The kinetic and thermodynamic parameters of the enzymatic reaction of aspartic protease extracted from Withania coagulans were investigated. The activation energy, ΔH^#, ΔS^#, and ΔG^# of casein hydrolysis were 34.677 kJ mol⁻¹, 31.96–32.16 kJ mol⁻¹, –131.26 to −125.0 J mol⁻¹, and 70.62–72.96 kJ mol⁻¹, respectively, which show the favourable formation of the enzyme-substrate complex, high tendency of the enzyme to casein hydrolysis and its spontaneous conversion to product. The half-life of the enzyme indicates its stability as a function of temperature. The calculated Z-value shows that D-value decreases ten times as a consequence of increasing the temperature by 8.6 °C. The activation energy (254.43 kJ mol⁻¹), ΔH^# (251.54–251.71 kJ mol⁻¹), ΔS^# (424.12–425.36 kJ mol⁻¹) and ΔG^# (103.52–112.6 kJ mol⁻¹) for protease inactivation indicate high stability, compaction and enzyme resistance to thermal denaturation. Overall, these features make it a suitable industrial enzyme.

研究了从Withania凝聚物提取的天冬氨酸蛋白酶的酶促反应的动力学和热力学参数。活化能，ΔH ^＃，ΔS ^＃，和ΔG ^＃酪蛋白水解为34.677千焦摩尔^-1，31.96-32.16千焦耳摩尔^-1，-131.26至-125.0Ĵ摩尔^-1，和70.62-72.96千焦耳摩尔^-1分别显示出酶-底物复合物的良好形成，酶发生酪蛋白水解的趋势以及其自发转化为产物的趋势。酶的半衰期表明其稳定性随温度的变化。计算得出的Z值表明，由于温度升高8.6°C，D值降低了十倍。活化能（254.43 kJ mol ^-1），ΔH ^＃（251.54–251.71 kJ mol ^-1），ΔS ^＃（424.12–425.36 kJ mol ^-1）和ΔG ^＃（103.52–112.6 kJ mol ^-1）对蛋白酶的灭活表明其高稳定性，紧密性和酶对热变性的抵抗力。总体而言，这些特征使其成为合适的工业酶。