site > International journal > (2011) Polycationic amino acid tags enhance soluble expression of Candida antarctica lipase B in recombinant Escherichia coli.

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작성일 : 12-07-18 08:53

(2011) Polycationic amino acid tags enhance soluble expression of Candida antarctica lipase B in recombinant Escherichia coli.

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http://www.springerlink.com/content/t5172v4787505850/ [471]

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

Hyun-Jung Jung, Sun-Ki Kim, Won-Ki Min, Sung-Suk Lee, Kyungmoon Park, Yong-Cheol Park* and Jin-Ho Seo
Bioprocess and Biosystems Engineering. 34(7): 833-839, 2011.09.01
(SCI I/F: 1.809)

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 2TM (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 ± 0.03 U/mg protein, corresponding to a fourfold enhancement compared with the authentic CalB.

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