Effect of Oxidation on Physicochemical Properties and Structure of Mutton Myosin

The physicochemical properties and structure of mutton myosin were investigated through the simulation of natural oxidation using a Fenton oxidation system. Various degrees of oxidation (0, 1, 5, 10, 15, and 20 mmol/L hydrogen peroxide solution) were employed to analyze the changes in myosin characteristics. The results pertaining to physicochemical properties revealed a decrease in myosin solubility and an increase in turbidity with escalating the degree of oxidation. Additionally, the water holding capacity of gels exhibited an initial increase followed by a subsequent decrease. The primary structure analysis indicated that oxidation causes varying degrees of myosin degradation and cross-linked aggregation. The secondary structure examination suggested a decrease in the content of α -helices but an increase in the content of β -sheet. Furthermore, the tertiary structure assessment demonstrates that both carbonyl content and surface hydrophobicity of myosin solution were increased, while the total sulfhydryl and active sulfhydryl content are decreased. Meanwhile, the contents of hydrophobic interaction and disulfide bonds of protein gels firstly increased and then deceased. In conclusion, oxidative modification can significantly impact the physicochemical properties and structure of myosin. Moderate oxidation can enhance the structure of myosin gels and improve water holding capacity. These findings collectively signify that regulating the degree of oxidation can be a valuable strategy for controlling and enhancing the quality of meat products.