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Biomolecules 2013, 3(3), 449-460; doi:10.3390/biom3030449
Article

Enantiocomplementary Yarrowia lipolytica Oxidoreductases: Alcohol Dehydrogenase 2 and Short Chain Dehydrogenase/Reductase

1
, 1,2
, 1
, 3
, 3
 and 1,*
1 ACIB (Austrian Centre of Industrial Biotechnology) GmbH, Petersgasse 14/III, Graz 8010, Austria 2 Institute of Organic Chemistry, TU Graz, Stremayrgasse 9, Graz 8010, Austria 3 LONZA AG, Rottenstrasse 6, Visp 3930, Switzerland
* Author to whom correspondence should be addressed.
Received: 3 July 2013 / Revised: 31 July 2013 / Accepted: 2 August 2013 / Published: 12 August 2013
(This article belongs to the Special Issue Enzymes and Their Biotechnological Applications)
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Abstract

Enzymes of the non-conventional yeast Yarrowia lipolytica seem to be tailor-made for the conversion of lipophilic substrates. Herein, we cloned and overexpressed the Zn-dependent alcohol dehydrogenase ADH2 from Yarrowia lipolytica in Escherichia coli. The purified enzyme was characterized in vitro. The substrate scope for YlADH2 mediated oxidation and reduction was investigated spectrophotometrically and the enzyme showed a broader substrate range than its homolog from Saccharomyces cerevisiae. A preference for secondary compared to primary alcohols in oxidation direction was observed for YlADH2. 2-Octanone was investigated in reduction mode in detail. Remarkably, YlADH2 displays perfect (S)-selectivity and together with a highly (R)-selective short chain dehydrogenase/ reductase from Yarrowia lipolytica it is possible to access both enantiomers of 2-octanol in >99% ee with Yarrowia lipolytica oxidoreductases.
Keywords: Zn-dependent alcohol dehydrogenase; Yarrowia lipolytica; biooxidation; short chain dehydrogenase/reductase; medium chain secondary alcohols; enantioselective reduction Zn-dependent alcohol dehydrogenase; Yarrowia lipolytica; biooxidation; short chain dehydrogenase/reductase; medium chain secondary alcohols; enantioselective reduction
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Napora-Wijata, K.; Strohmeier, G.A.; Sonavane, M.N.; Avi, M.; Robins, K.; Winkler, M. Enantiocomplementary Yarrowia lipolytica Oxidoreductases: Alcohol Dehydrogenase 2 and Short Chain Dehydrogenase/Reductase. Biomolecules 2013, 3, 449-460.

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