Neat lipase-catalysed kinetic resolution of racemic 1-phenylethanol and a straightforward modelling of the reaction

Abstract

Enzymatic kinetic resolution of racemic 1-phenylethanol catalysed by immobilized Candida antarctica lipase B was investigated in a neat system at the temperature range of 30–70 °C. Synthetic triglycerides, namely glycerol triacetate and glycerol tributyrate, were applied as the esterification agents. Both esterification agents were efficient regarding to the enantioselectivity (>1000). Initial rate of reaction and the kinetic constants were influenced by the applied esterification agent significantly. A detailed modelling approach is presented and verified in the temperature range on 30–60 °C for the tributyrin system.