Abstract
The lipase from wheat germ was used for the kinetic resolution of secondary alcohols. It has the opposite enantioselectivity against the Kazlauskas rule and acts as an anti-Kazlauskas catalyst. The effect of initial water activity, organic solvent, acyl donor and temperature were investigated. Wheat germ lipase had a high activity and enantioselectivity only in n-hexane with a high initial water activity (alpha(w) = 0.97), especially with 1-phenylethanol (C 32%, E > 200). Its performance changed little with the chain length of acyl donor and temperature.
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