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    Isolation and Characterisation of Polyphenoloxidase from Jerusalem Artichoke (Helianthus tuberosus)
    (Selçuk Üniversitesi Fen-Edebiyat Fakültesi, 2003) Aydemir, Tülin; Kavrayan, Demet; Çınar, Seda
    Polyphenol oxidase (PPO) was isolated from Jerusalem artichoke (Helianthus tuberosus). PPO showed activity to catechol, L-dopa and DL-dopa, but the enzyme had no activity toward L-tyrosine. PH and temperature optima Jerusalem artichoke PPO were 7,0 and 25 °C. The enzyme was significantly stable at neutral pH region. The times required for 50 % inactivation of activity at 60 and 80 °C were found to be 40 and 20 min. respectively. Km and Vmax values were 5.88 mM and 25 402 IU/mg.min with catechol, respectively. Most effective inhibitors was found to be thiourea ?-mercaptoethanol and potassium cyanide.