Ultrasonic modification of whey protein isolate: Implications for the structural and functional properties

Effect of high-intensity ultrasound on the structural, rheological, emulsifying and gelling properties of insoluble potato protein isolates

“…For instance, a better emulsifying property of soybean protein, walnut protein and myofibrillar protein was obtained after HIU treatment [10] , [13] , [15] . The foaming ability of whey protein and the gelation property of soybean protein were enhanced by HIU treated [16] .…”

Recent advances in modified food proteins by high intensity ultrasound for enhancing functionality: Potential mechanisms, combination with other methods, equipment innovations and future directions

“…Hydrophobic interactions are the main driver of protein folding and play the primary role in maintaining the tertiary structure of proteins, which are mainly influenced by the surface hydrophobicity of protein molecules. Meng et al [36] found that the surface hydrophobicity of whey isolates increased significantly after moderate sonication, which can be attributed to the unfolding of proteins due to the tertiary structural changes of whey isolates caused by sonication, changing the local environment of hydrophobic groups. In contrast, excessive sonication resulted in a decrease in surface hydrophobicity due to protein reaggregation to re-embed the hydrophobic region into the interior of the protein molecule [36] .…”

“…Meng et al [36] found that the surface hydrophobicity of whey isolates increased significantly after moderate sonication, which can be attributed to the unfolding of proteins due to the tertiary structural changes of whey isolates caused by sonication, changing the local environment of hydrophobic groups. In contrast, excessive sonication resulted in a decrease in surface hydrophobicity due to protein reaggregation to re-embed the hydrophobic region into the interior of the protein molecule [36] . Not only animal-derived proteins but similar phenomena were also seen in the effects of HIU on the structure of amaranth isolates and chickpea isolates studied by Tomé Constantino & Garcia-Rojas [37] and Xu et al [38] , respectively.…”

“…The foamability of proteins, mainly used in foods such as ice cream, bread, and butter, belongs to the property of the interface between the continuous aqueous phase and the dispersed gas phase, and depends mainly on the movement, unfolding, and rearrangement of protein molecules at the gas–water interface. Foam expansion (FE) and foam stability (FS) are commonly used to measure the foaming properties of proteins [36] . Xiong et al [55] observed that HIU induced partial unfolding of the pea protein isolate and rapid adsorption at the air–water interface to form a relatively viscoelastic interfacial film, thereby increasing the FS from 58% to 73.3% ( Fig.…”

Artigo de revisão: Propriedades biológicas das proteínas e peptídeos do soro do leite caprino

“…Koirala et al, (2021) observou que os hidrolisados da proteína do soro do leite caprino têm a capacidade antioxidante aumentada quando tratados por ultrassonicação. Provavelmente o potencial antioxidante destas proteínas está relacionado aos aminoácidos metionina e cisteína, presentes nas proteínas β-Lactoglobulina, α-Lactoalbumina, BSA e a lactoferrina (Meng et al, 2021).…”