Comparison of hydrodynamic and ultrasonic cavitation effects on soy protein isolate functionality

Ultrasonic treatment on physicochemical properties of water-soluble protein from Moringa oleifera seed

“…The H 0 of proteins was an indication that the number of exposed hydrophobic groups on the surface of protein molecules were available for bonding, which was important for protein stability and conformation and influence protein functionality [11] , [14] . The influences of ultrasonic power on the H 0 of MOWP were displayed in Fig.…”

“…Stathopulos et al [29] reported that H 0 of bovine serum protein treated by ultrasound was enhanced due to the gradual exposure of hydrophobic group. Ren et al [11] reported that H 0 of soy protein isolate treated by ultrasound was increased because large aggregates in soy protein isolate were dissociated, which increased the exposure of hydrophobic regions. H 0 values of whey protein [21] and wheat germ protein [13] treated by ultrasound were also increased.…”

“…Meanwhile, the increase in water solubility may also be owing to formation of soluble protein aggregates [18] , which was confirmed by the results of SDS-PAGE and SEM. The change in λ max in the intrinsic fluorescence spectroscopy analysis was also an indication that ultrasonic cavitation changed the MOWP tertiary structure, suggesting that ultrasound treatment could disrupt some of the non-covalent interactions of protein, such as hydrogen bonds and hydrophobic interactions, which could improve protein solubilities [11] . These results were similar with the published results of soybean protein isolate [30] and pea protein [18] that the ultrasonic effect could improve the solubility of protein.…”

“…Moreover, the FTIR results showed that the β-sheets and β-turns in MOWP were converted into random coil. Therefore, Ultrasonic treatment altered the emulsifying properties of MOWP, which might be attributed to the change of aggregates, solubility, H 0 , and secondary structure [11] . Chen et al [34] reported similar conclusions that ultrasonic power improved protein emulsification.…”

“…In recent years, ultrasonic technology has been widely used in food processing, especially in protein modification, due to its environmentally friendly and low-cost advantages [10] . The works on ultrasonic modification of proteins have been widely investigated [10] , [11] , [12] , [13] , [14] , [15] , [16] , [17] , [18] , [19] , [20] , [21] , [22] . Generally, cavitation effects generated by ultrasound could alter molecular structure and spatial conformation of protein, resulting in the improvement of functional properties of protein such as solubility, emulsifying and foaming properties [10] , [11] , [12] , [13] , [14] .…”