Characterization and changes in polyphenol oxidase from eggplant fruit (Solanum melongena L.) during storage at low temperature
Analía Concellón, María C. Añón and Alicia R. Chaves ,
Food Chemistry Volume 88, Issue 1 , November 2004, Pages 17-24
2004
บทคัดย่อ
Polyphenoloxidase (PPO) from eggplantfruitwas characterized, and its catecholase activity studied during storage offruitat 0 and 10 °C. The high catecholase activity was observed using 4-methylcatechol as substrate at pH 6 and 30 °C and activation with sodium dodecyl sulphate (SDS) was unnecessary. The soluble PPO fraction was the most thermostable, as well as the most active, form of the enzyme.Fruitsstored at 10 °C were undamaged, whereas those kept at 0 and 5 °C experiencedchilling injuryfrom days 6 and 8, respectively, as indicated by the decrease of lightness (L0) of pulp tissue. During exposure offruitsat 10 °C, the activities of soluble and insoluble PPO fractions increased, whereas, at 0 °C, PPO activity of both fractions decreased and maintained lower levels when browning of pulp tissue was observed. Soluble PPO activity at 0 °C was directly related to the value for L0.