A kinetic approach to the thermal inactivation of an imobilized triosephosphate isomerase

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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°C, a characteristic activation preceding the thermal inactivation was observed. Following the intramolecular changes caused by heat, the values of KM and Vmax 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. © 1992 John Wiley & Sons, Inc.