2026-05-12T03:49:53Zhttps://riubu.ubu.es/oai/requestoai:riubu.ubu.es:10259/75982023-03-25T01:05:21Zcom_10259.4_2516com_10259_5086com_10259_2604col_10259.4_2517
Ortega Santamaría, Natividad
405
600
0000-0001-6269-7577
Sáez, Laura
d10bb033-847e-4c6e-8fcb-4f002c720420
600
Palacios Santamaría, David
412
600
0000-0002-4170-9126
Busto Núñez, Mª Dolores
82
600
0000-0003-1647-7850
2023-03-24T11:44:12Z
2023-03-24T11:44:12Z
2022-06
http://hdl.handle.net/10259/7598
10.3390/ijms23126828
1422-0067
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.
application/pdf
eng
MDPI
International Journal of Molecular Sciences. 2022, V. 23, n. 12, 6828
https://doi.org/10.3390/ijms23126828
Atribución 4.0 Internacional
http://creativecommons.org/licenses/by/4.0/
info:eu-repo/semantics/openAccess
Lipases
Thermal inactivation
Thermodynamic parameters
Molecular dynamics simulations
B. cepacia
R. miehei
Bioquímica
Biochemistry
Kinetic Modeling, Thermodynamic Approach and Molecular Dynamics Simulation of Thermal Inactivation of Lipases from Burkholderia cepacia and Rhizomucor miehei
info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
International Journal of Molecular Sciences
23
12
THUMBNAIL
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ORIGINAL
Ortega-ijms_2022.pdf
Ortega-ijms_2022.pdf
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https://riubu.ubu.es/bitstream/10259/7598/1/Ortega-ijms_2022.pdf
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MD5
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10259/7598
oai:riubu.ubu.es:10259/7598
2023-03-25 02:05:21.051
Repositorio Institucional de la Universidad de Burgos
bubrep@ubu.es
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