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

Food Res Int. 2018 Apr:106:1042-1048. doi: 10.1016/j.foodres.2018.01.039. Epub 2018 Feb 3.

Abstract

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 (HRGS). An innovative model system was designed, in which gels, prepared with increasing levels of myofibrillar proteins, were oxidized by a HRGS (Fe3+/H2O2, 60 °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 non-destructive 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.

Keywords: Florescence spectroscopy; Molecular affinity; Protein oxidation; Schiff bases; Terpenes; Tryptophan.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cymenes
  • Food Preservation
  • Meat / analysis*
  • Monoterpenes* / chemistry
  • Monoterpenes* / metabolism
  • Monoterpenes* / pharmacology
  • Muscle Proteins* / chemistry
  • Muscle Proteins* / metabolism
  • Myofibrils / chemistry
  • Oxidation-Reduction / drug effects*
  • Spectrometry, Fluorescence
  • Swine
  • Thymol* / chemistry
  • Thymol* / metabolism
  • Thymol* / pharmacology
  • Tryptophan

Substances

  • Cymenes
  • Monoterpenes
  • Muscle Proteins
  • Thymol
  • Tryptophan
  • carvacrol