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Production of chiral alcohols by enantioselective reduction with NADH-dependent phenylacetaldehyde reductase fromCorynebacteriumstrain, ST-10

Authors
Journal
Journal of Molecular Catalysis B Enzymatic
1381-1177
Publisher
Elsevier
Publication Date
Volume
6
Identifiers
DOI: 10.1016/s1381-1177(98)00118-0
Keywords
  • Chiral Alcohol
  • (S)-1-Phenylethanol
  • (S)-2-Alkanol
  • Enzymatic Reduction
  • Phenylacetaldehyde Reductase (Nadh)
  • Corynebacteriumsp.
Disciplines
  • Biology
  • Chemistry

Abstract

Abstract Phenylacetaldehyde reductase (PAR) (systematic name, 2-phenylethanol: NAD + oxidoreductase) isolated from styrene-assimilating Corynebacterium strain ST-10 was used to produce chiral alcohols. This enzyme with a broad substrate range reduced various prochiral 2-alkanones and aromatic ketones to yield optically active secondary alcohols with an enantiomeric purity of 87–100% enantiomeric excess (e.e.). The stereochemistry of PAR revealed that the pro-R hydrogen of NADH was transferred to carbonyl moiety of acetophenone derivatives or alkanones through its re face. The combination with a NADH-regenerating system using formate dehydrogenase and formate was able to practically produce optically pure alcohols.

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