Kinetic and thermodynamic study of aspartic protease extracted from Withania coagulans. (May 2021)

• Record Type: Journal Article
• Authors: Ahmadi, Salman; Salehi, Mahmoud; Ausi, Solmaz
• Is Part Of: International dairy journal. Volume 116(2021)
• Publication Date: 2021-05
• Subjects: Dairying -- Periodicals; Industrie laitière -- Périodiques; Electronic journals; 338.1762142
• DOI: 10.1016/j.idairyj.2020.104960
• Languages: English
• ISSNs: 0958-6946

Abstract

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.