Effect of ultrasonic on the structure and quality characteristics of quinoa protein oxidation aggregates.

Protein oxidation leads to covalent modification of structure and deterioration of functional properties of quinoa protein. The objective of this study was to investigate the effects of ultrasonic treatment on the functional and physicochemical properties of quinoa protein oxidation aggregates. In this concern, 2,2'-azobis (2-amidinopropane) dihydrochloride (AAPH) was selected as oxidative modification of quinoa protein. The microstructure of quinoa protein displayed by scanning electron microscope (SEM) indicated that oxidation induced extensive aggregation, leading to carbonylation and degradation of sulfhydryl groups. Aggregation induced by oxidation had a negative effect on the solubility, turbidity, emulsifying stability. However, according to the analysis of physicochemical properties, ultrasonic significantly improved the water solubility of quinoa protein. The quinoa protein treated by ultrasonic for 30 min exhibited the best dispersion stability in water, which corresponded to the highest ζ-potential, smallest particle size and most uniform distribution. Based on the FT-IR, SDS-PAGE and surface hydrophobicity analysis, the increase of α-helix, β-turn and surface hydrophobicity caused by cavitation effect appeared to be the main mechanism of quinoa protein solubilization. In addition, the hydrophobic region of the protein was re-buried by excessive ultrasonic treatment, and the protein molecules were reaggregated by disulfide bonds. Microstructural observations further confirmed that ultrasonic treatment effectively inhibited protein aggregation and improved the functional properties of quinoa protein.