食品科学2012，Vol.33Issue(11)：205-209,5.
热稳定酸眭β-葡萄糖苷酶的分离纯化及其酶学性质
Purification and Characterization of Thermostable Acidic β-Glucosidase from spergillus niger L
摘要
Abstract
In this study,an acidic β-glucosidase（BGL） was purified from acid-tolerant Aspergillus niger L. mycelia by ethanol precipitation,DEAE-Sepharose column chromatography and Sephadex G-100 column chromatography.SDS-PAGE showed that the molecular weight of the enzyme was 125.7 kD.Further characterization revealed that it had maximal hydrolytic activity on p-nitrophenyl-β-D-glucopyranoside（pNPG） at pH 3.0 - 4.0 and 70 ℃ with a Km of 2.35 mmol/L and a kcat/Km of 2.99 × 10^4 mol/L·s.The kcat/Km values for hydrolyzing geniposide and salicin were 1.26 × 10^4 L/（mol·s） and 1.37 × 10^4 L/（mol·s）,respectively.The hydrolytic activity was activated obviously by Mn2＋ but inhibited faintly by Fe^2＋,Zn^2＋ and Cu^2＋.The BGL was highly stable at pH 2.0 - 8.5,and 85% of its original activity could be maintained after 60 min of heat treatment at 65 ℃.Thus,the enzyme was highly stable to heat.关键词
胞内酶/乙醇沉淀/对硝基苯-β-D．吡喃葡萄糖苷/京尼平苷/β-葡萄糖苷酶Key words
intracellular enzyme/ethanol precipitation/p-nitrophenyl- β-D-glucopyranoside/genipin/β-glucosidase分类
生物科学引用本文复制引用
陈今朝,王剑锋,王慧超,谭永忠..热稳定酸眭β-葡萄糖苷酶的分离纯化及其酶学性质[J].食品科学,2012,33(11):205-209,5.基金项目
重庆市科技攻关计划项目 （）
