海枣曲霉β-葡萄糖苷酶的提纯与性质  

PURIFICATION AND PROPERTIES OF β-GLUCOSIDASE FROM AsPERGILLUS PHOENICIS

作　　者：曾宇成 张树政[1] 

机构地区：[1]中国科学院微生物研究所

出　　处：《微生物学报》1989年第3期195-199,共5页Acta Microbiologica Sinica

摘　　要：通过聚乙二醇6000-磷酸钾缓冲液双相分离,Sephadex G-100凝胶过滤、DEAE-Sephadcx A-50及SE-Sephadex C-50离子交换柱层析等提纯步骤,从海枣曲霉(Aspergillus_phoenicis)麦麸培养物抽提液中提纯到凝胶电泳均一的β-葡萄糖苷酶。该酶的最适pH5.0,最适温度60%,在pH 4.0—7.5之间及55℃以下稳定。Ag^+及Hg^(2+)对该酶有强烈的抑制作用。用SDS-凝胶电泳法及梯度凝胶电泳法测得该酶的分子量分别为118000及195000薄层凝胶等电聚焦法测得其等电点为pH 3.95。A β-glucosidase has been purified to electrophoretically homogeneity from the wheat bran culture of Aspergillus phoenicis by PEG 6000-phosphate biphasic seperation, column chromatography on Sephadex G-100, DEAE-Sephadex A-50 and SE-Sephadex C-50. The enzyme showed optimal activity at pH 5.0 and 60℃. It was stable in the pH range of 4.0—7.5 and up to 55℃. The enzyme activity was strongly inhibited by Ag^+ and Hg^(2+) The molecular weight of the enzyme was 118000 as determined by SDS-PAGE and 195000 by gradient-PAGE. The isoelectric point was pl 3.95 as determined by PAGIF.

关 键 词：海枣曲霉 葡萄糖苷酶 提纯 性质 

分 类 号：TQ925[轻工技术与工程—发酵工程]