Polyphenol oxidase from Allium sp.

Arslan O., Temur A., Tozlu I.

JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, cilt.45, sa.8, ss.2861-2863, 1997 (SCI-Expanded) identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 45 Sayı: 8
  • Basım Tarihi: 1997
  • Doi Numarası: 10.1021/jf960929w
  • Dergi Adı: JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.2861-2863
  • Van Yüzüncü Yıl Üniversitesi Adresli: Hayır

Özet

Polyphenol oxidase (PPO) was isolated from Allium sp. PPO showed activity to catechol and DL-dopa (K-m values were 25 mM for cathecol and 33 mM for DL-dopa; V-max values were 666 EU/mL . min for cathecol and 166 EU/mL . min for DL-dopa). Catechol was the most suitable substrate for Allium sp. PPO (lowest K-m value). The optimum pH for the PPO was 7.5 on substrates catechol and DL-dopa. Heat inactivation studies showed temperature >40 degrees C resulted in loss of enzyme activity. Heating for 30 min at 40 degrees C did not cause a significant loss of enzymatic activity. Allium sp. PPO was significantly inhibited in the presence of ascorbic acid, 2-mercaptoethanol, and sodium metabisulfide.