Substrate specificity, heat inactivation and inhibition of polyphenoloxidase from Anethum graveolens L.


Arslan O., Tozlu I.

ITALIAN JOURNAL OF FOOD SCIENCE, vol.9, no.3, pp.249-253, 1997 (Journal Indexed in SCI) identifier identifier

  • Publication Type: Article / Article
  • Volume: 9 Issue: 3
  • Publication Date: 1997
  • Title of Journal : ITALIAN JOURNAL OF FOOD SCIENCE
  • Page Numbers: pp.249-253

Abstract

Polyphenoloxidase (PPO), isolated from Anethum graveolens L, showed activity on catechol, L-tyrosine and DL-DOPA. The optimum pH for the PPO was 7.0. Heat inactivation studies showed that heating for 40 and 15 min at 60 degrees and 80 degrees C, respectively, caused a 50% loss in enzymatic activity. The enzyme catalysed browning reaction was significantly inhibited in the presence of ascorbic acid, 2-mercaptoethanol, uric acid and barbituric acid. The most effective inhibitors were ascorbic acid and 2-mercaptoethanol.