Partially purification and characterization of polyphenol oxidase of quince

YAĞAR H., SAĞIROĞLU A.

Turkish Journal of Chemistry, cilt.26, sa.1, ss.97-103, 2002 (SCI-Expanded, Scopus, TRDizin) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 26 Sayı: 1
  • Basım Tarihi: 2002
  • Dergi Adı: Turkish Journal of Chemistry
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus, TR DİZİN (ULAKBİM)
  • Sayfa Sayıları: ss.97-103
  • Anahtar Kelimeler: Characterization, Polyphenoloxidase, Purification, Quince
  • Trakya Üniversitesi Adresli: Evet

Özet

Polyphenol oxidase (PPO, EC 1.14.18.1) was extracted from quince (Cydonia oblonga) by using 0.1 M phosphate buffer, pH 6.8. The polyphenol oxidase of quince was partially purified by (NH4)2SO4 and dialysis. Substrate specificity experiments were carried out with catechol, pyrogallol, L-DOPA, p-cresole and tyrosine. Catechol was the most suitable substrate compound for quince PPO. The Michaelis constants were 4.54 mM, 7.35 mM and 17.8 mM for catechol, pyrogallol and L-DOPA, respectively at 25°C. The optimum pH and temperature were determined with the specific substrate catechol as 8.0 and 40°C, respectively. Of eight inhibitors tested L-cysteine, ascorbic acid and potassium cyanide were the most effective against quince PPO.