</link>
            <description>Conclusion:
Use of constraints corresponding to different physiological states was found to greatly influence the target predictions given minimization of metabolic adjustment (MOMA) as biological objective function. In vivo verification of the targets, selected based on their predicted metabolic adjustment, successfully led to overproducing strains. Overall, we propose and demonstrate a framework for in silico design and target selection for improving microbial cell factories. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4142519</comments>
            <pubDate>Mon, 08 Nov 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4142519</guid>        </item>
        <item>
            <title>Inclusion bodies: a new concept</title>
            <link>http://www.medworm.com/index.php?rid=4124579&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F9%2F1%2F80</link>
            <description>In the last decades, the understanding of inclusion body biology and consequently, of their properties and potential biotechnological applications have dramatically changed. Therefore, the development of new purification protocols aimed to preserve those properties is becoming a pushing demand. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4124579</comments>
            <pubDate>Mon, 01 Nov 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4124579</guid>        </item>
        <item>
            <title>Two-stage, self-cycling process for the production of bacteriophages</title>
            <link>http://www.medworm.com/index.php?rid=4124578&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F9%2F1%2F81</link>
            <description>Conclusions:
Production of bacteriophage T4 in the semi-continuous, automated SCF/SCI system was efficient and reproducible from cycle to cycle. Synchronization of the host in the first stage prior to infection led to improvements in the specific productivity of phages in the second stage while maintaining the volumetric productivity. These results demonstrate the significant potential of this approach for both upstream and downstream process optimization. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4124578</comments>
            <pubDate>Mon, 01 Nov 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4124578</guid>        </item>
        <item>
            <title>Quantification of the physiochemical constraints on the export of spider silk proteins by Salmonella type III secretion</title>
            <link>http://www.medworm.com/index.php?rid=4105072&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F9%2F1%2F78</link>
            <description>Conclusions:
We show that the natural system encoded in SPI-1 only produces high titers of secreted protein for 4-8 hours when the natural psicA promoter is used to drive expression. Secretion efficiency can be high, but declines for charged or large sequences. A quantitative characterization of these constraints will facilitate the effective use and engineering of this system. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4105072</comments>
            <pubDate>Sun, 24 Oct 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4105072</guid>        </item>
        <item>
            <title>Genome-wide identification of Saccharomyces cerevisiae genes required for tolerance to acetic acid</title>
            <link>http://www.medworm.com/index.php?rid=4105071&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F9%2F1%2F79</link>
            <description>Conclusions:
Approximately 490 of the 650 determinants of tolerance to acetic acid identified in this work are implicated, for the first time, in tolerance to this weak acid. These are novel candidate genes for genetic engineering to obtain more robust yeast strains against acetic acid toxicity. Among these genes there are number of transcription factors that are documented regulators of a large percentage of the genes found to exert protection against acetic acid thus being considered interesting targets for subsequent genetic engineering. The increase of potassium concentration in the growth medium was found to improve the expression of maximal tolerance to acetic acid, consistent with the idea that the adequate manipulation of nutrient concentration of industrial growth medium can be an...</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4105071</comments>
            <pubDate>Sun, 24 Oct 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4105071</guid>        </item>
        <item>
            <title>Physiological relation between respiration activity and heterologous expression of selected benzoylformate decarboxylase variants in Escherichia coli</title>
            <link>http://www.medworm.com/index.php?rid=4081609&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F9%2F1%2F76</link>
            <description>Conclusions:
The BFD-variants with high cofactor binding affinity (wild type, His281Ala, Ser181Thr) obviously extract thiamine from the medium and bind it tightly to the enzyme. This might explain the hampered growth of these clones. In contrast, growth of clones expressing variants with low cofactor binding affinity (Leu476His, Leu476Pro, Leu476Pro-Ser181Thr) is not impaired. Leu476Gln has an intermediate cofactor binding strength, thus, growth of its host strain depends on the specific cultivation conditions. This paper shows that slight differences of the amino acid composition can affect protein expression and cultivation and might require an adaptation of media components. Effects such as the observed are hardly foreseeable and difficult to detect in conventional screening processes. ...</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4081609</comments>
            <pubDate>Mon, 18 Oct 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4081609</guid>        </item>
        <item>
            <title>Expression and purification of ELP-intein-tagged target proteins in high cell density E. coli fermentation</title>
            <link>http://www.medworm.com/index.php?rid=4081608&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F9%2F1%2F77</link>
            <description>Conclusions:
By using fed batch E. coli fermentation at high cell density, ELP-intein-tagged proteins can be expressed and purified at high yield with low cost. Further, the impact of media components and fermentation design can significantly impact the overall process cost, particularly at large scale. This work thus demonstrates an important advances in the scale up of self-cleaving ELP tag-mediated processes. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4081608</comments>
            <pubDate>Mon, 18 Oct 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4081608</guid>        </item>
        <item>
            <title>Glucose uptake regulation in E. coli by the small RNA SgrS: comparative analysis of E. coli K (JM109 and MG1655) and E. coli B (BL21).</title>
            <link>http://www.medworm.com/index.php?rid=4012158&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F9%2F1%2F75</link>
            <description>Conclusions:
The results suggest that E. coli B (BL21) tolerates high glucose concentration not only by its more efficient central carbon metabolism, but also by controlling the glucose transport into the cells regulated by the sRNA SgrS, which may suggest a way to control glucose consumption and increase its efficient utilization. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4012158</comments>
            <pubDate>Mon, 27 Sep 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4012158</guid>        </item>
        <item>
            <title>Display of wasp venom allergens on the cell surface of Saccharomyces cerevisiae</title>
            <link>http://www.medworm.com/index.php?rid=3998327&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F9%2F1%2F74</link>
            <description>Conclusions:
All the three major wasp venom allergens were expressed on the yeast surface. A high-level expression, which was observed only for antigen 5, was needed for detection of IgE binding by FACS and for induction of histamine release. The non-modified S. cerevisiae cells did not cause any unspecific reaction in FACS or histamine release assay despite the expression of high-mannose oligosaccharides.In perspective the yeast surface display may be used for allergen discovery from cDNA libraries and possibly for sublingual immunotherapy as the cells can serve as good adjuvant and can be produced in large amounts at a low price. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3998327</comments>
            <pubDate>Thu, 23 Sep 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3998327</guid>        </item>
        <item>
            <title>Single cell oils of the cold-adapted oleaginous yeast
Rhodotorula glacialis DBVPG 4785</title>
            <link>http://www.medworm.com/index.php?rid=3993035&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F9%2F1%2F73</link>
            <description>Conclusions:
This study is the first proposed biotechnological application for Rhodotorula glacialis species, whose oleaginous biomass accumulates high amounts of lipids within a wide range of temperatures through appropriate cultivation C:N ratio. Although R. glacialis DBVPG 4785 is a cold adapted yeast, lipid production occurs over a broad range of temperatures and it can be considered an interesting microorganism for the production of single cell oils. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3993035</comments>
            <pubDate>Wed, 22 Sep 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3993035</guid>        </item>
        <item>
            <title>Fed-batch process for the psychrotolerant marine bacterium Pseudoalteromonas haloplanktis</title>
            <link>http://www.medworm.com/index.php?rid=3993036&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F9%2F1%2F72</link>
            <description>Conclusion:
The growth of P. haloplanktis to higher cell densities on complex medium is possible. A first fed-batch fermentation strategy could be established which is feasible to be used in lab-scale or for industrial purposes. The substrate concentration of the feeding solution was found to influence the maximal biomass yield considerably. The bottleneck for growing P. haloplanktis to high cell densities still remains the availability of a highly concentrated substrate and the reduction of the substrate complexity. However, our results indicate glutamic acid as a major carbon source, which provides a good basis for further improvement of the fed-batch process. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3993036</comments>
            <pubDate>Mon, 20 Sep 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3993036</guid>        </item>
        <item>
            <title>Isolation of cell-free bacterial inclusion bodies</title>
            <link>http://www.medworm.com/index.php?rid=3980359&amp;cid=s_34082_77_f&amp;fid=34082&amp;url=http%3A%2F%2Fwww.microbialcellfactories.com%2Fcontent%2F9%2F1%2F71</link>
            <description>Conclusions:
The application of the developed protocol allows obtaining bacterial free inclusion bodies suitable for use in mammalian cell cultures and other biological interfaces. (Source: Microbial Cell Factories)</description>
            <author>Microbial Cell Factories</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3980359</comments>
            <pubDate>Thu, 16 Sep 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3980359</guid>        </item>
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