Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
7587154 | Food Chemistry | 2017 | 8 Pages |
Abstract
To understand the conformational changes of mushroom PPO, the secondary structural change of the enzyme during thermosonication treatment at different power (60, 80 and 100%), temperature (20-60 °C) and time (0-30 min) combinations was investigated by using FTIR spectroscopy and compared with the change in enzyme activity. The enzyme inactivation higher than 99% was obtained at 100% amplitude at 60 °C for 10 min. FTIR studies showed that marked spectral changes were noted after ultrasound treatment at 20 °C. The α-helix and β-sheet contents decreased, while aggregated β-sheet, turns and random coil contents increased as temperature increased up to 60 °C during thermosonication treatment for 10 min indicating protein denaturation. Aggregated bands located at 1683 and 1616 cmâ1 became evident after ultrasound treatment at 40 °C. When temperature was lowered back to 25 °C, from ultrasound treatment at 60 °C, these bands were still observed, indicating the irreversible change in the structure.
Related Topics
Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
Hande BaltacıoÄlu, Alev Bayındırlı, Feride Severcan,