Correlation of Rutin Accumulation with 3-O-Glucosyl Transferase and Phenylalanine Ammonia-lyase Activities During the Ripening of Tomato Fruit


Capanoglu E., BEEKWILDER J., MATROS A., BOYACIOGLU D., HALL R. D., MOCK H. P.

PLANT FOODS FOR HUMAN NUTRITION, vol.67, no.4, pp.371-376, 2012 (SCI-Expanded) identifier identifier

  • Publication Type: Article / Article
  • Volume: 67 Issue: 4
  • Publication Date: 2012
  • Doi Number: 10.1007/s11130-012-0321-1
  • Journal Name: PLANT FOODS FOR HUMAN NUTRITION
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Page Numbers: pp.371-376
  • Istanbul Technical University Affiliated: Yes

Abstract

In tomato, the predominant flavonoid is quercetin-3-rutinoside (rutin). In this study, we aim to investigate the phenylalanine ammonia-lyase (PAL) and the quercetin-3-O-glucosyl transferase (3-GT) reactions in the formation of rutin during tomato fruit ripening. Tomatoes of the Moneymaker variety at different development stages (green, breaker, turning, pink, red, and deep red) were divided into flesh and peel fractions. In each sample, both the content of rutin and the enzymatic activities for PAL and 3-GT were recorded. The highest activities of PAL were recorded in the peel of turning fruit (3,000 mu kat/mg fresh weight). In fruit flesh, maximal activity was observed in red fruit (917.3 mu kat/mg). For both tissues, PAL activity strongly decreased at the final (deep red) fruit stage. The activity of 3-GT in peel peaked in the turning fruit stage (50.7 pkat/mg), while in flesh maximal activity (33.4 pkat/mg) was observed in green fruit, which rapidly declined at the turning stage. Higher levels of rutin were detected in the tomato peel compared to the flesh part with the highest level being found at the green stage. The relation of PAL and 3-GT activities to rutin content is also evaluated.