2026-04-28T15:17:19Zhttps://riubu.ubu.es/oai/requestoai:riubu.ubu.es:10259/50762021-11-10T09:38:20Zcom_10259_4244com_10259_5086com_10259_2604col_10259_4245
Repositorio Institucional de la Universidad de Burgos
author
Benito Román, Oscar
author
Sanz Díez, Mª Teresa
author
Melgosa Gómez, Rodrigo
author
Paz Barragán, Esther de
author
Escudero Barbero, Isabel
author
Beltrán Calvo, Sagrario
2019-03-20T08:44:13Z
2019-05
0896-8446
http://hdl.handle.net/10259/5076
10.1016/j.supflu.2018.07.026
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.
eng
Attribution-NonCommercial-NoDerivatives 4.0 International
Polyphenol oxidase
HPCD
Enzyme inactivation
Supercritical carbon dioxide
Studies of polyphenol oxidase inactivation by means of high pressure carbon dioxide (HPCD)
info:eu-repo/semantics/article
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