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- W628093669 abstract "The use of enzymes as catalysts in enantioselective ketone reduction has gained broad synthetic interest in organic chemistry since this biocatalytic methodology was found to be a versatile, robust, efficient, and industrially feasible synthetic approach toward enantiomerically pure alcohols. In such processes, which are based on the use of isolated enzymes, immobilized enzymes, and recombinant whole-cell catalysts, respectively, different types of cofactor regenerations based in particular on substrate- and enzyme-coupled methods have been successfully applied. The advantages of these types of alcohol dehydrogenase (ADH)-catalyzed ketone reductions are not only the well-known excellent enantio-, diastereo-, and regioselectivities of enzymes but also the high volumetric productivities and excellent substrate loadings that are tolerated by many (recombinant) biocatalyst systems. With respect to the search for suitable ADHs, a broad range of well-established screening tools have been developed. In addition, numerous recombinant ADHs are already available, and the known ADHs show a broad, often complementary substrate spectrum. Furthermore, biocatalytic ketone reductions have also demonstrated their suitability to be combined with other enzymatic or ‘classic’ chemical or chemocatalytic reaction steps toward chemoenzymatic one-pot multistep processes." @default.
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- W628093669 date "2012-01-01" @default.
- W628093669 modified "2023-09-26" @default.
- W628093669 title "Asymmetric Biocatalytic Reduction of Ketones" @default.
- W628093669 hasPublicationYear "2012" @default.
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