Abstract
The thermostability of cellobiohydrolase I Cel7A from Trichoderma reesei was investigated using dynamic light scattering. While the whole enzyme displayed a melting point of 59°C, the catalytic domain obtained via papain-catalyzed proteolysis was shown to denature at 51°C and the cellulose-binding domain (with linker attached) melted at 65-66°C. This variation in individual melting temperatures is proposed to account for the full retention of binding capacity of Cel7A at 50°C, along with a loss of catalytic activity observed for the catalytic domain alone. Thus, the cellulose-binding domain of Cel7A acts as a thermostabilizing domain for the enzyme. The effect of reducing agents on the protein melting behavior was also investigated.
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