Oct 3, 2014

Effect of Temperature on Xylanase II from Trichoderma reesei QM 9414: A Calorimetric, Catalytic, and Conformational Study

Enzyme Research
G López, P Estrada


The secondary structure of xylanase II from Trichoderma reesei is lost in an apparent irreversible cooperative process as temperature is increased with a midpoint transition of 58.8 ± 0.1°C. The shift of the spectral centre of mass above 50°C is also apparently cooperative with midpoint transition of 56.3 ± 0.2°C, but the existence of two isofluorescent points in the fluorescence emission spectra suggests a non-two-state process. Further corroboration comes from differential scanning calorimetry experiments. At protein concentrations ≤0.56 mg·mL(-1) the calorimetric transition is reversible and the data were fitted to a non-two-state model and deconvoluted into six transitions, whereas at concentrations greater than 0.56 mg·mL(-1) the calorimetric transition is irreversible with an exothermic contribution to the thermogram. The apparent T m increased linearly with the scan rate according to first order inactivation kinetics. The effect of additives on the calorimetric transition of xylanase is dependent on their nature. The addition of sorbitol transforms reversible transitions into irreversible transitions while stabilizing the protein as the apparent T m increases linearly with sorbitol concentration. d-Glucono-1,5-lactone, a...Continue Reading

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Mentioned in this Paper

Xylanase Activity
Trichoderma reesei
Xylan Endo-1,3-beta-Xylosidase
Calorimetry, Differential Scanning
Protein Concentration, Test Strip Measurement

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