Abstract

The enzymatic kinetic resolution of a broad set of beta-amino ketones was investigated by using a collection of 16 Baeyer-Villiger monooxygenases from different bacterial origins, which display various substrate specificities. Within this platform of enzymes excellent enantioselectivities (E>200) were found towards aliphatic and aromatic 4-amino-2-ketones, and some enzymes even showed opposite enantioselectivity. The intermediate beta-aminoalkyl acetates underwent autohydrolysis yielding optically pure beta-amino alcohols, which are key intermediates in the synthesis of natural products and bioactive compounds of high interest for the pharmaceutical industry. Furthermore, in some cases the abnormal esters were formed.

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