Enzymatic resolutions of cyclic amino alcohol precursors

Abstract
Racemic butyrates of trans-2-azido as well as trans-2-nitro and trans-2-cyano cycloalkanols were hydrolysed to the corresponding optically active alcohols with the aid of lipases from Candida cylindracea and Pseudomonas sp. respectively. These precursors of amino alcohols could be produced in optical yields ranging from 85 to > 98% e.e. Differences in the catalytic behaviour of the two enzymes depending on ring sizes were observed.

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