Optimization of a heterologous signal peptide by site-directed mutagenesis for improved secretion of recombinant proteins in escherichia coli
A heterologous signal peptide (SP) from Bacillus sp. G1 was optimized for secretion of recombinant cyclodextrin glucanotransferase (CGTase) to the periplasmic and, eventually, extracellular space of Escherichia coli. Eight mutant SPs were constructed using site-directed mutagenesis to improve the se...
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Main Authors: | , , , , , , , |
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Format: | Article |
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2012
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Online Access: | http://eprints.utm.my/id/eprint/47318/ http://dx.doi.org/10.1159/000336524 |
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