In vitro characterization of an enzymatic redox cascade composed of an alcohol dehydrogenase, an enoate reductases and a Baeyer-Villiger monooxygenase.
Bottom Line: An artificial enzyme cascade composed of an alcohol dehydrogenase, an enoate reductase and a Baeyer-Villiger monooxygenase was investigated in vitro to gain deeper mechanistic insights and understand the assets and drawbacks of this multi-step biocatalysis.Several substrates composed of different structural motifs were examined and provided access to functionalized chiral compounds in high yields (up to >99%) and optical purities (up to >99%).Hence, the applicability of the presented enzymatic cascade was exploited for the synthesis of biorenewable polyesters.
Affiliation: Institute of Applied Synthetic Chemistry, Vienna University of Technology, Getreidemarkt 9/163-OC, 1060 Vienna, Austria.Show MeSH
Mentions: For a better comparison of the in vitro with the in vivo cascades we further investigated a non-sequential reaction approach by mixing starting material, all enzymes and cofactors at once. By applying this one pot, single operation protocol we observed a significant increase in the production of the undesired by-product dihydrocarveol (6c-ol) in comparison to the sequential cascade of (1S,5R)-carveol (6a) (Fig. 4).
Affiliation: Institute of Applied Synthetic Chemistry, Vienna University of Technology, Getreidemarkt 9/163-OC, 1060 Vienna, Austria.