为实现手性2-氯-1-苯乙醇两个高纯度对映体的酶法合成,考察了多种脂肪酶的动力学拆分效果,并探讨了有机溶剂、温度以及水活度对脂肪酶催化拆分(R,S)2-氯-1-1-苯乙醇的影响,研究了固定化酶的重复利用性.结果表明:一种来自Pseudomonas cepacia的固定化脂肪酶Lipase PSIM,在正己烷体系、35℃和水活度0.69时,能同时得到两个高纯度的对映体(eep99%,ees99%);经过5次重复反应后Lipase PSIM的相对酶活仍有85%.
Two enantiomers of chiral 2-chloro-1-phenylethanol with high optical purity were synthesized using the enzymatic method, and the kinetic resolution of various lipases were investigated. Moreover, the effects of organic solvent, temperature and water activity on the lipase-catalyzed resolution of (R, S)-2-chloro-1-phenylethanol were analyzed, and the reuse of immobilized enzymes was investigated. The results indicate that a new immobilized lipase from Pseudomonas cepacia marked as Lipase PS IM shows high activity, by which two high-purity enantiomers (eep 99% and ees 99% , respectively) can be separated in n-hexane at 35℃with a water activity of 0. 69; and that the relative activity of Lipase PS IM after five repetitive reactions is still up to 85%.