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 (center dot 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 a ddition of h ydrogen peroxide (H2O2) concentration. However, levels of s ulfhydryl 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). F inally, a mechanism was proposed to hypothesize t he effect of protein oxidation on the formation of AGEs under MPG conditions. (c) 2023 Beijing Academy of Food Sciences. Publishing services by Elsevier B.V. on behalf of KeAi Communications Co., Ltd. This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).

Automated summary

It is limited to investigate the relationship between protein oxidation and the formation of advanced glycation end products (AGEs) after chicken myofibrillar protein glycation. In this study, protein oxidation models were developed using different concentrations of hydroxyl radicals (center dot OH) after mild glycation of chicken myofibrillar protein. The results showed that AGEs and surface hydrophobicity (H0) levels increased with the addition of hydrogen peroxide (H2O2) concentration, while sulfhydryl group, free amino group, and particle size decreased. The protein carbonyl value increased until a concentration of 10 mmol/L H2O2.