A Novel Reductase from Candida albicans for the Production of Ethyl (S)-4-Chloro-3-hydroxybutanoate | Zendy

Mingdong An | Zendy; Ping Cai | Zendy; Ming Yan | Zendy; Ning Hao | Zendy; Shanshan Wang | Zendy; Huan Liu | Zendy; Yan Li | Zendy; Lin Xu | Zendy

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A Novel Reductase from <i>Candida albicans</i> for the Production of Ethyl (<i>S</i>)-4-Chloro-3-hydroxybutanoate

Author(s) -

Mingdong An,

Ping Cai,

Ming Yan,

Ning Hao,

Shanshan Wang,

Huan Liu,

Yan Li,

Lin Xu

Publication year - 2012

Publication title -

bioscience biotechnology and biochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.509

H-Index - 116

eISSN - 1347-6947

pISSN - 0916-8451

DOI - 10.1271/bbb.120048

Subject(s) - enantiomeric excess , biocatalysis , candida albicans , chemistry , stereochemistry , reductase , enantiomer , substrate (aquarium) , escherichia coli , catalysis , enzyme , nuclear chemistry , medicinal chemistry , biochemistry , biology , enantioselective synthesis , microbiology and biotechnology , gene , reaction mechanism , ecology

A novel NADPH-dependent reductase (CaCR) from Candida albicans was cloned for the first time. It catalyzed asymmetric reduction to produce ethyl (S)-4-chloro-3-hydroxybutanoate ((S)-CHBE). It contained an open reading frame of 843 bp encoding 281 amino acids. When co-expressed with a glucose dehydrogenase in Escherichia coli, recombinant CaCR exhibited an activity of 5.7 U/mg with ethyl 4-chloro-3-oxobutanoate (COBE) as substrate. In the biocatalysis of COBE to (S)-CHBE, 1320 mM (S)-CHBE was obtained without extra NADP+/NADPH in a water/butyl acetate system, and the optical purity of the (S)-isomer was higher than 99% enantiomeric excess.

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