Molecular structural modification of β-conglycinin using pH-shifting with ultrasound to improve emulsifying properties and stability

Ultrasound-induced structural changes of different milk fat globule membrane protein-phospholipids complexes and their effects on physicochemical and functional properties of emulsions

“…The above phenomena indicated that ultrasonic treatment had a certain effect on the stretching vibration and other changes of chemical bonds in polypeptide chains, thus changing the electrostatic force between molecules [24] , [27] . Moreover, we found that ultrasonic treatment had the greatest change in the peak movement of the amide I band of the MPL-MFGMP, which increased from 1636.17 cm −1 in the absence of ultrasound to 1652.88 cm −1 (ultrasonic condition of 300 W for 15 min), suggesting that the ultrasonic condition significantly affected the change in the number of protein hydrogen bonds [28] . The secondary structure changes of MPL-MFGMP were more obvious after ultrasound, however, the shift of absorption peaks in EYL-MFGMP and SL-MFGMP complexes was not obvious, which may be attributed to the fact that electrostatic interaction was not the key force, and there was also a strong hydrophobic interaction [24] .…”

Soybean isolate protein complexes with different concentrations of inulin by ultrasound treatment: Structural and functional properties

“…It could be reasonably speculated that continuing to increase the mass fraction of INU, negative charges were present in large quantities, which resulted in aggregation and decreased the stability of the solution. The increase in the absolute value of the ζ-potential of the ultrasound group was caused by ultrasound disrupting protein conformation, leading to more charge accumulating on the molecular chain [19] . It illustrated that ultrasound treatment and the addition of an appropriate amount of INU significantly improved the ζ-potential of the solution ( P < 0.05).…”

“…Sample protein concentrations were diluted to 0.1 mg/mL with DI water. The ζ-potential and particle size of the samples were determined by laser Doppler electrophoresis technique and by dynamic light scattering using a NANO ZS90 (Malvern Instruments Ltd., UK) [19] .…”

Improvement of the emulsifying properties of Zanthoxylum seed protein by ultrasonic modification

“…In general, the emulsion experienced an increase in particle size during heat treatment, which may be due to the aggregation of the protein interfacially adsorbed and the accumulation of the protein dispersed in the water phase [36] . As depicted in Table 2 , the droplet size of the emulsion prepared from ultrasonicated ZSP was much smaller than that of native ZSP after heating at 70–90 °C for 30 min, indicating their better thermal stability.…”