Characterization of a new esterase for enantioselective resolution of (R, S)-methyl mandelate

Characterization of a new esterase for enantioselective resolution of (R, S)-methyl mandelate

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...

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Veröffentlicht in:Materials express 2019-12, Vol.9 (9), p.1112-1119
Hauptverfasser: Xie, Haiwei, Chen, Yongzhi, Deng, Dun
Format: Artikel
Sprache:eng
Schlagworte:
(r)-Methyl Mandelate
Catalytic activity
Cyclohexane
E coli
Enantiomers
Enantioselective
Enzymes
Esterase
Heptanes
Lipolytic Enzymes Of Family X
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Zusammenfassung: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.
ISSN:2158-5849
2158-5857
DOI:10.1166/mex.2019.1604