TY - JOUR ID - TI - Homotopy perturbation method for kinetic analysis of thermalinactivation of jack bean urease AU - M.G. Sobamowoa,*, O.A. Adeleyeb PY - 2018 VL - 4 IS - 2 SP - 187 EP - 199 JO - Karbala International Journal of Modern Science مجلة كربلاء العالمية للعلوم الحديثة SN - 2405609X 24056103 AB - In this work, theoretical modeling and determination of molar concentration of the native and denatured jack bean urease (EC3.5.1.5)arepresented.Athree-reactionkineticmodelofthermalinactivationofureaseisanalyzedusinghomotopyperturbationmethod.The obtained analytical solutions are used to study the kinetics of thermal inactivation of the enzyme as applied in biotechnology. Fromthe results, it is established that the molar concentration of native enzyme decreases as the time increases while the molar concentrationofthedenaturedenzymeincreasesasthetimeincreases.Thetimetakentoreachthemaximumvalueofthemolarconcentrationofnativeenzyme is the same as the time taken to reach the minimum value of the molar concentration of the denature enzyme. The molarconcentration of the denatured enzyme reaches the steady state value when reaction time is less than or equal to 5s. Also, the molarconcentration of the denatured enzyme becomes zerowhen rate constant of dissociation reaction of the native form of the enzyme into adenatured form, is less than or equal to 0.01 s1. The analytical solutions are verified with numerical solutions using RungeeKutta withshooting method and good agreementsare established betweenthe solutions. The information given in thistheoretical investigation willassist in the kinetic analysis of the experimental results over handling rate constants and molar concentrations.

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