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(H_(0))steadily increased with the a ddition of h ydrogen peroxide(H_(2)O_(2))concentration.However,levels of s ulfhydryl group,free amino group,and particle size gradually decreased with the H_(2)O_(2)concentration.The protein carbonyl value increased in H_(2)O_(2)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 t he effect of protein oxidation on the formation of AGEs under MPG conditions.

Glyoxal induced advanced glycation end products formation in chicken meat emulsion instead of oxidation

Advanced glycation end products(AGE) are potential harmful substances formed in the advanced Maillard reaction and increasingly investigated in muscle foods. However, the contribution of oxidation to the AGE formation is controversial. Moreover, reports on glyoxal(GO) induced AGE formation in chicken meat emulsion(CME) are limited. Thus, the effects of GO on emulsifying properties, rheological behavior and AGE formation in CME were investigated. Our findings exhibited that levels of Nε-carboxymethyllysine(CML) and Nε-carboxyethyllysine(CEL) were associated with lipid oxidation but not significantly(P > 0.05). Levels of AGE peaked when GO concentration ranged from 5 mmol/L(CML) to 10 mmol/L(CEL). The droplets’ aggregation associated with the disulfide bond when the concentration of GO was at 0.5–30 mmol/L while non-disulfide bond association occurred at 30–50 mmol/L GO concentration. In conclusion, compared to the effect of oxidation, GO exhibited the main role in the AGE formation of CME. This study will provide theoretical significance for further understanding and controlling the formation of AGE in CME.