Adsorption Characteristics of Fungal Family 1 Cellulose-Binding Domain from Trichoderma reesei Cellobiohydrolase I on Crystalline Cellulose: Negative Cooperative Adsorption via a Steric Exclusion Effect

被引:23
|
作者
Sugimoto, Naohisa [1 ]
Igarashi, Kiyohiko [1 ]
Wada, Masahisa [1 ,2 ]
Samejima, Masahiro [1 ]
机构
[1] Univ Tokyo, Grad Sch Agr & Life Sci, Dept Biomat Sci, Bunkyo Ku, Tokyo 1138657, Japan
[2] Kyung Hee Univ, Coll Life Sci, Dept Plant & Environm New Resources, Yongin 446701, Gyeonggi Do, South Korea
基金
日本科学技术振兴机构;
关键词
SURFACE; HYDROLYSIS; LIGANDS; PROTEIN;
D O I
10.1021/la302352k
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
Cellobiohydrolases (CBHs) hydrolyzing crystalline cellulose share a two-domain structure of catalytic domain (CD) and cellulose-binding domain (CBD). To focus on the binding characteristics of CBD, we analyzed the adsorption of fusion protein of fungal family 1 CBD from Trichoderma reesei CBH I and red-fluorescent protein on crystalline and amorphous celluloses. Binding data were better fitted by Hill's model with negative cooperativity than by other adsorption models, suggesting the occurrence of a steric exclusion effect among the fusion molecules on the cellulose surfaces. The degree of negative cooperativity depended on the nature of the cellulose. The significance of this phenomenon for catalysis by intact CBHI is discussed.
引用
收藏
页码:14323 / 14329
页数:7
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