Ultrasonic structural modification of myofibrillar proteins from Coregonus peled improves emulsification properties

Abstract

Graphical abstract

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

“…These results are similar to those of Amiri et al [27] and Zhu et al [13] . In contrast, some studies postulate that HIU processing reduces the R–SH contents of proteins [10] . For example, it has been reported that ultrasound treatment could generate free radicals and superoxide, which oxidize the free R–SH group to form sulfinic and sulfonic acid [25] .…”

“…The emulsifying property of the samples was measured as described by Deng et al [10] with minor modifications. The protein samples (3 mg) were homogenized with 27 mL deionized water, followed by emulsification of soy oil and sample solution in a ratio of 1:3 for 2 min using a high-speed homogenizer (CTK 10 K, Brookfield, USA) at 10,000 rpm/min.…”

“…The solubility and functional properties of proteins can be enhanced and modified by applying various innovative non-thermal methods, such as high-intensity ultrasound [10] , high pressure [11] and pulsed electric fields [12] . Amongst the processing approaches, high-intensity ultrasound (HIU) technology is a safe and environmentally friendly alternative for protein modification [10] , [13] . HIU produces its effects in liquid media through acoustic cavitation.…”

“…At present, HIU is successfully applied to improve the emulsification, foaming, viscosity and gelation characteristics of proteins. 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] .…”

Effects of Ultrasonic Treatment on the Structure, Functional Properties of Chickpea Protein Isolate and Its Digestibility In Vitro

“…Regardless of whether SDS-PAGE was under reducing or non-reducing conditions, it can be observed that the molecular weight distribution of all samples was similar, which indicated that subunits of the CPI had not changed obviously after ultrasonic modification. This was because that ultrasonic treatment neither broke the original covalent bonds nor induced the formation of new ones [ 30 ]. These results were consistent with some reported researches [ 31 ].…”