微乳液中脂肪酶和含明胶的微乳液凝胶中固定化脂肪酶的催化特性  

Catalytic Behavior of Lipase in W/O Microemulsion and Immobilized Lipase in Gelatin Microemulsion-Based Organogels

作　　者：周国伟[1] 李干佐[1] 黄锡荣[1] 徐健[1] 何宏娟[1] 李传光[1] 

机构地区：[1]山东大学胶体与界面化学教育部重点实验室,济南250100

出　　处：《高等学校化学学报》2001年第9期1526-1529,共4页Chemical Journal of Chinese Universities

基　　金：国家自然科学基金 (批准号 :2 990 30 0 6 )资助

摘　　要：在双 2 -乙基己基琥珀酸酯磺酸钠 ( AOT)油包水微乳液中 Calytical脂肪酶催化月桂酸和戊醇的酯化反应动力学研究表明 ,反应符合乒乓 ( Bi Bi)机制 .表观速率常数 km酸 =0 .1 35 1 8mol/ L,km醇 =0 .2 2 4 2 3mol/ L,最大反应速度 vmax=1 .3873× 1 0 - 5mol/ ( L· min· mg) .将该脂肪酶固定于含明胶的微乳液凝胶 ( MBGs)中 ,制得固定化脂肪酶 ,含酶 MBGs在非极性溶剂中可作为固相催化剂 ,并研究了其在辛烷中催化酯化的性能 .所制得的含酶 MBGs物理稳定性好 ,重复利用 1 0次以上 ,其转化率仍达初始转化率的 90 %The kinetics of the esterification of lauric acid and 1 pentanol catalyzed by Calytical (CL) lipase, was studied in water/bis (2 ethylhexyl)sulfosuccinate sodium(AOT)/isooctane microemulsions. The kinetics studies showed that the reaction followed a Ping Pong Bi Bi mechanism. The values of all apparent kinetic parameters were determined. The apparent kinetic parameters of the reaction were found to be \{ k m(lauric acid)=\}0 135 18 mol/L, k m(1 pentanol)=0 224 23 mol/L and v max =1 387 3×10 -5 \{mol/(L·min·mg) . Lipase has also been immobilized in gelatin containing AOT microemulsion based organogels(MBGs). These lipase containing MBGs prove to be a novel solid phase catalysts for the use in apolar organic solvents and have a good physical stability. These lipase containing MBGs retained its higher activity after 10 runs esterification reactions.

关 键 词：油包水微乳液 酶催化 固定化酶 微乳液凝胶 动力学 催化 酯化 脂肪酶 月桂酸 戊醇 

分 类 号：O621.256.4[理学—有机化学] Q67[理学—化学]