The effect of protein oxidation on the formation of advanced glycation end products after chicken myofibrillar protein glycation

Investigation that protein oxidation to the formation of advanced glycation end products (AGEs) after chicken myofibrillar protein glycation is limited. Models of protein oxidation induced by different concentrations of hydroxyl radicals (·OH) were developed after the chicken myofibrillar protein mild glycation (MPG). Results exhibited that levels of AGEs and surface hydrophobicity (H0) steadily increased with the addition of hydrogen peroxide (H2O2) concentration. However, levels of sulfhydryl group, free amino group, and particle size gradually decreased with the H2O2 concentration. The protein carbonyl value increased in H2O2 concentration until 10 mmol/L. Pearson’s correlation indicated that MPG structure modification (unfolding and degradation) induced by protein oxidation were significantly positively correlated with AGEs concentration (P < 0.05). Finally, a mechanism was proposed to hypothesize the effect of protein oxidation on the formation of AGEs under MPG conditions.