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Functional characterization of salt‐tolerant microbial esterase WDEst17 and its use in the generation of optically pure ethyl ( R )‐3‐hydroxybutyrate
Author(s) -
Wang Yilong,
Xu Yongkai,
Zhang Yun,
Sun Aijun,
Hu Yunfeng
Publication year - 2018
Publication title -
chirality
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.43
H-Index - 77
eISSN - 1520-636X
pISSN - 0899-0042
DOI - 10.1002/chir.22847
Subject(s) - esterase , chemistry , biocatalysis , enantiomer , kinetic resolution , enantiomeric excess , salt (chemistry) , enzyme , organic chemistry , stereochemistry , combinatorial chemistry , catalysis , enantioselective synthesis , reaction mechanism
The two enantiomers of ethyl 3‐hydroxybutyrate are important intermediates for the synthesis of a great variety of valuable chiral drugs. The preparation of chiral drug intermediates through kinetic resolution reactions catalyzed by esterases/lipases has been demonstrated to be an efficient and environmentally friendly method. We previously functionally characterized microbial esterase PHE21 and used PHE21 as a biocatalyst to generate optically pure ethyl ( S )‐3‐hydroxybutyrate. Herein, we also functionally characterized one novel salt‐tolerant microbial esterase WDEst17 from the genome of Dactylosporangium aurantiacum subsp. Hamdenensis NRRL 18085. Esterase WDEst17 was further developed as an efficient biocatalyst to generate ( R )‐3‐hydroxybutyrate, an important chiral drug intermediate, with the enantiomeric excess being 99% and the conversion rate being 65.05%, respectively, after process optimization. Notably, the enantio‐selectivity of esterase WDEst17 was opposite than that of esterase PHE21. The identification of esterases WDEst17 and PHE21 through genome mining of microorganisms provides useful biocatalysts for the preparation of valuable chiral drug intermediates.