Affordable Access

Publisher Website

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.

There are no comments yet on this publication. Be the first to share your thoughts.

Statistics

Seen <100 times
0 Comments