title: Enantiocomplementary Yarrowia lipolytica Oxidoreductases: Alcohol Dehydrogenase 2 and Short Chain Dehydrogenase/Reductase.
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.
authors: ACIB (Austrian Centre of Industrial Biotechnology) GmbH, Petersgasse 14/III, Graz 8010, Austria. kamila.napora@acib.at.
authors: Kamila
authors: K
authors: Napora-Wijata
authors: ACIB (Austrian Centre of Industrial Biotechnology) GmbH, Petersgasse 14/III, Graz 8010, Austria. gernot.strohmeier@acib.at.
authors: Gernot A
authors: GA
authors: Strohmeier
authors: ACIB (Austrian Centre of Industrial Biotechnology) GmbH, Petersgasse 14/III, Graz 8010, Austria. manojsonavane4@gmail.com.
authors: Manoj N
authors: MN
authors: Sonavane
authors: LONZA AG, Rottenstrasse 6, Visp 3930, Switzerland. m.avi@gmx.net.
authors: Manuela
authors: M
authors: Avi
authors: LONZA AG, Rottenstrasse 6, Visp 3930, Switzerland. karen.robins@lonza.com.
authors: Karen
authors: K
authors: Robins
authors: ACIB (Austrian Centre of Industrial Biotechnology) GmbH, Petersgasse 14/III, Graz 8010, Austria. margit.winkler@acib.at.
authors: Margit
authors: M
authors: Winkler