Milk protein concentrate (MPC) is a high-protein dairy product. It is underutilized due to its poor solubility compared with other milk protein products. This study aimed to investigate the effect of enzymatic hydrolysis on the physicochemical properties and solubility of MPC. Results showed that Alcalase hydrolysates possessed a higher degree of hydrolysis (DH) than Protamex and Flavourzyme hydrolysates. Similar results could be obtained using sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS-PAGE). The molecular weight of the hydrolysate of Alcalase was less than 10 kDa. Changes to the molecular weight thereby led to a modification in the fluorescence intensity, Fourier-transform infrared spectrometry, and ultraviolet absorption. The solubility of all hydrolysates was significantly increased (p < 0.05). Correlation analysis showed a positive correlation between solubility, DH, and bitterness; the correlation coefficients were 0.81 for DH and 0.61 for bitterness. Electronic tongue analysis showed that the bitterness of Alcalase hydrolysates was the highest, while the values for Protamex hydrolysates were the lowest.

The effects of limited hydrolysis following glycosylation with dextran on the structural properties and antioxidant activity of the soybean protein isolate (SPI) were investigated. Three SPI hydrolysate (SPIH) fractions, F30 (>30 kDa), F30-10 (10–30 kDa), and F10 (<10 kDa), were confirmed using gel permeation chromatography. The results demonstrated that the glycosylation of F30 was faster than that of F30-10 or F10. The enzymolysis caused the unfolding of the SPI to expose the internal hydrophobic cores, which was further promoted by the grafting of dextran, making the obtained conjugates have a loose spatial structure, strong molecular flexibility, and enhanced thermal stability. The grafting of dextran significantly enhanced the DPPH radical or •OH scavenging activity and the ferrous reducing power of the SPI or SPIH fractions with different change profiles due to their different molecular structures. The limited enzymolysis following glycosylation was proven to be a promising way to obtain SPI-based food ingredients with enhanced functionalities.

Food proteins and peptides are generally considered a source of dietary antioxidants. The aim of this study was to investigate the antioxidant activity, allergenicity, and peptide profiles of whey protein hydrolysates (WPHs) using different hydrolysis methods. The results demonstrated that the degrees of hydrolysis of the hydrolysates with one-step (O-AD) and two-step (T-AD) methods reached 16.25% and 17.64%, respectively. The size exclusion chromatography results showed that the O-AD had a higher content of >5 and <0.3 kDa, and the distribution of peptide profiles for the two hydrolysates was significantly different. Furthermore, 5 bioactive peptides and 15 allergenic peptides were identified using peptidomics. The peptide profiles and the composition of the master proteins of the O-AD and T-AD were different. The DPPH and ABTS radical scavenging abilities of WPHs were measured, and hydrolysates were found to exhibit a strong radical scavenging ability after being treated using different hydrolysis methods. An enzyme-linked immunosorbent assay showed that the sensitization of WPHs was significantly reduced. This study may provide useful information regarding the antioxidant properties and allergenicity of WPHs.