Polyphenol oxidase from Allium sp.

Arslan O., Temur A., Tozlu I.

JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, vol.45, no.8, pp.2861-2863, 1997 (SCI-Expanded) identifier identifier

  • Publication Type: Article / Article
  • Volume: 45 Issue: 8
  • Publication Date: 1997
  • Doi Number: 10.1021/jf960929w
  • Journal Name: JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Page Numbers: pp.2861-2863
  • Van Yüzüncü Yıl University Affiliated: No

Abstract

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.