Characterization of a new esterase for enantioselective resolution of (R,S)-methyl mandelate
文献类型： 外文期刊
作者： Xie, Haiwei 1 ; Chen, Yongzhi 1 ; Deng, Dun 2 ;
作者机构： 1.Huizhou Univ, Sch Life Sci, Huizhou 516007, Peoples R China
2.Guangdong Acad Agr Sci, State Key Lab Livestock & Poultry Breeding, Inst Anim Sci, Guangzhou 510640, Guangdong, Peoples R China
关键词： Lipolytic Enzymes of Family X; Esterase; Enantioselective; (R)-Methyl Mandelate
期刊名称：MATERIALS EXPRESS （ 影响因子：1.65； 五年影响因子：1.614 ）
ISSN： 2158-5849
年卷期： 2019 年 9 卷 9 期
页码：
收录情况： SCI
摘要： 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 degrees C and it could be activated at 0 degrees 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.
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