Abstract
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.
Published Version
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