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Updated: Jul 3, 2026

Measuring Enzymatic Stability by Isothermal Titration Calorimetry
Published on: March 26, 2019
A kinetic approach to the thermal inactivation of an immobilized triosephosphate isomerase
M Abrahám1, Z Pénzes, B Szajáani
1Department of Biochemistry, Attila József University, POB 533, Szeged 6701, Hungary.
Abstract:
The process of thermal inactivation of triosephosphate isomerase covalently attached to a silica-based support activated with p-benzoquinone was found to be a complex one. At 50 degrees C, a characteristic activation preceding the thermal inactivation was observed. Following the intramolecular changes caused by heat, the values of K(M) and V(max) were determined during the activation. It was presumed that the complex thermal inactivation kinetics reflects the microheterogeneity of the immobilized enzyme molecules. The phosphate ion proved to be a better stabilizer than the substrate.
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