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</figure> | </figure> | ||
+ | <div class="contentbox"> | ||
+ | <h1 class="box-heading"><i>Bacillus subtilis</i> – Gram-positive model organism</h1> | ||
+ | <p>B. subtilis is the best-studied Gram-positive microorganisms, and a model bacterium studying bacterial differentiation (e.g. endospore formation) and phenotypic heterogeneity. Its ability to become naturally competent makes <i>B. subtilis</i> an organism with easily tractable genetics. The GRAS (generally recognized as safe) status and secretory capacity made <i>B. subtilis</i> a preferred host of choice for big scale production of secreted proteins, such as lipases, proteases and amylases, highlighting the industrial relevance of this bacterium.</p> | ||
+ | <p></p> | ||
+ | In addition, the iGEM Team LMU-Munich 2012 has constructed the Bacillus BioBrickBox, which contains several well evaluated integrative and replicative vectors and other parts for the use in <i>B. subtilis</i>, thus providing a powerful toolbox to engineer <i>B. subtilis</i>. | ||
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+ | |||
+ | <div class="contentbox"> | ||
+ | <h1 class="box-heading">References</h1> | ||
+ | <table class="source"> | ||
+ | <colgroup> | ||
+ | <col width="5%"> | ||
+ | <col width="95%"> | ||
+ | </colgroup> | ||
+ | <tr> | ||
+ | <td><a target="_blank" href ="https://www.ncbi.nlm.nih.gov/pubmed/23311580">[1]</a></td> | ||
+ | <td>van Dijl J. M. and Hecker M. (2013) <i>Bacillus subtilis</i>: from soil bacterium to super-secreting cell factory. <i>Mircobial Cell Factories 12</i>, 3 (1-6).</td> | ||
+ | </tr> | ||
+ | <tr> | ||
+ | <td><a target="_blank" href ="https://www.ncbi.nlm.nih.gov/pubmed/17938627">[2]</a></td> | ||
+ | <td>Papanikou E., Karamanou S. and Economou A. (2007) Bacterial protein secretion through the translocase nanomachine.. <i>Nature Reviews Microbiology 5</i>, 11 (839-851).</td> | ||
+ | </tr> | ||
+ | <tr> | ||
+ | <td><a target="_blank" href ="https://www.ncbi.nlm.nih.gov/pubmed/16997527">[3]</a></td> | ||
+ | <td>Fu L. L., Xu Z. R., Li W. F., Shuai J. B., Lu P. and Hu C. X. (2006) Protein secretion pathways in <i>Bacillus subtilis</i>: implication for optimization of heterologous protein secretion. <i>Biotechnology advances 25</i>, 1 (1-12).</td> | ||
+ | </tr> | ||
+ | <tr> | ||
+ | <td><a target="_blank" href ="https://www.ncbi.nlm.nih.gov/pubmed/16930615">[4]</a></td> | ||
+ | <td>Brockmeier U., Caspers M., Freudl R., Jockwer A., Noll T. and Eggert T. (2013) Systematic screening of all signal peptides from <i>Bacillus subtilis</i>: a powerful strategy in optimizing heterologous protein secretion in Gram-positive bacteria. <i> Journal of molecular biology 362</i>, 3 (393-402).</td> | ||
+ | </tr> | ||
+ | <tr> | ||
+ | <td><a target="_blank" href ="https://www.ncbi.nlm.nih.gov/pubmed/27927208">[5]</a></td> | ||
+ | <td>Hemmerich J., Rohe P., Kleine B., Jurischka S., Wiechert W., Freudl R. and Oldiges M. (2016) Use of a Sec signal peptide library from <i>Bacillus subtilis</i> for the optimization of cutinase secretion in <i>Corynebacterium glutamicum</i>. <i>Mircobial Cell Factories 15</i>, 208.</td> | ||
+ | </tr> | ||
+ | <tr> | ||
+ | <td><a target="_blank" href ="https://www.ncbi.nlm.nih.gov/pubmed/27516938">[6]</a></td> | ||
+ | <td>Pechsrichuang P., Songsiriritthigul C., Haltrich D., Roytrakul S., Namvijtr P., Bonaparte N., Yamabhai M. (2016) OmpA signal peptide leads to heterogenous secretion of <i>B. subtilis</i> chitosanase enzyme from <i>E. coli</i> expression system. <i>Springerplus 5</i>, 1200.</td> | ||
+ | </tr> | ||
+ | <tr> | ||
+ | <td><a target="_blank" href ="https://www.ncbi.nlm.nih.gov/pubmed/24295448">[7]</a></td> | ||
+ | <td>Radeck, J., Kraft, K., Bartels, J., Cikovic, T., Dürr, F., Emenegger, J., Kelterborn, S., Sauer, C., Fritz, G., Gebhard, S., and Mascher, T. (2013) The <i>Bacillus</i> BioBrick Box: generation and evaluation of essential genetic building blocks for standardized work with <i>Bacillus subtilis. J Biol Eng 7</i>, 29.</td> | ||
+ | </tr> | ||
+ | <tr> | ||
+ | <td><a target="_blank" href ="https://www.ncbi.nlm.nih.gov/pubmed/16500607">[8]</a></td> | ||
+ | <td>Xiao Z., Storms R. and Tsang A. (2007) A quantitative starch-iodine method for measuring alpha-amylase and glucoamylase activities. <i>Analytical Biochemistry 351</i>, 1 (146-148).</td> | ||
+ | </tr> | ||
+ | </table> | ||
+ | </div> | ||
</main> | </main> | ||
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