RT info:eu-repo/semantics/article
T1 Kinetic Modeling, Thermodynamic Approach and Molecular Dynamics Simulation of Thermal Inactivation of Lipases from Burkholderia cepacia and Rhizomucor miehei
A1 Ortega Santamaría, Natividad
A1 Sáez, Laura
A1 Palacios Santamaría, David
A1 Busto Núñez, Mª Dolores
K1 Lipases
K1 Thermal inactivation
K1 Thermodynamic parameters
K1 Molecular dynamics simulations
K1 B. cepacia
K1 R. miehei
K1 Bioquímica
K1 Biochemistry
AB The behavior against temperature and thermal stability of enzymes is a topic of importancefor industrial biocatalysis. This study focuses on the kinetics and thermodynamics of the thermalinactivation of Lipase PS from B. cepacia and Palatase from R. miehei. Thermal inactivation wasinvestigated using eight inactivation models at a temperature range of 40–70 ◦C. Kinetic modelingshowed that the first-order model and Weibull distribution were the best equations to describethe residual activity of Lipase PS and Palatase, respectively. The results obtained from the kineticparameters, decimal reduction time (D and tR), and temperature required (z and z’) indicated a higherthermal stability of Lipase PS compared to Palatase. The activation energy values (Ea) also indicatedthat 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#), andenthalpy (∆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 enthalpiccontribution for both lipases. A comparative molecular dynamics simulation and structural analysisat 40 ◦C and 70 ◦C were also performed.
PB MDPI
YR 2022
FD 2022-06
LK http://hdl.handle.net/10259/7598
UL http://hdl.handle.net/10259/7598
LA eng
DS Repositorio Institucional de la Universidad de Burgos
RD 11-dic-2024