Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
23960 | Journal of Biotechnology | 2011 | 7 Pages |
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.
Related Topics
Physical Sciences and Engineering
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Bioengineering
Authors
Mélanie Hall, Jonathan Rubin, Sven H. Behrens, Andreas S. Bommarius,