Enhanced cecropin B2 production via chitin-binding domain and intein self-cleavage system.

Abstract:

: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.

authors

Fang YT,Lai WS,Liu JH,Liu YC

doi

10.1002/bab.1716

subject

Has Abstract

pub_date

2019-03-01 00:00:00

pages

209-215

issue

2

eissn

0885-4513

issn

1470-8744

journal_volume

66

pub_type

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