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Titolo:
Production of chiral alcohols by enantioselective reduction with NADH-dependent phenylacetaldehyde reductase from Corynebacterium strain, ST-10
Autore:
Itoh, N; Mizuguchi, N; Mabuchi, M;
Indirizzi:
Toyama Prefectural Univ, Biotechnol Res Ctr, Toyama 9390398, Japan Toyama Prefectural Univ Toyama Japan 9390398 Ctr, Toyama 9390398, Japan Fukui Univ, Dept Appl Chem & Biotechnol, Fac Engn, Fukui 9108507, Japan Fukui Univ Fukui Japan 9108507 iotechnol, Fac Engn, Fukui 9108507, Japan
Titolo Testata:
JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC
fascicolo: 1-2, volume: 6, anno: 1999,
pagine: 41 - 50
SICI:
1381-1177(19990104)6:1-2<41:POCABE>2.0.ZU;2-V
Fonte:
ISI
Lingua:
ENG
Soggetto:
CARBONYL REDUCTASE; DEHYDROGENASE; PURIFICATION; YEAST;
Keywords:
chiral alcohol; (S)-1-phenylethanol; (S)-2-alkanol; enzymatic reduction; phenylacetaldehyde reductase (NADH); Corynebacterium sp.;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Physical, Chemical & Earth Sciences
Citazioni:
21
Recensione:
Indirizzi per estratti:
Indirizzo: Itoh, N Toyama Prefectural Univ, Biotechnol Res Ctr, Kurokawa 5180, Toyama9390398, Toyama Prefectural Univ Kurokawa 5180 Toyama Japan 9390398 90398,
Citazione:
N. Itoh et al., "Production of chiral alcohols by enantioselective reduction with NADH-dependent phenylacetaldehyde reductase from Corynebacterium strain, ST-10", J MOL CAT B, 6(1-2), 1999, pp. 41-50

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 acetophenonederivatives 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. (C) 1999 Elsevier Science B.V. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 12/07/20 alle ore 13:18:22