SUBSTRATE-SPECIFICITY, HEAT INACTIVATION AND INHIBITION OF POLYPHENOLOXIDASE FROM ANETHUM-GRAVEOLENS L

Authors
ARSLAN O TOZLU I
Citation
O. Arslan et I. Tozlu, SUBSTRATE-SPECIFICITY, HEAT INACTIVATION AND INHIBITION OF POLYPHENOLOXIDASE FROM ANETHUM-GRAVEOLENS L, Italian journal of food sciences, 9(3), 1997, pp. 249-253
Citations number
15
Categorie Soggetti
Food Science & Tenology
Journal title
Italian journal of food sciences → ACNP
ISSN journal
11201770
Volume
9
Issue
3
Year of publication
1997
Pages
249 - 253
Database
ISI
SICI code
1120-1770(1997)9:3<249:SHIAIO>2.0.ZU;2-Q
Abstract
Polyphenoloxidase (PPO), isolated from Anethum graveolens L, showed ac tivity 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 signif icantly inhibited in the presence of ascorbic acid, 2-mercaptoethanol, uric acid and barbituric acid. The most effective inhibitors were asc orbic acid and 2-mercaptoethanol.