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dc.contributor.authorOrtega Santamaría, Natividad 
dc.contributor.authorSáez, Laura
dc.contributor.authorPalacios Santamaría, David 
dc.contributor.authorBusto Núñez, Mª Dolores 
dc.date.accessioned2023-03-24T11:44:12Z
dc.date.available2023-03-24T11:44:12Z
dc.date.issued2022-06
dc.identifier.urihttp://hdl.handle.net/10259/7598
dc.description.abstractThe 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.en
dc.format.mimetypeapplication/pdf
dc.language.isoenges
dc.publisherMDPIen
dc.relation.ispartofInternational Journal of Molecular Sciences. 2022, V. 23, n. 12, 6828en
dc.rightsAtribución 4.0 Internacional*
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/*
dc.subjectLipasesen
dc.subjectThermal inactivationen
dc.subjectThermodynamic parametersen
dc.subjectMolecular dynamics simulationsen
dc.subjectB. cepaciaen
dc.subjectR. mieheien
dc.subject.otherBioquímicaes
dc.subject.otherBiochemistryen
dc.titleKinetic Modeling, Thermodynamic Approach and Molecular Dynamics Simulation of Thermal Inactivation of Lipases from Burkholderia cepacia and Rhizomucor mieheien
dc.typeinfo:eu-repo/semantics/articlees
dc.rights.accessRightsinfo:eu-repo/semantics/openAccesses
dc.relation.publisherversionhttps://doi.org/10.3390/ijms23126828es
dc.identifier.doi10.3390/ijms23126828
dc.identifier.essn1422-0067
dc.journal.titleInternational Journal of Molecular Sciencesen
dc.volume.number23es
dc.issue.number12es
dc.type.hasVersioninfo:eu-repo/semantics/publishedVersiones


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