Use of high-intensity ultrasound to improve emulsifying properties of chicken myofibrillar protein and enhance the rheological properties and stability of the emulsion

Laccase cross-linking of sonicated α-Lactalbumin improves physical and oxidative stability of CLA oil in water emulsion

“…It was formerly stated that TGase-treated protein had higher EAI than native protein with pH increased from 4 to 6 [47] . Interestingly, EAI of myofibrillar protein was significantly increased by 95.07% after ultrasound treatment from 0 to 6 min [48] .

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Effects of ultrasound-assisted basic electrolyzed water (BEW) extraction on structural and functional properties of Antarctic krill (Euphausia superba) proteins

“…In this study, increasing the duration of ultrasound significantly elevated the β-sheet from 33.2% to 38.98%, but reduced the α-helix (from 23.6% to 22.1%) and β-turn (from 15.4% to 12.5%), suggesting that the ultrasound treatment favored the transition of α-helix and β-turn to β-sheet. The conformation of α-helix was mainly stabilized by intramolecular hydrogen bonds, and the disruption of hydrogen bonds would increase the flexibility of protein structures [45] . Overall speaking, the ultrasound-assisted DW ( Fig.…”

“…It was reported that the decrease of protein particle size increased the adsorption rate of proteins at the oil-water interface, and the high absorption and migration rate effectively prevented gravitational separation, flocculation and coalescence [45] , [60] , which ultimately maintained the stability of emulsions. Meanwhile, the ultrasound-induced disordered and irregular structures also contributed to the stability of emulsions.…”

Effect of Interaction between Mealworm Protein and Myofibrillar Protein on the Rheological Properties and Thermal Stability of the Prepared Emulsion Systems

“…In addition, there was no crossover of the values of G′ and G″ with the increase in the measured angular frequency range for all samples. In the case of emulsion stabilized with proteins such as myofibril, the value of G′ was generally higher than that of G″, thus indicating a more stable emulsion system due to the restricted structure [ 27 ].…”

“…As the myofibrillar proteins required for the emulsification of fat droplets were not enough, the fat molecules remained afloat. Myofibril protein can be absorbed at the interface between water and fat droplets during the formation of the emulsion, which contributes to the prevention of gravitational separation, flocculation, and coalescence due to its hydrophobic amino acid residue such as SH group [ 27 , 30 ]. Conversely, the backscattering profile of EI100 showed a considerable difference when compared to others ( Figure 2 f).…”