Polyphenol oxidase potentials of three wild mushroom species harvested from Liser High Plateau, Trabzon

Colak A., Şahin E., Yıldırım M., Sesli E.

FOOD CHEMISTRY, cilt.103, sa.4, ss.1426-1433, 2007 (SCI-Expanded) identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 103 Sayı: 4
  • Basım Tarihi: 2007
  • Doi Numarası: 10.1016/j.foodchem.2006.10.059
  • Dergi Adı: FOOD CHEMISTRY
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.1426-1433
  • Anahtar Kelimeler: Armillaria mellea, Lepista nuda, Hypholoma fasciculare, polyphenol oxidase, mushroom, PARTIAL-PURIFICATION, DIPHENOLASE ACTIVITIES, NUTRITIONAL-VALUE, L., MONOPHENOLASE, GRAPES, FRUITS, DIFFERENTIATION, TYROSINASE, MELANINS
  • Karadeniz Teknik Üniversitesi Adresli: Evet

Özet

Crude enzyme extracts were prepared from Armillaria mellea (A. mellea), Lepista nuda (L. nuda) and Hypholoma fasciculare (H. fasciculare), which were harvested from the Liser High Plateau-Macka (Trabzon, Turkey). The crude polyphenol oxidase (PPO) extracts from each mushroom were highly active against 4-methylcatechol. Native polyacrylamide gel electrophoresis, stained by L-3,4-dihydroxyphenylalanine, showed the polyphenol oxidase potentials. The optimum pH value, for each enzyme, was 7.0. When enzyme extracts were incubated at pH 7.0 for 24 h at 4 degrees C, it was observed that L. nuda and H. fasciculare enzyme activities decreased by about 26% and 18%, respectively, but, A. mellea enzyme activity increased by about 11%. The temperature optima of A. mellea, L. nuda and H. fusciculare were, respectively, 30, 30 and 20 degrees C. Cr3+ and Cu2+ ions inhibited each activity. Also, sodium metabisulphite and ascorbic acid were strong inhibitors of the enzyme activities. (c) 2006 Elsevier Ltd. All rights reserved.