THERMAL DENATURATION OF TRANSGLUTAMINASE UNDER VARIOUS RATE CONSTANTS: MATHEMATICAL AND COMPUTATIONAL OVERVIEW

In this paper, we present a mathematical model for the dynamics of the enzyme tissue Transglutaminase -TGase, which is a calcium dependent ubiquitous enzyme that catalyzes the post translational modification of proteins and plays a crucial role in the pathogenesis of celiac disease. Investigating the thermal denaturation of transglutaminase is essential for comprehending its stability, activity, and ideal temperature range for biotechnological applications, as well as the relationships between protein structure and function, and the optimization of industrial processes. This proposed model considers the thermal denaturation of the enzyme TGase under various rate constants, based on the reaction mechanism with optimal mathematical outcome. The expressions for molar concentration of the three forms of the enzyme TGase viz., native, partially denatured and fully denatured forms are obtained analytically. The solution equations were analyzed and interpreted using different values of the parameters. The results were demonstrated using graphs to understand the change in molar concentration of native and denatured forms of the enzyme under various rate constants and with respect to time. The result of the study showed that over time the concentration of the native enzyme form decreases, while the concentration of the denatured form increases.