来自芽孢杆菌IMET B 376的一种胞外β-葡聚糖酶的纯化与特性分析

Purification and characterization of an extracellular beta-glucanase from Bacillus IMET B 376.

作者信息

Borriss R

出版信息

Z Allg Mikrobiol. 1981;21(1):7-17. doi: 10.1002/jobm.3630210103.

Abstract

beta-1.3-1.4-glucanase (E.C. 3.2.1.73) was obtained in highly purified form from the culture fluid of Bacillus IMET B 376 by precipitation with ammonium sulfate, adsorption on CM-cellulose and then affinity chromatography on lichenan-Sepharose 4B. The purified enzyme was active on lichenan and barley glucan but not on laminarin and on CM-cellulose. The molecular weight of the enzyme was estimated to be 26,000 daltons. The Km values for lichenan and barley glucan were determined to be 1.43 and 1.15 mg/ml, respectively. The beta-glucanase has a broad pH optimum between 6 to 8, and was particularly thermostable in presence of Ca++.

摘要

β-1,3-1,4-葡聚糖酶（E.C. 3.2.1.73）通过硫酸铵沉淀、CM-纤维素吸附，然后在地衣多糖-琼脂糖4B上进行亲和层析，从芽孢杆菌IMET B 376的培养液中以高度纯化的形式获得。纯化后的酶对地衣多糖和大麦葡聚糖有活性，但对海带多糖和CM-纤维素无活性。该酶的分子量估计为26,000道尔顿。地衣多糖和大麦葡聚糖的Km值分别测定为1.43和1.15 mg/ml。β-葡聚糖酶在pH 6至8之间具有较宽的最适pH值，并且在有Ca++存在时特别耐热。