Fate of meat proteins oxidation at intestinal stage mediated by polyphenol-hydrocolloids

Heat-induced meat protein oxidation is critical for public health and food security, with mutagenic and carcinogenic implications when ingested. Herein, we determined the fate of meat protein oxidation mediated by polyphenol–polysaccharide (P–P) addition by determining the amino acid (AA) metabolites released at the intestinal stage. The increased carbonyl and disulfide bond formation in the control sample impaired the degree of hydrolysis (DH), decreased antioxidant response, and limited the access of digestive enzymes to cleave protein linkages. We spotlighted proteins-polysaccharide interaction, resistant to gastric enzymes, hampering protein digestibility at gastric and intestinal stages, which was intervened by P–P addition. A novel assay based on SEM-EDS mapping was used for metal chelation, revealing that P–P chelated the metal ions, especially Fe 2+ and Cu 2+ , preventing early oxidation manifestation. We explored that some functionally least important AAs (e.g., methionine) provided “sacrificial protection” for oxidatively susceptible AAs. At the intestinal stage, 89 AA metabolites were released, and the P–P interaction boosted anti-oxidative metabolites, upregulated the oxidatively susceptible AAs, and promoted AA-based pathways. The metabolic pathways of these compounds, as well as their modes of action on various illnesses, may lead to the development of novel diagnostic procedures, medicines, and functional food components.