Impact of pH-shift processing combined with ultrasonication on structural and functional properties of proteins isolated from rainbow trout by-products

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

“…The maximum fluorescence emission occurred at 336 nm without changes under different treatments. The fluorescence intensity of the treated samples increased with increasing sonication intensity and time compared to the control, indicating changes in the local microenvironments of tryptophan and tyrosine residues [26] . Changes in the tertiary structure of ISPP due to the sonication effect consequently buried tryptophan and tyrosine residues into hydrophobicity area, leading to an increase in the fluorescence intensity [14] , [26] .…”

“…The fluorescence intensity of the treated samples increased with increasing sonication intensity and time compared to the control, indicating changes in the local microenvironments of tryptophan and tyrosine residues [26] . Changes in the tertiary structure of ISPP due to the sonication effect consequently buried tryptophan and tyrosine residues into hydrophobicity area, leading to an increase in the fluorescence intensity [14] , [26] . The intrinsic fluorescence results were consistent with the surface hydrophobicity measurements, suggesting that sonication causes some structural changes in proteins.…”

“…The particle size of a protein in a solution can affect its solubility, emulsification, and gelling properties [26] . Fig.…”

Effect of ultrasonic treatment on the structure and functional properties of mantle proteins from scallops (Patinopecten yessoensis)

“…1 , hydrophilic scallop mantle protein, with the wide molecular weight of 14–115 kDa, is mainly composed of actin, tropomyosin and myosin light chain weighing 43 kDa, 36 kDa and 27 kDa, respectively. There was not statistically significant difference between different samples, suggesting that ultrasound didn’t supply enough energy to break chemical bonds and modify the primary structure of scallop mantle protein [27] .

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Effect of ultrasonic on the structure and quality characteristics of quinoa protein oxidation aggregates

“…Owing to the high requirements for environment, such as pH and temperature, pulsed electric field processing technology was difficult to operate in food processing [9] . As a non-thermal physical processing technology, ultrasonic was more suitable for application in food industry because of its green, efficient and simple operation mode [10] . The shear force generated by ultrasonic cavitation can destroy the forces that maintain protein structure, such as hydrogen bonds, Van der Waals forces and hydrophobicity.…”