Improved effect of ultrasound-assisted enzymolysis on egg yolk powder: Structural properties, hydration properties and stability characteristics

Effects of different protectants on the IgY content and physico‐chemical properties of spray‐dried egg yolk powder

“…However, the addition of protectants can effectively prevent protein aggregation via decreasing EYP hydrophobicity. In addition, it has been shown that the solubility of EYP was negatively correlated with its surface hydrophobicity, 32 which was consistent with the results of the present study. It was speculated that the reduced solubility of the exposed hydrophobic groups was related to extensive intermolecular interactions 33 …”

Effects of dual-frequency slit ultrasound on the enzymolysis of high-concentration hydrolyzed feather meal: Biological activities and structural characteristics of hydrolysates

“…3 e. As can be seen from the figure, the protein conversion rate, peptide yield, and A-value of UEH at 1.5 h was higher than that of CEH at 3 h, which indicated that DFSU improved the enzymolysis efficiency of HFM. The protein conversion rate, peptide yield, and A-value also increased as ultrasonic time increased, and the values reached the maximum (61.42%, 105.76 g, and 79.16, respectively) at 3 h. This phenomenon is because appropriate ultrasound time can refine and homogenize protein particles, increasing enzyme-substrate interactions remarkably [34] , [37] . However, prolonged ultrasonic treatment can cause excessive exposure of hydrophobic groups of protein, leading to protein aggregation and folding, which is harmful to enzymolysis [37] , [38] .…”

“…Similar results were also found in the study of Wang et al [26] and Wang et al [33] , both of whom reported increased protein yield followed by decreased trend with increasing ultrasonic power. This increase is because ultrasonic cavitation effects increase with the improvement of ultrasonic power density [34] . The fragmentation of protein particles and the change of protein polymer conformation are aroused by improving cavitation effects, increasing the accessibility of enzymes to substrates.…”

Mechanistic insights into the improved properties of mayonnaise from the changes in protein structures of enzymatic modification-treated egg yolk

“…33–35 The absorption peaks of egg yolk lipids were found at 1459 cm −1 and 1383 cm −1 and were mainly ascribed to the shear bending vibration of –CH 2 and the symmetric bending vibration of –CH 3 . 36,37 As shown in Fig. 6(B), the peak at 3100–3600 cm −1 changed slightly with increases in the enzyme dosage, which indicated that the hydrogen bond force was influenced and led to a change in the functional properties of egg yolk.…”