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Polyphenol oxidase from yali pear ( Pyrus bretschneideri )
Author(s) -
Zhou HongWei,
Feng Xen
Publication year - 1991
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.2740570302
Subject(s) - polyphenol oxidase , catechol , pyrogallol , pear , chlorogenic acid , chemistry , enzyme , catechol oxidase , polyphenol , biochemistry , food science , biology , botany , antioxidant , peroxidase
Polyphenol oxidase (PPO) was isolated from Yali pear (Pyrus bretschneideri R). At the end of purification by ion exchange chromatography on DEAE‐cellulose, 10.8‐fold purification was achieved. The enzyme showed activity to catechol, pyrogallol, chlorogenic acid and DL‐DOPA; of these four, chlorogenic acid was the best substrate. The optimum pH for the PPO was 7.0. PPO activity was not destroyed by heating to 30° for 30 min. The effects of various compounds as inhibitors of the reaction catalysed by the enzyme were tested.