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Updated: May 30, 2026

Expression of Recombinant Cellulase Cel5A from Trichoderma reesei in Tobacco Plants
Published on: June 13, 2014
The cellulose-binding domain of cellobiohydrolase Cel7A from Trichoderma reesei is also a thermostabilizing domain
Mélanie Hall1, Jonathan Rubin, Sven H Behrens
1School of Chemical & Biomolecular Engineering, Parker H. Petit Institute for Bioengineering and Bioscience, Georgia Institute of Technology, Atlanta, GA 30332-0363, USA.
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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