大连工业大学学报2012，Vol.31Issue(2)：79-82,4.
绞股蓝皂苷糖苷酶的分离纯化及酶性质的研究
Purification and characterization of gypenosidase
摘要
Abstract
Gypenosidase was purified and charaterized from Absidia sp. GYP4r. The enzyme was capable of hydrolyzing some glycosyl of Gypenosides to produce new Gypenosides containning lower sugar. The SDS-PAGE analysis showed that the molecular weight of the enzyme was about 68ku. The optimum pH and temperature were 5. 0 and 40 ℃ , the enzyme was stable at 20-60 ℃ and pH 2. 2-8. 0 respectively. Its Km value was 14. 20 mmol/L and the maximum rate was 0. 46 mmol/(L · h). Na+, K+ , Mg2+ , Zn2+ , Fe3+ , Ca2+ showed no effects on the enzyme activity, while Cu2+ could inhibit it to a certain extend.关键词
绞股蓝皂苷/绞股蓝皂苷糖苷酶/酶反应Key words
gypenoside/ gypenoside-glycosidase/ enzyme reaction分类
轻工纺织引用本文复制引用
毛泽仁,张景,金凤燮,鱼红闪..绞股蓝皂苷糖苷酶的分离纯化及酶性质的研究[J].大连工业大学学报,2012,31(2):79-82,4.基金项目
国家自然科学基金资助项目(30371744) （30371744）
辽宁省科学技术基金资助项目(20042132) （20042132）
辽宁省教育厅创新团队项目(2009T007). （2009T007）
