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Kinetic as well as energetic aspects of the thermal denaturation of Trichoderma reesei endo-1,4-β-xylanase II (TRX II) and its three thermostable disulfide mutants were characterized by means of differential scanning calorimetry (DSC) in different solution conditions. The calorimetric transitions were strongly scan-rate dependent, characteristic for an irreversible, kinetically controlled protein...
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