乳酸菌β-葡萄糖苷酶的分离纯化及特性研究  

Purification and Characterization of β-glucosidase from Lactic Acid Bacterium

作　　者：孟宪文[1] 李长彪[1] 刘长江[1] 高荣海[1] 张春红[1] 赵秀红[1] 郑艳[1] 

机构地区：[1]沈阳农业大学食品学院,辽宁沈阳110161

出　　处：《食品科学》2006年第11期116-119,共4页Food Science

基　　金：辽宁省科技厅科技攻关课题(2004205001)

摘　　要：本文采用硫酸铵分级沉淀、DEAE-52离子交换层析、SephadexG-100凝胶过滤方法分离纯化乳酸菌中β-葡萄糖苷酶。经SDS-PAGE测定其相对分子量约为60kD。该酶以对硝基苯酚-β-D-葡萄糖苷为底物时,最适pH值和最适温度分别为6.0和40℃。在45℃以下,pH值在4.5～7.0之间酶活力相对稳定。Hg2+和Ag+对该酶活力有明显的抑制作用。The β-glucosidase was purified to homogeneity by fractional ammonium sulphate precipitation, ion-exchange chromatography on DEAE-52 and SephadexG-100 gel-filtration chromatography. By SDS-PAGE, the molecular weight of the enzyme was estimated to be 60kDa. The enzyme exhibited optimum activity at 40℃ and pH6.0. Its activity maintained relatively stable under the condition at 45℃, pH4.5-7.0, and strongly inhibited by Hg^2＋, Ag^＋.

关 键 词：乳酸菌 Β-葡萄糖苷酶 纯化 酶法水解 

分 类 号：TS201.25[轻工技术与工程—食品科学]