CANDIDA-ANTARCTICA LIPASE-B CATALYZED KINETIC RESOLUTIONS - SUBSTRATESTRUCTURE REQUIREMENTS FOR THE PREPARATION OF ENANTIOMERICALLY ENRICHED SECONDARY ALCANOLS

The lipase B of the Candida antarctica yeast displays high enantiosele ctivity in transesterification reactions with chiral secondary alcohol s in non-aqueous media. This was exploited to resolve a series of race mates structurally related to 2-octanol, namely 3-hydroxy-1-undecyne, 3-hydroxy-1-nonene, 3-nonanol, 1-chloro-2-octanol, 2-methyl-3-nonanol, 2,2-dimethyl-3-nonanol. The substrates were designed to probe the alc ohol binding part of the active site of the lipase. The first four rac emates could be resolved to produce compounds of high enantiomeric pur ity. A lipase catalysed transesterification of 1-chloro-2-octanol was observed. 2-Methyl-3-nonanol and 2,2-dimethyl-3-nonanol did not form a ny detectable amounts of product ester. The kinetic resolutions of the alcohols were performed with S-ethyl thiooctanoate as the acyl donor.