Molecular interactions and redox effects of carvacrol and thymol on myofibrillar proteins using a non-destructive and solvent-free methodological approach

Lahmar A., AKCAN T., Chekir-Ghedira L., Estevez M.

FOOD RESEARCH INTERNATIONAL, vol.106, pp.1042-1048, 2018 (SCI-Expanded) identifier identifier

  • Publication Type: Article / Article
  • Volume: 106
  • Publication Date: 2018
  • Doi Number: 10.1016/j.foodres.2018.01.039
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Page Numbers: pp.1042-1048
  • Keywords: Terpenes, Tryptophan, Schiff bases, Protein oxidation, Molecular affinity, Florescence spectroscopy, LIPID OXIDATION
  • Dokuz Eylül University Affiliated: Yes


The present study provides molecular insight into the effect of thymol and carvacrol on the oxidative damage caused to myofibrillar proteins by a hydroxyl-radical generating system (HAGS). An innovative model system was designed, in which gels, prepared with increasing levels of myofibrillar proteins, were oxidized by a HRGS (Fe3+ /H2O2, 60 degrees C and 7 days) in the presence of lipids. The molecular affinity between myofibrillar proteins and both terpenes, as well as their effect on the oxidative stability of the gel systems, were studied using a nondestructive and solvent-free procedure based on fluorescence spectroscopy. Carvacrol displayed more affinity than thymol for establishing chemical interactions with protein residues. Both terpenes exhibited a significant antioxidant potential against the generation of lipid-derived volatile carbonyls and against the formation of protein crosslinking. This procedure may be applied to meat products to assess the effectiveness of a given antioxidant additive without size reduction or sample processing.