Adsorption behaviors of two cellobio-hydrolases and their core proteins from Trichoderma reesei on Avicel PH 101

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°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.