Adsorption behaviors of two cellobiohydrolases and their core proteins from Trichoderma reesei on Avicel PH 101

被引：10

作者：

Kim, DW

Jang, YH

Jeong, YK

机构：

[1] Department of Chemistry, College of Natural Sciences, Chungbuk National University, Cheongju

来源：

BIOTECHNOLOGY LETTERS | 1997年 / 19卷 / 09期

关键词：

D O I：

10.1023/A:1018397922881

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：

The cleavage of cellulose binding domain decreased the adsorption affinity and tightness of cellobiohydrolase I by 76.5 and 82.1%, as well as those of cellobiohydrolase II did by 20.7 and 68.3% at 25 degrees C. The synergism of the two cellobiohydrolases can be explained by assuming the formation of a partial complex of between binding domain of cellobiohydrolases I and core protein of cellobiohydrolases II, which have higher adsorption affinity and tightness than those of individual components, and different specificities in their attack on cellulose.

引用

页码：893 / 897

页数：5

共 12 条

[1]

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[2]

BIELY P, 1993, P 2 TRIC S TRICH REE, V8, P99

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