Partial purification and characterization of polyphenoloxidase from durum wheat (Triticum durum L.)

Altunkaya A., GÖKMEN V.

JOURNAL OF CEREAL SCIENCE, vol.55, no.3, pp.300-304, 2012 (SCI-Expanded) identifier identifier

  • Publication Type: Article / Article
  • Volume: 55 Issue: 3
  • Publication Date: 2012
  • Doi Number: 10.1016/j.jcs.2011.12.013
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Page Numbers: pp.300-304
  • Keywords: Durum wheat (Triticum durum cv Cakmak), Polyphenoloxidase, Heat stability, Inhibition, LETTUCE LACTUCA-SATIVA, PROTEINS, KERNEL, INACTIVATION, OXIDASE, COLOR
  • Hacettepe University Affiliated: Yes


A bright yellow color of pasta is an important qualitative trait for the durum wheat industry. Final color is the result of the balance between yellow and brown components in semolina. Polyphenoloxidase (PPO) is implicated as playing a significant role in darkening. This study aimed to characterize PPO activity of durum wheats. PPO was extracted and partially purified by ion-exchange chromatography on a column packed with diethyaminoethyl cellulose (DEAE). This procedure led to 26.33-fold purification with 24.7% recovery. The optimum temperature and pH of PPO were found to be 40 degrees C and 6.5, respectively. Heat stability of durum wheat PPO decreased as the temperatures increased from 30 to 80 degrees C. The z-value was calculated as 23.4 degrees C. It increased to 26.3 and 48.4 degrees C in the presence of 40% sucrose and 1 M NaCl, respectively. Durum wheat PPO was shown to use several phenolic compounds as substrate. Among the substrates used, the greatest substrate specificity was observed with catechol. Durum wheat PPO was sensitive to inhibitors such as ascorbic acid, cysteine, oxalic acid and citric acid. Ascorbic acid was the most effective inhibitor. (C) 2012 Elsevier Ltd. All rights reserved.