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.

摘要

酶催化的酯交换反应是实现拆分外消旋光学活性仲醇的重要途径。然而，由于使用乙烯基酯作为酰基供体，因此该路线遭受高环境和工程风险。在这项工作中，使用了另一种酰基供体丁酸乙酯，因为它对环境和催化剂均更友好。进行了固定化脂肪酶Novozym™435催化的1-苯基乙醇与丁酸乙酯酯交换反应的动力学研究。研究了搅拌速度，反应温度，催化剂负载量和反应物初始摩尔比的影响。Ping-Pong-Bi-Bi模型和伪均质模型用于关联实验数据以估算动力学参数。将基于浓度的Ping-Pong-Bi-Bi模型转换为基于活性的形式，以描述脂肪酶催化的反应系统的非理想性。在所有使用的模型中，基于活动的Ping-Pong-Bi-Bi动力学模型表现最佳。