The study was designed to investigate the mechanism of Riboflavin (RF)-mediated UVA photosensitive oxidation on beef myofibrillar proteins (MP) oxidized at different storage times. To elucidate the direct relationship between RF and protein oxidation, the mechanism of action was analyzed in terms of amino acid and side chain residues, protein structure, and protein oxidative metabolism. Oxidation of MP resulted in significant changes in the levels of carbonyls, sulfhydryls, Lysine, Arginine, Threonin, and Histidine. The oxidized MP secondary structure was changed, fluorescence intensity decreased, and surface hydrophobicity increased. Metabolomics results revealed that RF-mediated UVA photosensitized oxidation is primarily mediated by Riboflavin metabolism and co-regulated with Phenylalanine metabolism. Moreover, with the increase of frozen storage time, Arginine and proline metabolism was inhibited, and the contents of creatine were significantly reduced, which exacerbated MP oxidative damage. The results provide a theoretical basis for unraveling the mechanism of RF-mediated UVA photosensitive oxidation of MP.
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| http://dx.doi.org/10.1016/j.foodchem.2025.142788 | DOI Listing |
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