Yang H, Cao S G, Ma L, Ding Z T, Liu S D, Cheng Y H
National Laboratory of Enzyme Engineering, Jilin University, Changchun, China.
Biochem Biophys Res Commun. 1994 Apr 15;200(1):83-8. doi: 10.1006/bbrc.1994.1417.
In this paper, we used Ca-alginate gel beads coated with polyetheneimine and glutaraldehyde to adsorb Expansum penicillium lipase. The immobilized lipase catalyzed esterification of 1-dodecanol with dodecanoic acid in benzene. The results show that when the concentration of Ca-alginate, polyetheneimine (PEI) and glutaraldehyde is 1%, 6% and 1%, respectively, the activity of the immobilized lipase and the amount of adsorbed protein are the highest. The immobilized lipase is better than the SDS-immobilized lipase. The activity of the immobilized lipase connected by glutaraldehyde is higher than the activity of that without glutaraldehyde. The initial rate of the immobilized lipase and lyophilized lipase powder is 5.9 x 10(2) nmol/min.mgpr and 2.8 x 10(1) nmol/min.mgpr, respectively. After the immobilized lipase catalyzed the esterification reaction at 37 degrees C for about 12 hours, 93.3% of 1-dodecanol was converted to ester, but for lyophilized lipase powder, only 17.5% converted. Based on all above results, we have presumed and explained the structure of this kind of immobilized lipase.
在本文中，我们使用涂有聚乙烯亚胺和戊二醛的海藻酸钙凝胶珠来吸附扩展青霉脂肪酶。固定化脂肪酶催化了1-十二醇与十二烷酸在苯中的酯化反应。结果表明，当海藻酸钙、聚乙烯亚胺（PEI）和戊二醛的浓度分别为1%、6%和1%时，固定化脂肪酶的活性和吸附蛋白量最高。该固定化脂肪酶优于SDS固定化脂肪酶。通过戊二醛连接的固定化脂肪酶的活性高于未用戊二醛连接的固定化脂肪酶。固定化脂肪酶和冻干脂肪酶粉末的初始速率分别为5.9×10² nmol/min·mgpr和2.8×10¹ nmol/min·mgpr。固定化脂肪酶在37℃催化酯化反应约12小时后，93.3%的1-十二醇转化为酯，但对于冻干脂肪酶粉末，仅17.5%转化。基于上述所有结果，我们推测并解释了这种固定化脂肪酶的结构。
