Studies of polyphenol oxidase inactivation by means of high pressure carbon dioxide (HPCD)
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 t...
| Autores: | , , , , , |
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| Tipo de recurso: | artículo |
| Estado: | Versión aceptada para publicación |
| Fecha de publicación: | 2019 |
| País: | España |
| Institución: | Universidad de Burgos (UBU) |
| Repositorio: | Repositorio Institucional de la Universidad de Burgos (RIUBU) |
| OAI Identifier: | oai:riubu.ubu.es:10259/5076 |
| Acceso en línea: | http://hdl.handle.net/10259/5076 |
| Access Level: | acceso abierto |
| Palabra clave: | Polyphenol oxidase HPCD Enzyme inactivation Supercritical carbon dioxide Ingeniería química Chemical engineering |
| Sumario: | 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. |
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