Characterization of a new esterase for enantioselective resolution of (R, S)-methyl mandelate
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Published:2019-12-01
Issue:9
Volume:9
Page:1112-1119
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ISSN:2158-5849
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Container-title:Materials Express
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language:en
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Short-container-title:mat express
Author:
Xie Haiwei,Chen Yongzhi,Deng Dun
Abstract
A new esterase gene (EST35) was cloned from Dactylosporangium sp. BB08 and expressed in E. coli BL21 (DE3). Optimum catalytic activity of EST35 was at 30 C and it could be activated at 0 °C. EST35 remained high activity in 20% (V/V) cyclohexane,
hexane, heptane, methanol and DMSO. Interestingly the enzyme exhibits good enantioselectivity towards (R, S)-methyl mandelate leaving with an optical purity of 97% (R)-methyl mandelate and make EST35 a promising enzyme for biotechnology application.
Publisher
American Scientific Publishers
Subject
General Materials Science