Authors: Zhixia Zhong Zhinan Xu Li Peng Lei Huang Xiangming Fang Peilin Cen
Publish Date: 2005/12/02
Volume: 71, Issue: 5, Pages: 661-667
Abstract
Human betadefensin2 hBD2 is a cysteinerich cationic antimicrobial peptide with low molecular weight that exhibits a broad range of antimicrobial activity To improve the expression level of hBD2 in Escherichia coli tandem repeats of mature hBD2 gene were constructed and expressed as fusion proteins TrxAnmhBD2 n=1 2 4 8 by constructing the vectors of pET32nsmhBD2 n=1 2 4 8 The results showed that the tandem repeats of mhBD2 gene were highly expressed in our constructed system Comparing the expression levels of soluble mhBD2 BL21DE3/pET322smhBD2 was selected as an ideal recombinant strain for mature hBD2 production Under the optimized conditions of cultivation and isopropylthiogalactoside IPTG induction the maximum expression level of soluble mature hBD2 076 g/l with the highest percentage of fusion protein in soluble proteins 622 was obtained in the present work which was the highest yield of hBD2 reported so far
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