Journal
FOOD RESEARCH INTERNATIONAL
Volume 106, Issue -, Pages 1042-1048Publisher
ELSEVIER
DOI: 10.1016/j.foodres.2018.01.039
Keywords
Terpenes; Tryptophan; Schiff bases; Protein oxidation; Molecular affinity; Florescence spectroscopy
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Funding
- Spanish Ministry of Economy and Competitiveness [AGL2017-84586-R]
- Government of Extremadura
- FEDER [IB13132, GR15108]
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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.
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