Oxidation and Gel Structure of Duck Myofibrillar Protein in Post-slaughter Heat and Hydroxyl Radical-treated Duck Meat
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Abstract:
The oxidation and physical and chemical properties of duck myofibrillar protein (DMP) from duck meat treated with hydroxyl radicals in combination with high temperature after slaughter were investigated. Duck breast meat was treated for 0.5~4.5 h after slaughter at 0 ℃ or 40 ℃, and the extracted DMP was then exposed to different concentrations of hydrogen peroxide (H2O2; 0, 5, or 10 mmol/mL). The carbonyl content, sulfhydryl content, surface hydrophobicity, water retention, protein composition characteristics, and gel structure of the oxidized DMP were analyzed. Sulfhydryl content and water retention of DMP significantly decreased (p<0.05) as H2O2 concentration increased in both temperature treatment groups, while carbonyl content and surface hydrophobicity significantly increased (p<0.05). Notably, the differences between the high temperature treatment group (40 ℃) and the control group (0 ℃) were statistically significant (p<0.05). Treatment of DMP with 10 mmol/mL H2O2 at 40 ℃ resulted in carbonyl content, sulfhydryl content, surface hydrophobicity, and water retention of 15.72 nmol/mg pro, 21.73 nmol/mg pro, 96.57 μg, and 83.09%, respectively. Protein characterization revealed that the crosslinking degree among DMPs from different temperature treatment groups significantly increased as H2O2 concentration increased. DMPs treated at 40 ℃ had a higher degree of crosslinking than that treated at 0 ℃, and the uniformity of the gel network significantly decreased and the voids increased. These results indicate that treatment of DMP with hydroxyl radicals combined with high temperature increased the degree of crosslinking by forming disulfide bonds that affected the gel spatial structure. These findings provide some theoretical references for the control of protein oxidation in duck meat.
