中国食品学报2013，Vol.13Issue(2)：67-72,6.
脂环酸芽孢杆菌α-葡萄糖苷酶固定化及酶学性质研究
Enzymatic Properties of Immobilized α-Glucosidase from A.Contaminans
摘要
Abstract
α-glucosidase from Alicyclobacillus contaminans is immobilized with glutaraldehyde cross-linked chitosan. By the optimization of the immobilized conditions, the optimum conditions for the enzyme immobilization obtained are as follows: 0 the glutaraldehyde concentration was 0.2 mol/L, glutaraldehyde cross-linking time was 12 h, cross-linking pH was 7.5 and cross-linking temperature was 15 ℃. Optimum pH and temperature for the immobilized a-glucosidase were 4.5 and 55 ℃, respectively. Enzyme activity would not be lost in the pH value between 8.0 and 4.5, when the temperature is 65 ℃, the immobilized enzyme can be kept close to 100% of enzyme activity and the enzyme activity could remain more than 80% when it was stored for three weeks, the enzyme residual activity remained at 80% when α-glucosi-dase was reused 6 times. So the immobilized enzyme has a certa in industrial applications.关键词
脂环酸芽孢杆菌/α-葡萄糖苷酶/固定化/酶学性质Key words
Alicyclobacillus contaminans/ α-glucosidase/ immobilization/ enzymatic propertics引用本文复制引用
王周利,岳田利,袁亚宏,徐长云,刘晓珂,刘小波..脂环酸芽孢杆菌α-葡萄糖苷酶固定化及酶学性质研究[J].中国食品学报,2013,13(2):67-72,6.基金项目
国家自然科学基金项目(31071550,31171721) （31071550,31171721）
农业部"948"项目(2011-G8-3) （2011-G8-3）
陕西省科技攻关(2009K01-20) （2009K01-20）
