2026-04-28T15:17:18Zhttps://riubu.ubu.es/oai/request

oai:riubu.ubu.es:10259/50762021-11-10T09:38:20Zcom_10259_4244com_10259_5086com_10259_2604col_10259_4245

00925njm 22002777a 4500 dc 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 author 2019-05 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. 0896-8446 http://hdl.handle.net/10259/5076 10.1016/j.supflu.2018.07.026 Polyphenol oxidase HPCD Enzyme inactivation Supercritical carbon dioxide Studies of polyphenol oxidase inactivation by means of high pressure carbon dioxide (HPCD)