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- W2000764012 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." @default.
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- W2000764012 date "2011-10-01" @default.
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- W2000764012 title "The cellulose-binding domain of cellobiohydrolase Cel7A from Trichoderma reesei is also a thermostabilizing domain" @default.
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- W2000764012 doi "https://doi.org/10.1016/j.jbiotec.2011.07.016" @default.
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