Xie Rong, Cui Caixia, Chen Biqiang, Tan Tianwei
National Energy R&D Center for Biorefinery, Beijing Key Laboratory of Bioprocess, College of Biology Science and Technology, Beijing University of Chemical Technology, Beijing, 100029, People's Republic of China.
Appl Biochem Biotechnol. 2015 Oct;177(3):771-9. doi: 10.1007/s12010-015-1771-3. Epub 2015 Aug 6.
The purpose of this study was to investigate the feasibility of immobilizing Yarrowia lipolytica lipase lip2 on epoxy microspheres with or without gelatin modifications. The activity of lipase immobilized on gelatin-modified supports was twofold higher than those immobilized on native supports. There was no significant difference in the Michaelis-Menten constant (K M ) between the two immobilized lipases. However, lipase immobilized on gelatin modified supports showed an approximately fourfold higher V max than lipase immobilized on native supports. Lipase immobilization on the gelatin-modified support exhibited a significantly improved operational stability in an esterification system. After it was reused for a total of 35 batches, the ester conversion of lipase immobilized on gelatin-modified and native microspheres was 83 and 60 %, respectively. Furthermore, the immobilized lipase could be stored at 4 °C for 12 months without any loss of activity.
本研究的目的是探究在有或没有明胶修饰的情况下，将解脂耶氏酵母脂肪酶lip2固定在环氧微球上的可行性。固定在明胶修饰载体上的脂肪酶活性比固定在天然载体上的脂肪酶活性高两倍。两种固定化脂肪酶的米氏常数（KM）没有显著差异。然而，固定在明胶修饰载体上的脂肪酶的最大反应速度（Vmax）比固定在天然载体上的脂肪酶高约四倍。固定在明胶修饰载体上的脂肪酶在酯化体系中表现出显著提高的操作稳定性。在总共重复使用35批次后，固定在明胶修饰微球和天然微球上的脂肪酶的酯转化率分别为83%和60%。此外，固定化脂肪酶可以在4℃下储存12个月而没有任何活性损失。
