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Asymmetric reduction of ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate with two co-existing, recombinant Escherichia coli strains

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Abstract

Two recombinant strains, E. coli M15 (pQE30-alr0307) and E. coli M15 (pQE30-gdh0310), which were constructed to express, respectively, an NADPH-dependent aldehyde reductase gene and a glucose dehydrogenase gene, were mixed in an appropriate ratio and used for the asymmetric reduction of ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. The former strain acted as catalyst and the latter functioned in NADPH regeneration. The biotransformation was completed effectively without any addition of glucose dehydrogenase or NADP+/NADPH. An optical purity of 99% (ee) was obtained and the product yield reached 90.5% from 28.5 mM substrate.

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Correspondence to Zhinan Xu.

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Revisions requested 27 July 2004/23 September 2004; Revisions received 21 September 2004/29 November 2004

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Liu, Y., Xu, Z., Jing, K. et al. Asymmetric reduction of ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate with two co-existing, recombinant Escherichia coli strains. Biotechnol Lett 27, 119–125 (2005). https://doi.org/10.1007/s10529-004-7336-0

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  • DOI: https://doi.org/10.1007/s10529-004-7336-0

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