Molecular interactions and redox effects of carvacrol and thymol on myofibrillar proteins using a non-destructive and solvent-free methodological approach.
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.
['Lahmar|Aida|A|', 'Akcan|Tolga|T|', 'Chekir-Ghedira|Leila|L|', 'Estévez|Mario|M|']
D000818:Animals D000081007:Cymenes D005519:Food Preservation D008460:Meat D039821:Monoterpenes D009124:Muscle Proteins D009210:Myofibrils D010084:Oxidation-Reduction D013050:Spectrometry, Fluorescence D013552:Swine D013943:Thymol D014364:Tryptophan
Molecular affinity Terpenes Florescence spectroscopy Protein oxidation Schiff bases Tryptophan