大连工业大学学报2017，Vol.36Issue(4)：245-249,5.
白头翁皂苷糖基水解Ⅱ型酶的分离纯化及酶性质
Purification and properties of pulchinenoside glycosyl hydrolase Ⅱ
摘要
Abstract
The pulchinenoside glycosyl hydrolase Ⅱ (PSGaseⅡ) from Absidia sp.P39r was purified and characterized.Its molecular weight was 56 ku.The optimum pH was at pH 4 and the enzyme was stable at pH 3.0-7.0.The optimum temperature was 40 ℃ and the enzyme was stable at 20-40 ℃.Ions Na+, K+ and Mg2+ had no effects on the enzyme activity of PSGaseⅡ, but Fe3+, Cu2+ and Zn2+ had strong inhibitory effects on the enzyme reaction.Under the optimum conditions, Km was 19.60 mmol/L and the maximum reaction rate was 21.60 mmol/(L·min).Pulchinenoside PSⅠ was enzymatic hydrolyzed to pulchinenoside PSⅡ and then to pulchinenoside A by PSGaseⅡ.关键词
白头翁皂苷/水解酶/酶性质Key words
pulchinenoside/hydrolase/enzyme properties分类
轻工纺织引用本文复制引用
代蕊,刘春莹,徐龙权,林完泽,鱼红闪..白头翁皂苷糖基水解Ⅱ型酶的分离纯化及酶性质[J].大连工业大学学报,2017,36(4):245-249,5.基金项目
"重大新药创制"科技重大专项(2012ZX09503001-003) （2012ZX09503001-003）
国家高端外国专家项目(GDT20152100019). （GDT20152100019）
