Characterization of a Polyphenol Oxidase Having Monophenolase and Diphenolase Activities from a Wild Edible Mushroom, Russula delica

Keskin S., Ertunga N., Çolak A., Akatin M. Y., Özel A., Kolcuoğlu Y.

ASIAN JOURNAL OF CHEMISTRY, cilt.24, sa.3, ss.1203-1208, 2012 (SCI-Expanded) identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 24 Sayı: 3
  • Basım Tarihi: 2012
  • Dergi Adı: ASIAN JOURNAL OF CHEMISTRY
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.1203-1208
  • Anahtar Kelimeler: Diphenolase, Monophenolase, Polyphenol oxidase, Russula delica, MESPILUS-GERMANICA L., FRUITS, PURIFICATION, TYROSINASE, PEROXIDASE
  • Karadeniz Teknik Üniversitesi Adresli: Evet

Özet

A polyphenol oxidase (PPO) extracted from a wild edible mushroom, Russula delica, was characterized spectrophotometrically. Native polyacrylamide gel, stained with L-dihydroxyphenylalanine (L-DOPA), showed two bands supporting a polyphenol oxidase potential. pH and temperature optima were determined as 5.0 and 30 degrees C, respectively, for both of 3-(4-hydroxypheny1)-propionic acid (PHPPA) and 4-methylcatechol (4-MC). After incubating at this pH at 4 degrees C for 24 h, the crude extract retained about 90 % of its original monophenolase and diphenolase activities. The crude extract conserved about 90 % of its activities after 1 h incubation at 30 degrees C. V-max and K-01, values were calculated as 769.2 U/mg protein and 0.92 mM, respectively, for monophenolase and 71.4 U/mg protein and 0.27 mM, respectively, for diphenolase activity. It was found that benzoic acid was a potent inhibitor for both activities and some metal ions affected the activities. It is clear that R. delica possess polyphenol oxidase activities having interesting properties.