Effects of ultrasound synergized with microwave on structure and functional properties of transglutaminase-crosslinked whey protein isolate

In the present study, ultrasound (400 W, U), microwave heating (75 ℃ for 15 min, M) and ultrasound synergized with microwave heating (UM) pretreatments of whey protein isolate (WPI) were applied to investigate and compare their influence on structure, physicochemical and functional characteristic of transglutaminase (TGase)-induced WPI. From the results of size exclusion chromatography, it could be seen that all three physical pretreatments could promote the formation of polymers in TGase cross-linked WPI, whose polymer amounts were increased by the order of U, UM and M pretreatment. Among three physical methods, M pretreatment had the strongest effect on structure and functional characteristics of TGase-induced WPI. Furthermore, compared with TGase-induced WPI, α-helix and β-turn of M−treated TGase-induced WPI (M−WPI−TGase) were reduced by 7.86% and 2.93%, whereas its β-sheet and irregular curl were increased by 15.37% and 7.23%. Zeta potential, emulsion stability and foaming stability of M−WPI−TGase were increased by 7.8%, 59.27% and 28.95%, respectively. This experiment exhibited that M was a more effective pretreatment method than U, UM for WPI, which could promote its reaction with TGase and improve its functional properties.     

Impact of ultrasound treatment on lipid oxidation of Cheddar cheese whey

Ultrasound (US) has been suggested for many whey processing applications. This study examined the effects of ultrasound treatment on the oxidation of lipids in Cheddar cheese whey. Freshly pasteurized whey (0.86 L) was ultrasonicated in a contained environment at the same range of frequencies and energies for 10 and 30 min at 37 °C. The US reactor used was characterized by measuring the generation of free radicals in deionized water at different frequencies (20–2000 kHz) and specific energies (8.0–390 kJ/kg). Polar lipid (PL), free and bound fatty acids and lipid oxidation derived compounds were identified and quantified before and after US processing using high performance liquid chromatography equipped with an evaporative light scattering detector (HPLC–ELSD), methylation followed by gas chromatography flame ionized detector (GC-FID) and solid phase micro-extraction gas chromatography mass spectrometry (SPME-GCMS), respectively. The highest concentration of hydroxyl radical formation in the sonicated whey was found between 400 and 1000 kHz. There were no changes in phospholipid composition after US processing at 20, 400, 1000 and 2000 kHz compared to non-sonicated samples. Lipid oxidation volatile compounds were detected in both non-sonicated and sonicated whey. Lipid oxidation was not promoted at any tested frequency or specific energy. Free fatty acid concentration was not affected by US treatment per se. Results revealed that US can be utilized in whey processing applications with no negative impact on whey lipid chemistry.     

Effect of ultrasound treatments on functional properties and structure of millet protein concentrate

In this study, the effect of high power ultrasound (US) probe in varying intensities and times (18.4, 29.58, and 73.95 W/cm² for 5, 12.5 and 20 min respectively) on functional properties of millet protein concentrate (MPC) was investigated, and also the structural properties of best modified treatment were evaluated by FTIR, DSC, Zeta potential and SDS-PAGE techniques. The results showed the solubility in all US treated MPC was significantly (p < .05) higher than those of the native MPC. Foaming capacity of native MPC (271.03 ± 4.51 ml) was reduced after US treatments at low intensities (82.37 ± 5.51 ml), but increased upon US treatments at high intensities (749.7 ± 2 ml). In addition, EAI and ES increased after US treatments. One of the best US treatments that can improve the functional properties of MPC was 73.95 W/cm² for 12.5 min that resulted in reduction of molecular weight and increase nearly 36% in the negative surface charge that was confirmed by SDS-page and Zeta potential results, respectively.     

乳清分离蛋白-葡聚糖接枝物性质的荧光光谱法分析

乳清分离蛋白与葡聚糖的混合物在干热处理条件下,发生了以褐变为特征的美拉德反应。当葡聚糖分子量由67kD增至150kD时,游离氨基含量分别下降了35.77%和30.53%,糖链越长,其接入到蛋白质肽链的难度越大。采用荧光光谱对乳清分离蛋白-葡聚糖接枝物的性质进行分析。内源荧光光谱图显示,接枝产物在405nm的最大荧光强度显著提高,且350～500nm范围内的荧光强度顺序为:G67>G150,这说明接枝物中有Maillard反应体系所特有的荧光物质生成;由外援荧光光谱图得出,接枝产物在470nm的最大荧光强度均有明显降低,各溶液体系中荧光强度高低顺序依次为:WPI>G150>G67。疏水性指数的测定进一步说明两种不同分子量的葡聚糖接入到蛋白质肽链中,对乳清分离蛋白的疏水性均有一定的屏蔽作用。     

Effect of ultrasound pretreatment on structural,physicochemical, rheological and gelation properties of transglutaminase cross-linked whey protein soluble aggregates

A solution (10%, w/v) of whey protein soluble aggregates (WPISA) was pretreated with high-intensity ultrasound (HUS, 20 kHz) for different durations (10–40 min) before incubation with transglutaminase (TGase) to investigate the effect of HUS on the structural, physicochemical, rheological, and gelation properties of TGase cross-linked WPISA. Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) results showed that HUS increased the amounts of high-molecular-weight polymers/aggregates in WPISA after incubation with TGase. HUS significantly increased (P < 0.05) the degree of TGase-mediated cross-linking in WPISA, as demonstrated by a reduction in free amino group contents. HUS significantly increased (P < 0.05) the particle size, intrinsic fluorescence intensity, and surface hydrophobicity of TGase cross-linked WPISA, but had no significant impact (P > 0.05) on the zeta-potential or total free sulfhydryl group content of TGase cross-linked WPISA. The apparent viscosity and the consistency index of TGase cross-linked WPISA were significantly increased by HUS (P < 0.05), which indicated that HUS facilitated the formation of more high-molecular-weight polymers. HUS significantly increased (P < 0.05) the water holding capacity and gel strength of glucono-δ-lactone (GDL)-induced TGase cross-linked WPISA gels. The results indicated that HUS could be an efficient tool for modifying WPISA to improve its degree of TGase-mediated cross-linking, which would lead to improved rheological and gelation properties.     

High-intensity ultrasound pretreatment influence on whey protein isolate and its use on complex coacervation with kappa carrageenan: Evaluation of selected functional properties

The aim of this work was to evaluate the influence of high-intensity ultrasound (HIUS) treatment on whey protein isolate (WPI) molecular structure as a previous step for complex coacervation (CC) with kappa-carrageenan (KC) and its influence on CC functional properties. Protein suspension of WPI (1% w/w) was treated with an ultrasound probe (24 kHz, 2 and 4 min, at 50 and 100% amplitude), non HIUS pretreated WPI was used as a control. Coacervation was achieved by mixing WPI and KC dispersions (10 min). Time and amplitude of the sonication treatment had a direct effect on the molecular structure of the protein, FTIR-ATR analysis detected changes on pretreated WPI secondary structure (1600–1700 cm⁻¹) after sonication. CC electrostatic interactions were detected between WPI positive regions, KC sulfate group (1200–1260 cm⁻¹), and the anhydrous oxygen of the 3,6 anhydro-D-galactose (940–1066 cm⁻¹) with a partial negative charge. After ultrasound treatment, a progressive decrease in WPI particle size (nm) was detected. Rheology results showed pseudoplastic behavior for both, KC and CC, with a significant change on the viscosity level. Further, volume increment, stability, and expansion percentages of CC foams were improved using WPI sonicated. Besides, HIUS treatment had a positive effect on the emulsifying properties of the CC, increasing the time emulsion stability percentage. HIUS proved to be an efficient tool to improve functional properties in WPI-KC CC.     

Effect of ultrasound treatment on interactions of whey protein isolate with rutin

Rutin is a biologically active polyphenol, but its poor water solubility and low bioavailability limit its application to the food industry. We investigated the effect of ultrasound treatment on the properties of rutin (R) and whey protein isolate (WPI) using spectral and physicochemical analysis. The results revealed that there was covalent interaction between whey protein isolate with rutin, and the binding degree of whey isolate protein with rutin increased with ultrasound treatment. Additionally, solubility and surface hydrophobicity of WPI-R complex improved with ultrasonic treatment, and a maximum solubility of 81.9 % at 300 W ultrasonic power. The ultrasound treatment caused the complex to develop a more ordered secondary structure, resulting in a three-dimensional network structure with small and uniform pore sizes. This research could provide a theoretical reference for studying protein–polyphenol interactions and their applications in food delivery systems.     

The secondary structure of heated whey protein and its hydrolysates antigenicity

Fourier transform infrared spectroscopy(FTIR) and circular dichroism(CD) were used to investigate the conformational changes of heated whey protein(WP) and the corresponding changes in the hydrolysates immunoreactivity were determined by competitive enzyme-linked immunosorbent assay(ELISA).Results showed that the contents of α-helix and β-sheet of WP did not decrease much under mild heating conditions and the antigenicity was relatively high;when the heating intensity increased(70 ℃ for 25 min or 75 ℃ for 2...     

Influence of milk fat globule membrane and milk protein concentrate treated by ultrasound on the structural and emulsifying stability of mimicking human fat emulsions

The primary objective of the present study was to investigate the effectiveness of ultrasonic treatment time on the particle size, molecular weight, microstructure and solubility of milk fat globule membrane (rich in phospholipid, MPL) and milk protein concentrate (MPC). The mimicking human fat emulsions were prepared using modified proteins and compound vegetable oil and the structural, emulsifying properties and encapsulation efficiency of emulsions were evaluated. After ultrasonic treatment, the cavitation caused particle size decreased and structure change of both MPL and MPC, resulting in the enhancement of protein solubility. While, there was no significant change in molecular weight. Modified proteins by ultrasonic may cause a reduction in particle size and an improvement in emulsifying stability and encapsulation efficiency of emulsions. The optimal ultrasonic time to improve functional properties of MPL emulsion and MPC emulsion were 3 min and 6 min, respectively. The emulsifying stability of MPL emulsion was superior to MPC emulsion, which indicated that MPL is more suitable as membrane material to simulate human fat. Therefore, the obtained results can provide basis for quality control of infant formula.     

Effect of ultrasonic-ionic liquid pretreatment on the hydrolysis degree and antigenicity of enzymatic hydrolysates from whey protein

With the aim to reduce the antigenicity of whey protein hydrolysate in milk, the pretreatment method of coupling ultrasonic and ionic liquid (US-IL) and further enzymatic treatments were studied. Papain and alcalase were found to be suitable for ultrasonic-ionic liquid pretreatment. After ultrasound-ionic liquid treatment, the antigenic decline rates of ALA and BLG upon alcalase hydrolysis were 82.82% and 88.01%, and that of the papain hydrolysis was 81.87% and 88.46%, respectively. Upon ultrasonic-ionic liquid pretreatment, the molecular weight of whey protein did not change significantly, but the small molecular weight proportion of components in the enzymatic hydrolysate obviously increased. The findings showed that combining with US-IL pretreatment for further protease hydrolysis of whey proteins, the hydrolysate can be used in order to produce hypoallergenic bovine whey proteins.     

Production of biologically active peptides by hydrolysis of whey protein isolates using hydrodynamic cavitation

Whey protein isolate (WPI) hydrolysates have higher solubility in aqueous phase and enhanced biological properties. Hydrolysis of WPI was optimized using operating pressure (ΔP, bar), number of passes (N), and WPI concentration (C, %) as deciding parameters in hydrodynamic cavitation treatment. The optimum conditions for generation of WPI hydrolysate with full factorial design were 8 bar, 28 passes, and 4.5% WPI concentration yielding 32.69 ± 1.22 mg/mL soluble proteins. WPI hydrolysate showed alterations in binding capacity over WPI. SDS-PAGE and particle size analysis confirmed the hydrolysis of WPI. Spectroscopic, thermal and crystallinity analyses showed typical properties of proteins with slight variations after hydrodynamic cavitation treatment. ABTS, DPPH and FRAP assays of WPI hydrolysate showed 7–66, 9–149, and 0.038–0.272 µmol/mL GAE at 1–10, 0.25–4, and 3–30 mg/mL concentration, respectively. Further, a considerable enhancement in fresh weight, chlorophyll, carotenoids, reducing sugars, total soluble sugars, soluble proteins content and total phenolics content was noticed during in vitro growth of sugarcane in WPI hydrolysate supplemented medium at 50–200 mg/L concentration over the control. The process cost (INR/kg) to hydrolyze WPI was also calculated.     

Effects of multi-frequency ultrasound on physicochemical properties,structural characteristics of gluten protein and the quality of noodle

In this study, the influence of multi-frequency ultrasound irradiation on the functional properties and structural characteristics of gluten, as well as the textural and cooking characteristics of the noodles were investigated. Results showed that the textural and cooking characteristics of noodles that contain less gluten pretreated by multi-frequency ultrasonic were ultrasonic frequency dependent. Moreover, the noodles that contain a smaller amount of sonicated gluten could achieve the textural and cooking quality of commercial noodles. There was no significant difference in the cooking and texture characteristics between commercial noodles and noodles with 12%, 11%, and 10% gluten pretreated by single-frequency (40 kHz), dual-frequency (28/40 kHz), and triple-frequency sonication (28/40/80 kHz), respectively. Furthermore, the cavitation efficiency of triple-frequency ultrasound was greater than that of dual-frequency and single-frequency. As the number of ultrasonic frequencies increased, the solubility, water holding capacity and oil holding capacity of gluten increased significantly (p < 0.05), and the particle size was reduced from 197.93 ± 5.28 nm to 110.15 ± 2.61 nm. Furthermore, compared to the control group (untreated), the UV absorption and fluorescence intensity of the gluten treated by multi-frequency ultrasonication increased. The surface hydrophobicity of gluten increased from 8159.1 ± 195.87 (untreated) to 11621.5 ± 379.72 (28/40/80 kHz). Raman spectroscopy showed that the α-helix content of all sonicated gluten protein samples decreased after sonication, while the β-sheet and β-turn content increased, and tryptophan and tyrosine residues were exposed. Through scanning electron microscope (SEM) analysis, the gluten protein network structure after ultrasonic treatment was loose, and the pore size of the gluten protein network increased from about 10 μm (untreated) to about 26 μm (28/40/80 kHz). This work elucidated the effect of ultrasonic frequency on the performance of gluten, indicating that with increasing frequency combination increases, the ultrasound effect became more pronounced and protein unfolding increased, thereby impacting the functional properties and the quality of the final product. This study provided a theoretical basis for the application of multi-frequency ultrasound technology in the modification of gluten protein and noodle processing.     

Impact of ultrasound pretreatment on hydrolysate and digestion products of grape seed protein

The effects of ultrasound pretreatment with different working modes, including mono frequency ultrasound (MFU), simultaneous dual frequency ultrasound (SDFU) and alternate dual frequency ultrasound (ADFU) using energy-gather counter flow ultrasound equipment, on the degree of hydrolysis (DH) of grape seed protein (GSP) hydrolysate and IC₅₀ of GSP digestion products were studied. Amino acid composition analysis (AACA), ultraviolet–visible (UV) spectroscopy and atomic force microscopy (AFM) of GSP with different ultrasound pretreatments were measured. The results showed that MFU, SDFU and ADFU pretreatments improved the DH and reduced the IC₅₀ of GSP significantly (P < .05). The MFU of 20 kHz and SDFU of 20/40 kHz showed higher ACE inhibitory activity within the MFU and SDFU groups, respectively. ADFU of 20/35 kHz produced the highest ACE inhibitory activity among the three working modes (MFU, SDFU and ADFU). AACA showed that all the working modes of the ultrasound pretreatment could increase the amount of hydrophobic amino acids and the total amino acids. The changes in UV spectra and amino acid analysis indicated the unfolding of protein structure and exposure of more hydrophobic groups by SDFU and ADFU pretreatments. AFM analysis of the GSP indicated that the microstructures were destroyed and the particle size reduced after dual-frequency ultrasound pretreatments. Therefore, energy-gather counter flow ultrasound pretreatment is an effective method to improve the DH and reducing the IC₅₀ due to the changes of molecular conformation and effects on the microstructure by sonochemistry of GSP. In conclusion, it is necessary to select the frequency and working modes of ultrasound pretreatment for the preparation of ACE inhibitory peptide of GSP.     

Effect of high-intensity ultrasound on the physicochemical properties,microstructure, and stability of soy protein isolate-pectin emulsion

In this study, an emulsion stabilized by soy protein isolate (SPI)-pectin (PC) complexes was prepared to investigate the effects of high-intensity ultrasound (HIU) treatment (150–600 W) on the physicochemical properties, microstructure, and stability of emulsions. The results found that the emulsion treated at 450 W showed the best emulsion stability index (ESI) (25.18 ± 1.24 min), the lowest particle size (559.82 ± 3.17 nm), the largest ζ-potential absolute value (16.39 ± 0.18 mV), and the highest adsorbed protein content (27.31%). Confocal laser scanning microscopy (CLSM) and atomic force microscopy (AFM) revealed that the emulsion aggregation was significantly improved by ultrasound treatment, and the average roughness value (Rq) was the smallest (10.3 nm) at 450 W. Additionally, HIU treatment reduced the interfacial tension and apparent viscosity of the emulsion. Thermal stability was best when the emulsion was treated at 450 W, D₄₃ was minimal (907.95 ± 31.72 nm), and emulsion separation also improved. Consequently, the creaming index (CI) was significantly decreased compared to the untreated sample, indicating that the storage stability of the emulsion was enhanced.     

Effect of high intensity ultrasound on the structure and solubility of soy protein isolate-pectin complex

In this study, a soy protein isolate (SPI)-pectin (PC) complex was prepared, and the effects of different high intensity ultrasound (HIU) powers on the structure and solubility of the complex were studied. Fourier transform infrared (FTIR) spectroscopy analysis exhibited that with increasing HIU power, the α-helix content of the SPI in the complex was significantly reduced, and the random coil content increased; however, an opposite trend appeared after higher power treatments. Fluorescence spectra showed that HIU treatment increased the fluorescence intensity of the complex, and the surface hydrophobicity was increased. The trend of the protein structure studied by Raman spectroscopy was similar to that of FTIR and fluorescence spectroscopy. When the HIU treatment was performed for 15 min and at 450 W power, the particle size of the complex was 451.85 ± 2.17 nm, and the solubility was 89.04 ± 0.19 %, indicating that the HIU treatment caused the spatial conformation of the protein to loosen and improved the functional properties of the complex. Confocal laser scanning microscopy (CLSM) revealed that the complex after HIU treatment exhibited improved dispersibility in water and smaller particle size. Gel electrophoresis results indicated that HIU treatment did not affect the protein subunits of the complex. Therefore, the selection of a suitable HIU treatment power can effectively improve the structural properties and solubility of SPI in the complex, and promote the application of the SPI-PC complex in food processing and industries.     

Airborne ultrasonic application on hot air-drying of pork liver. Intensification of moisture transport and impact on protein solubility

Nowadays, there is increasing interest in developing strategies for the efficient and sustainable use of animal by-products, such as pork liver. In order to stabilize the product, a prior dehydration stage may be required due to its high perishability. The water removal process of pork liver is energy costly and time consuming, which justifies its intensification using novel technologies. In this sense, the aim of this study was to assess the effect of the airborne application of power ultrasound on the hot air-drying of pork liver. For that purpose, drying experiments were carried out at 30, 40, 50, 60 and 70 °C on pork liver cylinders at 2 m·s⁻¹ with (US) and without ultrasonic application (AIR). The drying process was modeled from the diffusion theory and, in the dried pork liver, the protein solubility was analyzed in order to determine the effect of drying on the protein quality. The ultrasound application increased the drying rate, shortening the drying time by up to 40% at 30 °C. The effect of power ultrasound at high temperatures (60 and 70 °C) was of lesser magnitude. Drying at 70 °C involved a noticeable reduction in the protein solubility for dried liver, while the impact of ultrasound application on the solubility was not significant (p > 0.05).     

Effect of high intensity ultrasound on transglutaminase-catalyzed soy protein isolate cold set gel

The effects of high intensity ultrasound (HIU, 105–110 W/cm² for 5 or 40 min) pre-treatment of soy protein isolate (SPI) on the physicochemical properties of ensuing transglutaminase-catalyzed soy protein isolate cold set gel (TSCG) were investigated in this study. The gel strength of TSCG increased remarkably from 34.5 to 207.1 g for TSCG produced from SPI with 40 min HIU pre-treatment. Moreover, gel yield and water holding capacity also increased after HIU pre-treatments. Scanning electron microscopy showed that HIU of SPI resulted in a more uniform and denser microstructure of TSCG. The content of free sulfhydryl (SH) groups was higher in HIU TSCG than non-HIU TSG, even though greater decrease of the SH groups present in HIU treated SPI was observed when the TSCG was formed, suggesting the involvement of disulfide bonds in gel formation. Protein solubility of TSCG in both denaturing and non-denaturing solvents was higher after HIU pretreatment, and changes in hydrophobic amino acid residues as well as in polypeptide backbone conformation and secondary structure of TSCG were demonstrated by Raman spectroscopy. These results suggest that increased inter-molecular ε-(γ-glutamyl) lysine isopeptide bonds, disulfide bonds and hydrophobic interactions might have contributed to the HIU TSCG gel network. In conclusion, HIU changed physicochemical and structural properties of SPI, producing better substrates for TGase. The resulting TSCG network structure was formed with greater involvement of covalent and non-covalent interactions between SPI molecules and aggregates than in the TSCG from non-HIU SPI.     

Effects of ultrasound and ultrasound assisted alkaline pretreatments on the enzymolysis and structural characteristics of rice protein

The objectives of this study were to investigate the effects of multi-frequency energy-gathered ultrasound (MFEGU) and MFEGU assisted alkaline pretreatments on the enzymolysis and the mechanism of two pretreatments accelerating the rice protein (RP) proteolysis process. The results showed that MFEGU and MFEGU assisted alkaline pretreatments improved significantly (P < 0.05) the degree of hydrolysis (DH) and the protein elution amount of RP. Furthermore under the same DH conditions, ultrasound and ultrasound assisted alkaline pretreatments were more save the enzymolysis time than the unpretreatment. The changes in UV–vis spectra, fluorescence emission spectra indicated unfolding and destruction of RP by MFEGU and MFEGU assisted alkaline pretreatments. The circular dichroism analysis showed that both pretreatments decreased α-helix but increased β-sheet and random coil of RP. Amino acid composition revealed that MFEGU and MFEGU assisted alkaline pretreatments could increase the protein elution amount and the ratio of hydrophobic amino acids. Atomic force microscopy (AFM) indicated that both pretreatments destroyed the microstructures and reduced the particle size of RP. Therefore, MFEGU and MFEGU assisted alkaline pretreatments are beneficial to improving the degree of hydrolysis due to its sonochemistry effect on the molecular conformation as well as on the microstructure of protein.     

Effects of pulsed ultrasound on rheological and structural properties of chicken myofibrillar protein

The effects of pulsed ultrasound (PUS) (power: 240 w) with varying time (0, 3, 6, 9, 12 and 15 min) on rheological and structural properties of chicken myofibrillar protein (CMP) were examined. PUS treatment significantly caused a decrease in the viscosity coefficients (k) but an increase in the flow index (n) value of CMP solutions within short time (0–6 min), while had no significant effect for longer time (9–15 min). Besides, at 6 min, the solubility and microstructure of CMP samples were optimum. The primary structure of CMP was not altered by PUS treatment. However, Raman spectroscopy revealed a decrease in the α-helix and β-sheets proportion and an increase in the β-turn of CMP following PUS treatment. Random coil reached a maximum at 6 min. The changes in tertiary and quaternary structure of CMP by PUS treatment also occurred. As PUS time extended, S₀-ANS for CMP increased measured by ANS fluorescence probe method. However, the normalized intensity of 760 cm⁻¹ increased from 0 min to 6 min, and then decreased to 15 min by Raman test. Moreover, the reactive sulphur (SH) contents and disulfide bonds (S-S) of samples increased while the total SH contents decreased within 0–6 min. At 9 min and above, the contents of reactive SH groups were almost equal to the contents of total SH groups. Differential scanning calorimetry (DSC) of CMP showed that peak temperature (T_d2) for myosin and peak temperature (T_d3) for actin were both reduced in the first 6 min, while T_d3 was not observed from 9 min following PUS treatment. Therefore, 6 min was the optimum PUS time to obtain better CMP rheological and structural properties.     

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

Protein oxidation leads to covalent modification of structure and deterioration of functional properties of quinoa protein. The objective of this study was to investigate the effects of ultrasonic treatment on the functional and physicochemical properties of quinoa protein oxidation aggregates. In this concern, 2,2′-azobis (2-amidinopropane) dihydrochloride (AAPH) was selected as oxidative modification of quinoa protein. The microstructure of quinoa protein displayed by scanning electron microscope (SEM) indicated that oxidation induced extensive aggregation, leading to carbonylation and degradation of sulfhydryl groups. Aggregation induced by oxidation had a negative effect on the solubility, turbidity, emulsifying stability. However, according to the analysis of physicochemical properties, ultrasonic significantly improved the water solubility of quinoa protein. The quinoa protein treated by ultrasonic for 30 min exhibited the best dispersion stability in water, which corresponded to the highest ζ-potential, smallest particle size and most uniform distribution. Based on the FT-IR, SDS-PAGE and surface hydrophobicity analysis, the increase of α-helix, β-turn and surface hydrophobicity caused by cavitation effect appeared to be the main mechanism of quinoa protein solubilization. In addition, the hydrophobic region of the protein was re-buried by excessive ultrasonic treatment, and the protein molecules were reaggregated by disulfide bonds. Microstructural observations further confirmed that ultrasonic treatment effectively inhibited protein aggregation and improved the functional properties of quinoa protein.