2024-03-29T07:55:49Zhttps://riubu.ubu.es/oai/requestoai:riubu.ubu.es:10259/50762021-11-10T09:38:20Zcom_10259_4244com_10259_5086com_10259_2604col_10259_4245
Studies of polyphenol oxidase inactivation by means of high pressure carbon dioxide (HPCD)
Benito Román, Oscar
Sanz Díez, Mª Teresa
Melgosa Gómez, Rodrigo
Paz Barragán, Esther de
Escudero Barbero, Isabel
Beltrán Calvo, Sagrario
Polyphenol oxidase
HPCD
Enzyme inactivation
Supercritical carbon dioxide
Tyrosinase from mushroom was used as a model polyphenol oxidase (PPO) enzyme to perform a systematic inactivation study using High Pressure Carbon Dioxide (HPCD). The ratio CO2/volume of enzyme (g/mL) loaded in the reactor was found to be critical. Above a critical ratio, pressure, temperature and time did not control the inactivation performance. Exposure time (2–15 min), temperature (25–45 °C) and pressure (5–20 MPa) allowed to show a characteristic inactivation pattern for PPO: a sudden decrease in activity (at least 75% of the total activity loss was observed within the first 2 min) was followed by a slowed decay. The experimental data were fitted into a two fraction kinetic model and the main kinetic parameters (ZP, ZT activation volume and activation energy) were calculated. The fluorescence spectroscopy analysis of the samples treated with HPCD revealed significant changes in the tertiary structure of the enzyme.
2019-03-20
2019-05
2021-06
info:eu-repo/semantics/article
0896-8446
http://hdl.handle.net/10259/5076
10.1016/j.supflu.2018.07.026
eng
The Journal of Supercritical Fluids. 2019, V. 147, p. 310-321
https://doi.org/10.1016/j.supflu.2018.07.026
info:eu-repo/grantAgreement/MINECO/CTQ2015-64396-R
http://creativecommons.org/licenses/by-nc-nd/4.0/
info:eu-repo/semantics/openAccess
Attribution-NonCommercial-NoDerivatives 4.0 International
Elsevier