Effect of ultrasound on physicochemical and foaming properties of a protein concentrate from giant squid (Dosidicus gigas) mantle

Ultrasound-assisted extraction of protein from Bombay locusts and its impact on functional and antioxidative properties

“…This phenomenon facilitates the unfolding of protein molecules in which hydrophobic domains became more exposed during treatment. Similar result was reported by Arredondo-Parada, et al 31 who found that SHP of protein concentrate from giant squid ( Dosidicus gigas ) mantle increased after ultrasound treatment. On the other hand, under the harsh condition of UAP used it could cause excessive unfolding and rendered polymerization or aggregation of protein molecules via covalent or hydrophobic/hydrophobic interaction, which resulted in lowered SHP 7 , 9 , 29 .…”

High-intensity ultrasound improves the physical stability of myofibrillar protein emulsion at low ionic strength by destroying and suppressing myosin molecular assembly

“…Extensive protein–protein interactions during protein aggregation would weaken the electrostatic repulsion between droplets because of the screening of charged groups, adversely affecting the physical stability of the emulsion. Likewise, Arredondo-Parada et al [33] suggested that the ultrasound-induced decreases in the net charge of squid proteins could be correlated with the migration of hydrophobic apolar sites.…”

“…The increased zeta-potential can be explained by the HIU-induced physical degradation of filamentous polymers and unfolding of proteins, culminating in exposure of the internal polar sites [33] . Moreover, previous studies have shown that the increased charges could interfere with the rod–rod electrostatic interactions responsible for the assembly of myosin filaments [11] , thereby, MPs acquire the ability to stabilize droplets.…”

Effect of multi-frequency ultrasound thawing on the structure and rheological properties of myofibrillar proteins from small yellow croaker

“…This showed that the MPs treated by DUT had the most uniform particle size distribution, and the MPs particles had the largest electrostatic repulsive force, thereby preventing the aggregation of proteins and having better stability. Arredondo-Parada et al [29] pointed out that ultrasound-induced changes in protein surface charge are related to the expansion of protein conformation and the exposure of hydrophobic non-polar residues.…”