CALB脂肪酶的固定化及其拆分2-辛醇的研究  

Immobilization of Lipase B from Candida Antarctic and Its Application to Resolution of 2-Octanol

作　　者：高红娟[1] 王卫飞[1] 夏小乐[2] 杨博[2] 王永华[1] 张水华[1] 

机构地区：[1]华南理工大学轻工与食品学院,广东广州510640 [2]华南理工大学生物科学与工程学院,广东广州510006

出　　处：《精细化工》2008年第4期338-341,共4页Fine Chemicals

基　　金：国家自然科学基金(20506007,20706021)~~

摘　　要：以AB-8、HZ-841、HZ-802三种大孔树脂做载体,采用物理吸附法,制备出固定化南极假丝酵母脂肪酶（CALB）,并用其进行了拆分2-辛醇的研究。其中AB-8树脂做载体拆分效果最佳,其蛋白吸附量为37.94 mg/g树脂,吸附率94.86%,转酯化酶活3 000 U/g固定化酶,对映体选择性E=104。单因素优化实验得到的最佳拆分条件为：温度40℃,加酶量2.67 g/L,底物醇浓度3.76 mol/L。在该条件下,产物转化率可达50%,e.ep为97.8%。固定化pH在5.0～9.0内对拆分效果无显著影响。Lipase B from Candida Antarctic （CALB） was adsorbed on macroporous resins AB -8, HZ - 841 and HZ -802, and the immobilized CALB was used in resolution of （R, S）-2-octanol. Better activity and enantioselectivity were observed when AB -8 was used as the support than the other two macroporous resins. The results showed that the protein adsorbed on AB - 8 was 37. 94 mg/g resin, the adsorptivity was 94. 86% ,the enzyme activity of immobilized CALB on AB -8 was 3 000 U/g,and the E value was 104. The optimum reaction conditions were temperature 40 ℃, enzyme amount 2. 67 g/L and concentration of 2-octanol 3.76 mol/L. The residual （R） -2-octanol was recovered at 50% conversion with 97.8% enantiomerie excess, pH value in range of 5.0 - 9.0 has no effect on the reaction.

关 键 词：大孔树脂 固定化酶 2-辛醇 光学拆分 生物工程 

分 类 号：Q556[生物学—生物化学]