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

Biomolecules

Kamila Napora-Wijata¹  Gernot A. Strohmeier¹  Manoj N. Sonavane¹  Manuela Avi²  Karen Robins² 

[1] ACIB (Austrian Centre of Industrial Biotechnology) GmbH, Petersgasse 14/III, Graz 8010, Austria; E-Mails:;LONZA AG, Rottenstrasse 6, Visp 3930, Switzerland; E-Mails:

关键词: Zn-dependent alcohol dehydrogenase;    Yarrowia lipolytica;    biooxidation;    short chain dehydrogenase/reductase;    medium chain secondary alcohols;    enantioselective reduction;   

DOI  :  10.3390/biom3030449

来源: mdpi

【 摘 要 】

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.

【 授权许可】

CC BY   
© 2013 by the authors; licensee Molecular Diversity Preservation International, Basel, Switzerland.