Characterization of catecholase and cresolase activities of eggplant polyphenol oxidase.
In the present paper the catecholase and cresolase activities of eggplant polyphenol oxidase (PPO) are described. To preserve the latter activity, a partially purified enzyme was used. Peroxidase was removed from the preparation to avoid its interference with PPO during phenol oxidation. The partially purified eggplant PPO was fully active. The catecholase/cresolase ratio of 41.1 indicated that, in a pH close to the physiological, diphenol oxidation predominates over monophenol oxidation. The characteristic lag phase of the cresolase activity is modulated by the pH, the monophenol and diphenol concentrations, and the enzyme's concentration. The effect of several inhibitors was also tested, and the K(i) values of the two most effective (tropolone and 4-hexylresorcinol) were determined.
Pérez-Gilabert
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M
Departamento de Bioquímica y Biología Molecular-A, Facultad de Biología, Universidad de Murcia, Campus de Espinardo, E-30071 Murcia, Spain.
García Carmona
F
F
D004156:Catechol Oxidase / Q000737:chemistry* / Q000302:isolation & purification; D006801:Humans; D006863:Hydrogen-Ion Concentration; D014442:Monophenol Monooxygenase / Q000737:chemistry* / Q000302:isolation & purification; D019657:Solanaceae / Q000201:enzymology*
D004156:Catechol Oxidase; D014442:Monophenol Monooxygenase