Polycationic amino acid tags enhance soluble expression of Candida antarctica lipase B in recombinant Escherichia coli
- Authors
- Jung, Hyun-Jung; Kim, Sun-Ki; Min, Won-Ki; Lee, Sung-Suk; Park, Kyungmoon; Park, Yong-Cheol; Seo, 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.
- Files in This Item
- There are no files associated with this item.
- Appears in
Collections - College of Science and Technology > Department of Biological and Chemical Engineering > 1. Journal Articles
![qrcode](https://api.qrserver.com/v1/create-qr-code/?size=55x55&data=https://scholarworks.bwise.kr/hongik/handle/2020.sw.hongik/19817)
Items in ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.