Asymmetric synthesis of (S)-4-chloro-3-hydroxybutanoate by sorbose reductase from Candida albicans with two co-existing recombinant Escherichia coli strains

Bioscience, Biotechnology, and Biochemistry
Ping CaiLin Xu

Abstract

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 1240 mM (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.

References

Sep 22, 2000·Analytical Biochemistry·Z ZhangR C Stanton
Nov 10, 2009·Journal of Industrial Microbiology & Biotechnology·Tarjan KaliaperumalAnju Chadha
Jul 14, 2012·Bioscience, Biotechnology, and Biochemistry·Mingdong AnLin Xu

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Citations

Apr 9, 2017·Applied and Environmental Microbiology·Min LiJian-He Xu

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Methods Mentioned

BETA
PCR

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