Effect of ultrasound on the characterization and peptidomics of foxtail millet bran protein hydrolysates.

Protein hydrolysates have attracted much attention for their high biological activity and are a crucial product form for the utilization of foxtail millet bran by-products. In this study, changes in the structure, functionality, activity and peptide profile of foxtail millet bran protein hydrolysates (FMBPHs) at different ultrasound powers (0 - 600 W) were investigated. The results showed that ultrasound promoted the transformation of α-helix and β-sheet to random coils and β-turn, and the exposure of hydrophobic groups and sulfhydryl groups in FMBPHs. The average particle size of the samples decreased, and the absolute value of the ζ-potential increased significantly. Simultaneously, smaller porous particles and loose fragments appeared on the surface of FMBPHs when the ultrasonic power was increased to 450 W. Additionally, 450 W ultrasound treatment improved solubility, foaming properties, emulsifying properties, thermal stability of FMBPHs. The DPPH, ABTS and hydroxyl radical scavenging ability (IC, 2.65, 1.06 and 3.02 mg/mL), Fe chelating activity (IC, 2.62 mg/mL), and reducing power of the samples were also enhanced. The peptidomics results demonstrated that ultrasonication increased the number of active peptides in the hydrolysate, and the relative abundance of 17 active peptides was obviously elevated at 450 W. Peptide map analysis showed that ultrasound-induced structural modifications affected the peptide profiles of Ubiquitin-like domain-containing protein, Cupin type-1 domain-containing protein, 40S ribosomal protein S19, and Oleosin 1, showing changes in the abundance of certain peptides, which may be related to changes in the characterization of FMBPHs.