The temporal evolution mechanism of structure and function of oxidized soy protein aggregates

The emulsifying activity of soy protein would decrease after long-term storage, which caused huge economic losses to food processing plants. This study explored the temporal evolution mechanism of oxidation on the structure and function of soy protein aggregates, which would improve the application of soy protein in food industry. Decreased α-helix and increased random coil were observed at the initial oxidation stage (0–4 h), which induced increases in hydrophobicity and disulfide bond content. In addition, emulsibility increased significantly. However, when the oxidation time extended to 6–12 h, the soluble aggregates transformed into insoluble aggregates with large particle size, low solubility, and molecular flexibility. Surface hydrophobicity and emulsifying activity were reduced, resulting in bridging flocculation of emulsion droplets. Mutual transformation between components is affected by factors that include spatial conformation and intermolecular forces, which eventually lead to functional changes in the protein molecules.