Abstract
The enzyme-mediated highly enantioselective hydrolysis of dicarboxylic acid monoesters was investigated. The racemic substrates, which were prepared by coupling of the corresponding alcohols with dicarboxylic anhydrides, were enantioselectively hydrolyzed by lipase from Candida antarctica (Novozym 435) in a buffer at 30 °C. The products were easily separated by a simple extraction procedure without laborious column chromatography to afford both enantiomers of the alcohols. We then determined that the dicarboxylic acid monoesters were suitable alternative substrates for the preparation of optically active alcohols.
Keywords: Dicarboxylic acid monoesters, enzymatic hydrolysis, kinetic resolution, lipase, optically active alcohols, enantioselectivity, esterification, enantiomeric, 3-methylglutaric acid monoester, substrates
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