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Efficient biosynthesis of a Cecropin A-melittin mutant in Bacillus subtilis WB700.


ABSTRACT: The efficient production of antimicrobial peptides (AMPs) for clinical applications has attracted the attention of the scientific community. To develop a novel microbial cell factory for the efficient biosynthesis of a cecropin A-melittin mutant (CAM-W), a recombinant Bacillus subtilis WB700 expression system was genetically modified with a novel vector, including a fusion gene encoding CAM-W, the autoprotease EDDIE and the signal peptide SacB under the control of the maltose-inducible promoter Pglv. A total of 159?mg of CAM-W was obtained from 1?L of fermentation supernatant. The purified CAM-W showed a consistent size with the expected molecular weight of 3.2?kDa. Our findings suggest that this novel expression system can be used as a powerful tool for the efficient production of CAM-W.

SUBMITTER: Ji S 

PROVIDER: S-EPMC5223193 | biostudies-literature | 2017 Jan

REPOSITORIES: biostudies-literature

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Efficient biosynthesis of a Cecropin A-melittin mutant in Bacillus subtilis WB700.

Ji Shengyue S   Li Weili W   Baloch Abdul Rasheed AR   Wang Meng M   Li Hengxin H   Cao Binyun B   Zhang Hongfu H  

Scientific reports 20170110


The efficient production of antimicrobial peptides (AMPs) for clinical applications has attracted the attention of the scientific community. To develop a novel microbial cell factory for the efficient biosynthesis of a cecropin A-melittin mutant (CAM-W), a recombinant Bacillus subtilis WB700 expression system was genetically modified with a novel vector, including a fusion gene encoding CAM-W, the autoprotease EDDIE and the signal peptide SacB under the control of the maltose-inducible promoter  ...[more]

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