Kinetic and thermodynamic study of aspartic protease extracted from Withania coagulans

The kinetic and thermodynamic parameters of the enzymatic reaction of aspartic protease extracted from Withania coagulans were investigated. The activation energy, Delta H-# , Delta S-# , and Delta G(# )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 degrees C. The activation energy (254.43 kJ mol(-1)), Delta H-# (251.54-251.71 kJ mol(-1)), Delta S-# (424.12-425.36 kJ mol(-1)) and Delta G(#) (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. (C) 2020 Elsevier Ltd. All rights reserved.