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Polycationic amino acid tags enhance soluble expression of Candida antarctica lipase B in recombinant Escherichia coli

Authors
Jung, Hyun-JungKim, Sun-KiMin, Won-KiLee, Sung-SukPark, KyungmoonPark, Yong-CheolSeo, Jin-Ho
Issue Date
Sep-2011
Publisher
SPRINGER
Keywords
Candida antarctica lipase B; Escherichia coli; Polycationic amino acid tag; Soluble expression; Inclusion body
Citation
BIOPROCESS AND BIOSYSTEMS ENGINEERING, v.34, no.7, pp.833 - 839
Journal Title
BIOPROCESS AND BIOSYSTEMS ENGINEERING
Volume
34
Number
7
Start Page
833
End Page
839
URI
https://scholarworks.bwise.kr/hongik/handle/2020.sw.hongik/19817
DOI
10.1007/s00449-011-0533-z
ISSN
1615-7591
Abstract
Lipase (EC 3.1.1.3) is a popular enzyme used as an ingredient in detergents and biocatalyst in many biochemical reactions. Lipase is usually expressed in Escherichia coli as an inactive inclusion body and at a low level. In this study, Candida antarctica lipase B (CalB) was fused with various polycationic amino acid tags and expressed in E. coli in order to increase a soluble expression level. By induction with 1.0 mM IPTG, the authentic and fused CalBs were expressed at 27-56% of total protein. The 10-arginine and 10-lysine tags fused at the C-terminal of CalB significantly increased the solubility of CalB by five- to ninefold, relative to the case of the authentic CalB expressed in a recombinant E. coli Origami 2(TM) (DE3) strain. Among a series of the C-terminal poly-arginine tags, the recombinant CalB combined with the 10-arginine tag (CalB-R10) possessed the highest lipase specific activity of 9.5 +/- A 0.03 U/mg protein, corresponding to a fourfold enhancement compared with the authentic CalB.
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