Issue 10, 2007
From the journal:

Chemical Communications

Identification of Candida tenuisxylose reductase as highly selective biocatalyst for the synthesis of aromatic α-hydroxyesters and improvement of its efficiency by protein engineering†

Regina Kratzera  and  Bernd Nidetzky*a  

* Corresponding authors

a Research Centre Applied Biocatalysis, Petersgasse 14, A-8010 Graz, Austria c/o Institute of Biotechnology and Biochemical Engineering, Graz University of Technology, Petersgasse 12/I, A-8010 Graz, Austria
E-mail: bernd.nidetzky@tugraz.at
Fax: +43 316 873 8434
Tel: +43 316 873 8400

Abstract

Wild-type Candida tenuisxylose reductase and two Trp-23 mutants thereof catalyze NADH-dependent reduction of a homologous series of aromatic α-keto esters with absolute pseudo re-face stereoselectivity and broad tolerance for the substituent on the aromatic ring, producing the corresponding R-alcohols in high yield.

Graphical abstract: Identification of Candida tenuisxylose reductase as highly selective biocatalyst for the synthesis of aromatic α-hydroxyesters and improvement of its efficiency by protein engineering

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Article information

DOI
https://doi.org/10.1039/B616475G
Article type
Communication
Submitted
10 Nov 2006
Accepted
15 Jan 2007
First published
26 Jan 2007

Chem. Commun., 2007, 1047-1049

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Identification of Candida tenuisxylose reductase as highly selective biocatalyst for the synthesis of aromatic α-hydroxyesters and improvement of its efficiency by protein engineering

R. Kratzer and B. Nidetzky, Chem. Commun., 2007, 1047 DOI: 10.1039/B616475G

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