English
| dc.contributor.author | Içier, F | |
| dc.contributor.author | Yildiz, H | |
| dc.contributor.author | Baysal, T | |
| dc.date.accessioned | 2024-07-18T11:58:05Z | |
| dc.date.available | 2024-07-18T11:58:05Z | |
| dc.description.abstract | ELSEVIER SCI LTD | |
| dc.identifier.issn | 1873-5770 | |
| dc.identifier.uri | http://akademikarsiv.cbu.edu.tr:4000/handle/123456789/7254 | |
| dc.language.iso | Article | |
| dc.publisher | 0260-8774 | |
| dc.subject | The heating method affects the temperature distribution inside a food, and directly modifies the time-temperature relationship for enzyme deactivation. Fresh grape juice was ohmically heated at different voltage gradients (20, 30, and 40 V/cm) from 20 degrees C to temperatures of 60, 70, 80 or 90 degrees C and the change in the activity of polyphenoloxidase enzyme (PPO) was measured. The critical deactivation temperatures were found to be 60 degrees C or lower for 40 V/cm, and 70 degrees C for 20 and 30 V/cm. Various kinetic models for the deactivation of PPO by ohmic heating at 30 V/cm were fitted to the experimental data. The simplest kinetic model involving one step first-order deactivation was better than more complex models. The activation energy of the PPO deactivation for the temperature range of 70-90 degrees C was found to be 83.5 kJ/mol. (c) 2007 Elsevier Ltd. All rights reserved. | |
| dc.title | English | |
| dc.type | PULSED ELECTRIC-FIELDS | |
| dc.type | PEROXIDASE INACTIVATION | |
| dc.type | THERMAL INACTIVATION | |
| dc.type | ORANGE JUICE | |
| dc.type | APPLE |