Model cellulose films exposed to H-insolens glucoside hydrolase family 45 endo-cellulase -: the effect of the carbohydrate-binding module

被引:29
作者
Eriksson, J
Malmsten, M
Tiberg, F
Callisen, TH
Damhus, T
Johansen, KS
机构
[1] Inst Surface Chem, SE-11486 Stockholm, Sweden
[2] Lund Univ, Dept Chem Phys, SE-22100 Lund, Sweden
[3] Uppsala Univ, Dept Pharm, SE-75123 Uppsala, Sweden
[4] Camurus AB, SE-22370 Lund, Sweden
[5] Novozymes AS, DK-2880 Bagsvaerd, Denmark
关键词
ellipsometry; cellulose model surface; spin coating; adsorption; cellulase; enzymatic degradation;
D O I
10.1016/j.jcis.2004.10.042
中图分类号
O64 [物理化学(理论化学)、化学物理学];
学科分类号
070304 ; 081704 ;
摘要
The effects of enzyme structure and activity on the degradation of model cellulose substrates were investigated by ellipsometry for the cellulase Humicola insolens GH45. The inactive variant D10N was found to adsorb at the cellulose surface but also to be incorporated into the cellulose films to an extent that depended on pH. For the native protein, the initial adsorption monitored for the inactive variant D10N was followed by enzyme-mediated degradation of the cellulose films. Again, a dependence on pH was found, such that higher pH resulted in slower enzymatic degradation. Removing the carbohydrate-binding module eliminated this pH dependence but also resulted in a decreased adsorption to the cellulose surface, and in a decreased net catalytic effect. (c) 2004 Elsevier Inc. All rights reserved.
引用
收藏
页码:94 / 99
页数:6
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