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- W4247667069 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." @default.
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- W4247667069 date "2019-12-01" @default.
- W4247667069 modified "2023-10-18" @default.
- W4247667069 title "Characterization of a new esterase for enantioselective resolution of (R, S)-methyl mandelate" @default.
- W4247667069 doi "https://doi.org/10.1166/mex.2019.1604" @default.
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