Journal
BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY
Volume 79, Issue 7, Pages 1090-1093Publisher
TAYLOR & FRANCIS LTD
DOI: 10.1080/09168451.2015.1012145
Keywords
coenzyme regeneration; (S)- 4-chloro-3-hydroxybutanoate; NADPH-dependent sorbose reductase; Candida albicans
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Funding
- National Basic Research Program of China [2011CBA0807]
- National High Technology Research and Development Program of China [2012AA022101]
- Priority Academic Program Development of Jiangsu Higher Education Institutions [1001020B]
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An NADPH-dependent sorbose reductase from Candida albicans was identified to catalyze the asymmetric reduction of ethyl 4-chloro-3-oxobutanoate (COBE). The activity of the recombinant enzyme toward COBE was 6.2 U/mg. The asymmetric reduction of COBE was performed with two coexisting recombinant Escherichia coli strains, in which the recombinant E. coli expressing glucose dehydrogenase was used as an NADPH regenerator. An optical purity of 99% (e.e.) and a maximum yield of 1240mM (S)-4-chloro-3-hydroxybutanoate were obtained under an optimal biomass ratio of 1:2. A highest turnover number of 53,900 was achieved without adding extra NADP(+)/NADPH compared with those known COBE-catalytic systems.
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