Trichoderma reesei cellobiohydrolase I with an endoglucanase cellulose-binding domain: action on bacterial microcrystalline cellulose

被引：61

作者：

Srisodsuk, M ^{[1
]}

Lehtio, J ^{[1
]}

Linder, M ^{[1
]}

MargollesClark, E ^{[1
]}

Reinikainen, T ^{[1
]}

Teeri, TT ^{[1
]}

机构：

[1] VTT BIOTECHNOL & FOOD RES, FIN-02044 ESPOO, FINLAND

来源：

JOURNAL OF BIOTECHNOLOGY | 1997年 / 57卷 / 1-3期

关键词：

cellulose-binding domain; endoglucanase; cellobiohydrolase; Trichoderma reesei;

D O I：

10.1016/S0168-1656(97)00088-6

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

Cellulolytic enzymes consist of distinct catalytic and cellulose-binding domains (CBDs). The presence of a CBD improves the binding and activity of cellulases on insoluble substrates but has no influence on their activities on soluble substrates. Structural and biochemical studies of a fungal CBD from Trichoderma reesei cellobiohydrolase I have revealed a wedge shaped structure with a flat cellulose binding surface containing three essential tyrosine residues. The face of the wedge is strictly conserved in all fungal CBDs while many differences occur on the other face of the wedge. Here we have studied the importance of these differences on the function of the T. reesei CBHI by replacing its CBD by a homologous CBD from the endoglucanase, EGI. Our data shows that, apart from slightly improved affinity of the hybrid enzyme, the domain exchange does not significantly influence the function of CBHI. (C) 1997 Elsevier Science B.V.

引用

页码：49 / 57

页数：9

共 43 条

[1] MONOCLONAL-ANTIBODIES AGAINST CORE AND CELLULOSE-BINDING DOMAINS OF TRICHODERMA-REESEI CELLOBIOHYDROLASE-I AND CELLOBIOHYDROLASE-II AND ENDOGLUCANASE-I [J].