Light exposure accelerates oxidative protein polymerization in beef stored in high oxygen atmosphere

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Protein oxidation of beef patties stored in high oxygen modified atmosphere packaging for 9 days was investigated. Meat was either stored in the dark, under light, or in the dark with addition of FeCl2/H2O2/myoglobin (forced oxidation). SDS-PAGE analysis showed high degree of protein polymerization for meat exposed to light, compared to the other samples. Light exposure induced reducible (disulfide) and non-reducible cross-links, while mainly disulfides were formed in meat stored in the dark. Light exposure was responsible for 58% loss of free thiols (Cys residues). No significant loss of other amino acid residues was observed and none of the most common oxidation products of tryptophan, tyrosine, and phenylalanine were detected. Intrinsic fluorescence measurements of tryptophan showed 27% loss in samples exposed to light, which was ascribed to loss of protein solubility via protein polymerization rather than tryptophan oxidation. Protein carbonyls were mainly detected in forced oxidized samples at Day 0.
Original languageEnglish
Article number125132
JournalFood Chemistry
Number of pages9
Publication statusPublished - 2019

    Research areas

  • Photo-oxidation, Meat, Protein thiols, Protein cross-linking, Protein oxidation, Tryptophan oxidation, Fluorescence

ID: 225557630