Homotopy perturbation method for kinetic analysis of thermal inactivation of jack bean urease

In this work, theoretical modeling and determination of molar concentration of the native and denatured jack bean urease (EC 3.5.1.5) are presented. A three-reaction kinetic model of thermal inactivation of urease is analyzed using homotopy perturbation method. The obtained analytical solutions are used to study the kinetics of thermal inactivation of the enzyme as applied in biotechnology. From the results, it is established that the molar concentration of native enzyme decreases as the time increases while the molar concentration of the denatured enzyme increases as the time increases. The time taken to reach the maximum value of the molar concentration of native enzyme is the same as the time taken to reach the minimum value of the molar concentration of the denature enzyme. The molar concentration of the denatured enzyme reaches the steady state value when reaction time is less than or equal to 5s. Also, the molar concentration of the denatured enzyme becomes zero when rate constant of dissociation reaction of the native form of the enzyme into a denatured form, is less than or equal to 0.01 s−1. The analytical solutions are verified with numerical solutions using Runge-Kutta with shooting method and good agreements are established between the solutions. The information given in this theoretical investigation will assist in the kinetic analysis of the experimental results over handling rate constants and molar concentrations.