Biocatalytic characterization of a short-chain alcohol dehydrogenase with broad substrate specificity from thermophilic Carboxydothermus hydrogenoformans.

Abstract:

:The gene encoding a novel short-chain alcohol dehydrogenase in the thermophilic bacterium, Carboxydothermus hydrogenoformans, was identified and overexpressed in Escherichia coli. The enzyme was thermally stable and displayed the highest activity at 70 °C and pH 6.0. It preferred NAD(H) over NADP(H) as a cofactor and exhibited broad substrate specificity towards aliphatic ketones, cycloalkanones, aromatic ketones, and ketoesters. Furthermore, ethyl benzoylformate was asymmetrically reduced by the purified enzyme, using an additional coupled NADH regeneration system, with 95 % conversion and in an enantiomeric excess of (99.9 %). The results of this study may lead to the discovery of a novel method for asymmetric reduction of alcohols, which is an important tool in organic synthesis.

journal_name

Biotechnol Lett

journal_title

Biotechnology letters

authors

Zhou S,Zhang SC,Lai DY,Zhang SL,Chen ZM

doi

10.1007/s10529-012-1082-5

subject

Has Abstract

pub_date

2013-03-01 00:00:00

pages

359-65

issue

3

eissn

0141-5492

issn

1573-6776

journal_volume

35

pub_type

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