The cellulose-binding domain of cellobiohydrolase Cel7A from Trichoderma reesei is also a thermostabilizing domain.

Autor: Hall M; School of Chemical & Biomolecular Engineering, Parker H. Petit Institute for Bioengineering and Bioscience, Georgia Institute of Technology, Atlanta, GA 30332-0363, USA., Rubin J, Behrens SH, Bommarius AS
Jazyk: angličtina
Zdroj: Journal of biotechnology [J Biotechnol] 2011 Oct 10; Vol. 155 (4), pp. 370-6. Date of Electronic Publication: 2011 Jul 22.
DOI: 10.1016/j.jbiotec.2011.07.016
Abstrakt: 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.
(Copyright © 2011 Elsevier B.V. All rights reserved.)
Databáze: MEDLINE
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