Kinetic Modeling, Thermodynamic Approach and Molecular Dynamics Simulation of Thermal Inactivation of Lipases from Burkholderia cepacia and Rhizomucor miehei.

ABSTRACT: The behavior against temperature and thermal stability of enzymes is a topic of importance for industrial biocatalysis. This study focuses on the kinetics and thermodynamics of the thermal inactivation of Lipase PS from B. cepacia and Palatase from R. miehei. Thermal inactivation was investigated using eight inactivation models at a temperature range of 40-70 °C. Kinetic modeling showed that the first-order model and Weibull distribution were the best equations to describe the residual activity of Lipase PS and Palatase, respectively. The results obtained from the kinetic parameters, decimal reduction time (D and t_R), and temperature required (z and z') indicated a higher thermal stability of Lipase PS compared to Palatase. The activation energy values (Ea) also in

SUBMITTER: Ortega N 

PROVIDER: S-EPMC9224459 | biostudies-literature | 2022 Jun

REPOSITORIES: biostudies-literature