棘托竹荪菌盖胞外β-葡萄糖苷酶酶学特性研究  

Study on Enzymatic Properties of Extracelluar β-glucosidase Isolated from Pileus of Dictyophora Echinovolvata

作　　者：黄志鸿[1] 檀东飞[2] 

机构地区：[1]福建医科大学基础医学院,福州350108 [2]福建师范大学生命科学学院,福州350117

出　　处：《福建医科大学学报》2014年第2期91-95,共5页Journal of Fujian Medical University

基　　金：福建省自然科学基金(X0650045)

摘　　要：目的研究棘托竹荪菌盖胞外β-葡萄糖苷酶酶学特性。方法将棘托竹荪菌盖胞外酶冻干粉以缓冲液进行溶解,经透析、离心后,以DNS为显色剂,以水杨苷为底物,采用分光光度法,对β-葡萄糖苷酶的主要酶学特性和不同抑制剂、激活剂对酶活性的影响进行研究。结果β-葡萄糖苷酶的最适反应pH为4.0,最适反应温度为65℃;Hg2+、Cu2+对酶起抑制作用,Fe2+、Zn2+对酶具有激活作用;棘托竹荪菌盖胞外β-葡萄糖苷酶对水杨苷的米氏常数(Km)为1.320×10-2 mol/L,最大反应速度Vmax为0.143 7μmol/min,比活力为2.874U/mg。结论棘托竹荪菌盖胞外β-葡萄糖苷酶偏好酸性环境,其温度适应范围较宽,温度升高可提升酶催化活性,但影响酶的稳定性。Objective To study the enzymatic characteristics of extracellutar β-glucosidase isolated from pileus of Dictyophora echinovolvata.Method The lyophilized powder of ectoenzyme that extracted from pileus of Dictyophora echinovolvata was reconstituted in a buffer solution.After dialysis and centrifugation,the characteristics of β-glucosidase and the effects of various different inhibitors and activators of β-glucosidase were investigated with the method of spectrophotometry in which DNS was chosen as chromogenic reagent,and the saligenin was used as substrate.Results The optimal pH for β-glucosidase activity was 4.0,and the temperature was 65 ℃.The β-glucosidase activity was inhibited by Hg2＋ and Cu2＋,but was activated by Fe2＋ and Zn2＋.The Km of β-glucosidase from pileus of Dictyophora echinovolvata was 1.32×10 2mol/L,the Vmax was 0.143 7 μmol/min and the specific activity was 2.874 U/mg.Conclusion The acidic conditions can enhance the enzyme activity of extracellular β-glucosidase,and the working temperature of β glucosidase has broad range.A higher temperature can increase β-glucosidase activity but impair its stabilization.

关 键 词：棘托竹荪 子实体类 真菌 分光光度法 β葡糖苷酶类 曲霉菌 黑 温度 

分 类 号：R285[医药卫生—中药学]