A HIGHLY-ACTIVE FUNGAL BETA-GLUCOSIDASE - PURIFICATION AND PROPERTIES

被引：8

作者：

FADDA, MB ^{[1
]}

CURRELI, N ^{[1
]}

POMPEI, R ^{[1
]}

RESCIGNO, A ^{[1
]}

RINALDI, A ^{[1
]}

SANJUST, E ^{[1
]}

机构：

[1] UNIV CAGLIARI, IST MICROBIOL, CAGLIARI, ITALY

来源：

APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY | 1994年 / 44卷 / 03期

关键词：

BETA-GLUCOSIDASE; PURIFICATION; BETA-GLUCOSIDES; CELLOBIOSE;

D O I：

10.1007/BF02779661

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A highly active thermostable beta-glucosidase was purified to homogeneity from a strain of Trichoderma sp. The enzyme was an extracellular glycoprotein and showed hydrolytic activity toward several beta-glucosides. Cellobiose was found to be the substrate of choice for this enzyme. This finding could suggest future technological applications of the purified protein.

引用

页码：263 / 270

页数：8

共 17 条

[1] BIODEGRADATION OF CELLULOSIC MATERIALS - SUBSTRATES, MICROORGANISMS, ENZYMES AND PRODUCTS [J].