Effect of Ultrasound on the Structure and Properties of Oat Protein Oxidized Aggregates

In this study,oat protein was used as raw material,and the oxidized protein was oxidized by oxidant azobisisobutyl hydrazine hydrochloride(2,2'-azobis(2-amidinopropane),AAPH),and the oxidized protein was ultrasonicated at different ultrasonic powers(0,100,200,300,400,500,600 W). Using oat protein as a control,the structure of the protein(particle size,turbidity,protein disperse index(PDI),potential,secondary structure,functional group,hydrophobicity)and functional properties(solubility,emulsification activity and emulsion stability). The results showed that compared with oxidized oat protein aggregates,the average particle size of soluble ultrasound(power 500 W)oat oxidized protein decreased from 855.33 nm to 507.34 nm,PDI decreased from 0.97 to 0.26,turbidity decreased from 543 to 267,surface hydrophobicity and solubility increased by 1180.4 and 2.3%,respectively. The emulsification activity and emulsion stability were increased by 207.95 and 361.48 m²/g,the disulfide bond content was decreased by 0.77 nmol/mg,the β₁-folding structure was decreased,and the α-helical structure the random curl was improved,and the subunit content increased. The emulsification properties of the oxidized protein after the super-life treatment were significantly improved,and higher than the emulsification of the oat protein after oxidation,which provided a methodological and theoretical basis for improving industrial production and reducing enterprise losses.