Some kinetic properties of polyphenol oxidase obtained from dill (Anethum graveolens)

Sakiroglu H., ÖZTÜRK A. E., PEPE A. E., ERAT M.

JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY, cilt.23, sa.3, ss.380-385, 2008 (SCI-Expanded) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 23 Sayı: 3
  • Basım Tarihi: 2008
  • Doi Numarası: 10.1080/14756360701587201
  • Dergi Adı: JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.380-385
  • Anahtar Kelimeler: polyphenol oxidase, dill, Anethum graveolens, kinetic properties, activation energy, inhibition, CHLOROGENIC ACID OXIDASE, PARTIAL-PURIFICATION, GRAPE POLYPHENOLOXIDASE, DIPHENOLASE ACTIVITIES, SUBSTRATE-SPECIFICITY, SUICIDE INACTIVATION, PHENOLIC-COMPOUNDS, HEAT INACTIVATION, TYROSINASE, PEROXIDASE
  • Atatürk Üniversitesi Adresli: Evet

Özet

Polyphenol oxidase (PPO) was partially purified from dill by (NH4)(2)SO4 precipitation followed by dialysis and gel filtration chromatography. Polyphenol oxidase activity was measured spectrophotometrically at 420nm using catechol, dopamine and chlorogenic acid as substrates. Optimum pH, temperature, and ionic strength were determined with three substrates. The best substrate of dill PPO was found to be chlorogenic acid. Some kinetic properties of the enzyme such as V-max, K-M and V-max/K-M were determined for all three substrates. The effects of various inhibitors on the reaction catalysed by the enzyme were tested and I-50 values calculated. The most effective inhibitor was L-cysteine. Activation energies, E-a, were determined from the Arrhenius equation. In addition, activation enthalpy, Delta H-a, and Q(10) values of the enzyme were also calculated.