Reaction kinetic studies on the immobilized-lipase catalyzed enzymatic resolution of 1-phenylethanol transesterification with ethyl butyrate

Abstract

The enzyme-catalyzed transesterification reaction is an important route to realize the resolution of racemic optically active secondary alcohols. However, this route suffers from the high environment and engineering risks due to the usage of vinyl ester as acyl donor. In this work, an alternative acyl donor, ethyl butyrate, was used because it is more environment-friendly and catalyst-friendly. The kinetic studies on transesterification of 1-phenylethanol with ethyl butyrate catalyzed by immobilized-lipase Novozym™ 435 were carried out. The effects of agitation speed, reaction temperature, catalyst loading and initial molar ratio of reactants were investigated. The Ping-Pong-Bi-Bi and pseudo-homogeneous models were used to correlate the experimental data to estimate the kinetic parameters. The concentration-based Ping-Pong-Bi-Bi model was translated into its activity-based form to describe the non-ideality of the lipase-catalyzed reaction system. The activity-based Ping-Pong-Bi-Bi kinetic model performed best among all the models used.