2026-06-29T22:09:57Zhttps://riubu.ubu.es/oai/request

oai:riubu.ubu.es:10259/75982023-03-25T01:05:21Zcom_10259.4_2516com_10259_5086com_10259_2604col_10259.4_2517

Ortega Santamaría, Natividad Sáez, Laura Palacios Santamaría, David Busto Núñez, Mª Dolores Lipases Thermal inactivation Thermodynamic parameters Molecular dynamics simulations B. cepacia R. miehei 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 tR), and temperature required (z and z’) indicated a higher thermal stability of Lipase PS compared to Palatase. The activation energy values (Ea) also indicated that higher energy was required to denature bacterial (34.8 kJ mol−1 ) than fungal (23.3 kJ mol−1 ) lipase. The thermodynamic inactivation parameters, Gibbs free energy (∆G# ), entropy (∆S # ), and enthalpy (∆H# ) were also determined. The results showed a ∆G# for Palatase (86.0–92.1 kJ mol−1 ) lower than for Lipase PS (98.6–104.9 kJ mol−1 ), and a negative entropic and positive enthalpic contribution for both lipases. A comparative molecular dynamics simulation and structural analysis at 40 ◦C and 70 ◦C were also performed. 2023-03-24 2023-03-24 2022-06 info:eu-repo/semantics/article http://hdl.handle.net/10259/7598 10.3390/ijms23126828 1422-0067 eng International Journal of Molecular Sciences. 2022, V. 23, n. 12, 6828 https://doi.org/10.3390/ijms23126828 http://creativecommons.org/licenses/by/4.0/ info:eu-repo/semantics/openAccess Atribución 4.0 Internacional MDPI