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Background  One-pot multi-step biocatalysis is advantageous over step-by-step synthesis as it reduces the number of process operation units, leading to significant process intensification. Whole-cell biocatalysis with metabolically active cells is especially valuable since all enzymes can be co-expressed in the cell whose metabolism can be exploited for supply of co-substrates and co-factors.    Results  In this study, a heterologous enzymatic system consisting of ω-transaminase and ketone reductase was introduced in  Saccharomyces cerevisiae , and evaluated for one-pot stereo-selective conversion of amines to alcohols. The system was applied for simultaneous kinetic resolution of  racemic  1-phenylethylamine to ( R )-1-phenylethylamine and reduction of the ketone intermediate to ( R )-1-phenylethanol. Glucose was used as sole co-substrate for both the supply of amine acceptor and the regeneration of NADPH in the reduction step.    Conclusions  The whole-cell biocatalyst was shown to sustain transaminase-reductase-catalyzed enantioselective conversion of amines to alcohols with glucose as co-substrate. The transamination catalyzed by recombinant vanillin aminotransferase from  Capsicum chinense  proved to be the rate-limiting step as a three-fold increase in transaminase gene copy number led to a two-fold increased conversion. The ( R )-selective NADPH-dependent alcohol dehydrogenase from  Lactobacillus kefir  proved to be efficient in catalyzing the reduction of the acetophenone generated in the transamination reaction.

Engineered baker’s yeast as whole-cell biocatalyst for one-pot stereo-selective conversion of amines to alcohols