Biocatalytic ketone reduction--a powerful tool for the production of chiral alcohols--part I: processes with isolated enzymes.

Enzymes are able to perform reactions under mild conditions, e.g., pH and temperature, with remarkable chemo-, regio-, and stereoselectivity.

Biocatalytic ketone reduction--a powerful tool for the production of chiral alcohols-part II: whole-cell reductions.

Enzymes are able to perform reactions under mild conditions, e.g., pH and temperature, with remarkable chemo-, regio-, and stereoselectivity.

Overcoming the thermodynamic limitation in asymmetric hydrogen transfer reactions catalyzed by whole cells.

Whole lyophilized cells of an Escherichia coli overexpressing the alcohol dehydrogenase (ADH-'A') from Rhodococcus ruber DSM 44541 were used for the asymmetric reduction of ketones to secondary alcohols. The recycling of the required nicotinamide cofactor (NADH) was achieved in a coupled-substrate process. In the course of the reaction the ketone is reduced to the alcohol and the hydrogen donor 2-propanol is oxidized to acetone by one enzyme.