Home > Publications database > Use of a Sec signal peptide library from Bacillus subtilis for the optimization of cutinase secretion in Corynebacterium glutamicum > print

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024 7 _ |a 10.1186/s12934-016-0604-6
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082 _ _ |a 610
100 1 _ |a Hemmerich, Johannes
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245 _ _ |a Use of a Sec signal peptide library from Bacillus subtilis for the optimization of cutinase secretion in Corynebacterium glutamicum
260 _ _ |a London
|c 2016
|b Biomed Central
336 7 _ |a article
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520 _ _ |a Technical bulk enzymes represent a huge market, and the extracellular production of such enzymes is favorable due to lowered cost for product recovery. Protein secretion can be achieved via general secretion (Sec) pathway. Specific sequences, signal peptides (SPs), are necessary to direct the target protein into the translocation machinery. For example, >150 Sec-specific SPs have been identified for Bacillus subtilis alone. As the best SP for a target protein of choice cannot be predicted a priori, screening of homologous SPs has been shown to be a powerful tool for different expression organisms. While SP libraries between closely related species were successfully applied to optimize recombinant protein secretion, this was not investigated for distantly related species. Therefore, in this study a Sec SP library from low-GC firmicutes B. subtilis is investigated to optimize protein secretion in high-GC actinobacterium Corynebacterium glutamicum using cutinase from Fusarium solani pisi as model protein. [...]
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700 1 _ |a Rohe, Peter
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700 1 _ |a Kleine, Britta
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700 1 _ |a Jurischka, Sarah-Kristin
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700 1 _ |a Wiechert, Wolfgang
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700 1 _ |a Freudl, Roland
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700 1 _ |a Oldiges, Marco
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773 _ _ |a 10.1186/s12934-016-0604-6
|g Vol. 15, no. 1, p. 208
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|t Microbial cell factories
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