大麦芽阿魏酸酯酶的分离纯化及其部分酶学性质的测定  

Purification and Partial Characterisation of Feruloyl Esterase from Barley Malt

作　　者：刘莎莎[1] 李华[2] 石庆华[1] 王希东[1] 程发祥[3] 

机构地区：[1]新疆农业大学农学院,乌鲁木齐830052 [2]中国农业大学(烟台),烟台2646701 [3]新疆农业大学动物科学学院动物营养实验室,乌鲁木齐830052

出　　处：《中国畜牧兽医》2010年第1期28-31,共4页China Animal Husbandry & Veterinary Medicine

基　　金：教育部高等学校博士学科点基金项目(20060758003)

摘　　要：本试验采用硫酸铵分级沉淀、透析、DEAE-52离子交换层析对大麦芽中的阿魏酸酯酶（FAE）进行了分离纯化,并测定了其部分酶学性质。结果显示,分离纯化后获得了阿魏酸酯酶纯品,纯化倍数达34倍;经SDS-PAGE电泳显示为单一条带,并测定其相对分子质量约为29.3 ku;最适反应温度为50℃;最适pH为5.5,但阿魏酸酯酶在60℃以下,pH 4.57.5之间有较好的稳定性;Zn^2＋、Cu^2＋、Fe^3＋对酶活有很强的抑制作用,Na^＋和EDTA对酶有一定的激活作用。The activity of feruloyl esterase has been enhanced in barley grain and barley malt.Feruloyl esterase solution was extracted from barley malt has been purified by ammonium sulfate precipitation,DEAE-cellulose column chromatography.The feruloyl esterase was purified 34-fold as shown in SDS-PAGE gel electrophoresis and the molecular weight estimated to be about 29.3 kD.Characterization of the enzyme exhibited that the optimum pH and the optimum temperature were 5.5 and 50 ℃,respectively,and it lost little activity after one hour below 60 ℃ from pH 4.5 to 7.5.It was inhibited by Zn^2＋,Fe^3＋,Cu^2＋,and strongly activated by EDTA and Na^＋.

关 键 词：大麦芽 阿魏酸酯酶 分离纯化 酶学性质 

分 类 号：Q55[生物学—生物化学]