Improving the gel properties of duck egg white by synergetic phosphorylation/ultrasound: Gel properties, crystalline structures, and protein structure

Improving the gel properties of salted egg white/cooked soybean protein isolate composite gels by ultrasound treatment: Study on the gelling properties and structure

“…As shown in Fig. 2 A , it was discovered that the ζ -potential absolute values of SEW-CSPI composite gels were all more than 30 mV, which indicated that the composite gel system was relatively stable [34] . As the SEW addition increased, the ζ -potential absolute values of composite gels (0, 150 and 300 W) exhibited the overall downward trends ( P < 0.05).…”

“…ζ -potential can characterize the charge on the protein surface, thus reflecting the aggregation and stability of protein gels [34] . As shown in Fig.…”

“…SDS-PAGE is often used to analyze the protein profile on the basis of their molecular weight [34] . As shown in Fig.…”

“…Several absorption peaks were shown in the second-derivation spectra of composite gels ( Fig. 6 D-F ), including intermolecular β -sheets (1625–1615 cm −1 ), intramolecular β -sheets (1642–1612 cm −1 ), random coils (1650–1640 cm −1 ), α -helices (1660–1651 cm −1 ), β -turn (1690–1661 cm −1 ), and intermolecular antiparallel β -sheets (1700–1690 cm −1 ) [34] . Among these absorption peaks, β -sheets were dominant in the secondary structure of the protein in ultrasound-treated and untreated composite gels.…”

Effect of high intensity ultrasonic treatment on structural, rheological, and gelling properties of potato protein isolate and its co‐gelation properties with egg white protein

“…Hardness of the two protein gels tended to increase and then decrease with increasing duration of ultrasonic treatment. Ultrasound changes particle size of proteins, exposes hydrophobic groups, and alters their intermolecular forces, which can lead to the unfolding of protein structures, thus enhancing cross‐linking between proteins and/or between protein and water molecules increasing gel hardness (Xue et al., 2022). However, excessive ultrasonication may induce further entrapping of proteins, thus weakening the interactions between proteins and gel strength.…”