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Family 1 carbohydrate-binding module (CBM1) is widely distributed in fungal cellulases and proteins related to cellulose degradation. It plays an important role in adsorbing proteins and enhancing enzymatic degradation at liquid-solid interfaces. In this study, we constructed a fusion protein (CBM1GFP) consisting of the CBM1 and a green fl uorescent protein, and used this to develop a simple method of regulating CBM1 adsorption onto cellulose, which is available for enzyme recycling. We were able to control the amount of adsorbed CBM1-GFP within the range of 5‒65% by increasing the concentration of acetate buffer. The same adsorption behavior was also seen in the recombinant Trametes hirsuta endoglucanase (rEG) containing the CBM1, but not observed in cellobiohydrolase I (rEx-1). The amount of rEG adsorbed was signifi cantly correlated to its hydrolytic activity against crystalline cellulose. After adsorption in 100 mM acetate buffer, the proteins were desorbed with water at 45°C. At this stage, the amount of adsorbed CBM1-GFP, rEx-1 and rEG decreased to 35, 20 and 7%, respectively. This regulation system can be easily combined with existing saccharifi cation and enzyme recycling processes.

Regulation of Adsorption Behavior of Carbohydrate-Binding Module Family 1 and Endo-β-1,4-Glucanase onto Crystalline Cellulose