化学学报 ›› 2001, Vol. 59 ›› Issue (3): 344-349. 上一篇    下一篇

研究论文

微乳液和微乳液凝胶中脂肪酶催化的酯合成反应

周国伟;李干佐;李越中;徐健;王仁会;李传光   

  1. 山东大学胶体与界面化学教育部重点实验室;山东大学微生物技术国家重点实验 室
  • 发布日期:2001-03-15

Esterification reaction catalyzed by lipase in W/O microemulsion based organogels

Zhou Guowei;Li Ganzuo;Li Yuezhong;Xu Jian;Wang Renhui;Li Chuanguang   

  • Published:2001-03-15

在ACT/异辛烷/水形成的油包水微乳液中,研究了Candidalipolytical(CL)脂肪酶催化庚酸和庚醇的酯化反应,动力学研究表明反应符合乒乓(Ping-Pong)BiBi机制,两底物酸和醇均有抑制效应,并测定了反应的表观动力学常数,将CL脂肪酶固定于含明胶的微乳液凝胶(MBGs)中,可制得固定化脂肪酶,含酶的MBGs在非极性有机溶剂中可作为一种新的固相催化剂,并研究了MBGs在异辛烷中催化合成酯反应的性能,所制得的MBGs重复利用性和贮存稳定性都非常好。

关键词: 微乳, 脂肪酶, 酶催化, 固定化酶, 酯化

Esterification reactions of heptanoic acid with heptanol, catalyzed by Candida lypolytical (CL) lipase, was studied in water-in-oil microemulsions formed by water/bis-(2-ethylhexyl) sulfosuccinate sodium (AOT)/isooctane. Kinetic studies showed that the reaction follows a Ping-Pong Bi Bi mechanism with inhibition by both substrates. The values of all apparent kinetic parameters were determined. Lipase has also been immobilized in gelatin-containing AOT microemulsion-based organogels (MBGs) without any loss of catalytic activity. These lipase-containing MBGs prove to be novel solid-phase catalysts for use in apolar organic solvents and have good storage stability. These lipase-containing MBGs retained its higher activity after many runs esterification reactions.

Key words: MICROEMUSION, LIPASE, ENZYME CATALYSIS, FIXED ENZYME, ESTERIFICATION

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