Magomedova Zalina, Grecu Andreea, Sensen Christoph W, Schwab Helmut, Heidinger Petra
Institute of Molecular Biotechnology, Graz University of Technology, NAWI Graz, Petersgasse 14/1, A-8010 Graz, Austria.
Institute of Molecular Biotechnology, Graz University of Technology, NAWI Graz, Petersgasse 14/1, A-8010 Graz, Austria.
J Biotechnol. 2016 Mar 10;221:78-90. doi: 10.1016/j.jbiotec.2016.01.030. Epub 2016 Jan 23.
Biocatalysis has significant advantages over organic synthesis in the field of chiral molecule production and several types of stereoselective enzymes are already in use in industrial biotechnology. However, there is still a high demand for new enzymes capable of transforming bulky molecules with sufficient operability. In order to reveal novel high-potential biocatalysts, the complete genome of the β-proteobacterium Ralstonia eutropha H16 was screened for potential short-chain dehydrogenases/reductases (SDRs). We were able to identify two (S)-enantioselective SDRs named A5 and B3. These showed clear preference towards long-chain and aromatic secondary alcohols, aldehydes and ketones, with diaryl diketone benzil as one of the best substrates. In addition the phylogenetic analysis of all enzyme types, which are known to facilitate benzil reduction, revealed at least two separate evolutionary clusters. Our results indicate the biotechnological potential of SDRs A5 and B3 for the production of chiral compounds with potential commercial value.
