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Enhanced cecropin B2 production via chitin‐binding domain and intein self‐cleavage system
Author(s) -
Fang YiTing,
Lai WeiShiang,
Liu JyungHurng,
Liu YungChuan
Publication year - 2018
Publication title -
biotechnology and applied biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.468
H-Index - 70
eISSN - 1470-8744
pISSN - 0885-4513
DOI - 10.1002/bab.1716
Subject(s) - intein , cecropin , cleavage (geology) , chitin , peptide , recombinant dna , antimicrobial peptides , antimicrobial , staphylococcus aureus , microbiology and biotechnology , escherichia coli , chemistry , biology , biochemistry , bacteria , gene , chitosan , genetics , rna , paleontology , fracture (geology) , rna splicing
In this study, various constructs and hosts were used to produce high levels of cecropin B2 (cecB2). To mitigate cecB2's toxic inhibition of host cells, various cecB2 constructs were built. Results showed that the combination of a chitin‐binding domain and an intein self‐cleavage motif in front of cecropin B2, without a His‐tag, was best for cecB2 expression. E. coli ER2566 was the best host, and 2YT was the best medium for cultivation. Under these conditions, a cecB2 yield of 98.2 mg/L could be obtained after purification. The purified cecB2 expressed a wide antimicrobial effect on most Gram‐negative strains, including multidrug‐resistant Acinetobactor baumannii and Staphylococcus aureus . This study provides a systematic approach to the efficient production of the antimicrobial peptide (AMP) cecB2 via the recombinant E. coli process, which is expected to be an efficient way for the production of other AMPs.