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The thermal stability of the Fusarium solani pisi cutinase as a function of pH

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Author(s): Petersen Steffen B. | Fojan Peter | Petersen Evamaria I. | Petersen Maria Teresa Neves

Journal: Journal of Biomedicine and Biotechnology
ISSN 1110-7243

Volume: 1;
Issue: 2;
Start page: 62;
Date: 2001;
Original page

ABSTRACT
We have investigated the thermal stability of the Fusarium solani pisi cutinase as a function of pH, in the range from pH 2–12. Its highest enzymatic activity coincides with the pH-range at which it displays its highest thermal stability. The unfolding of the enzyme as a function of pH was investigated by microcalorimetry. The ratio between the calorimetric enthalpy (?Hcal) and the van′t Hoff enthalpy (?Hv) obtained, is far from unity, indicating that cutinase does not exhibit a simple two state unfolding behaviour. The role of pH on the electrostatic contribution to the thermal stability was assessed using TITRA. We propose a molecular interpretation for the pH-variation in enzymatic activity.
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