Emulsion gels stabilized by soybean protein isolate and pectin: Effects of high intensity ultrasound on the gel properties,stability and β-carotene digestive characteristics

In this study, soybean protein isolate (SPI) and pectin emulsion gels were prepared by thermal induction, and the effects of high intensity ultrasound (HIU) at various powers (0, 150, 300, 450 and 600 W) on the structure, gel properties and stability of emulsion gels were investigated. Fourier transform infrared spectroscopy (FTIR) and X-ray diffraction (XRD) showed that the interaction between SPI and pectin was enhanced and the crystallinity of the emulsion gels was changed due to the HIU treatment. Confocal laser scanning microscopy (CLSM) and scanning electron microscopy (SEM) observations revealed that the particle size of the emulsion gels was decreased significantly by HIU treatment. The emulsion gel structure became more uniform and denser, which was conducive to storage stability. In addition, according to the low field nuclear magnetic resonance (LF-NMR) analysis, HIU treatment had no obvious impact on the content of bound water as the power increased to 450 W, while the content of free water decreased gradually and became immobilized water, which indicated that the water holding capacity of the emulsion gels was enhanced. Compared with untreated emulsion gel, differential scanning calorimetry (DSC) analysis showed that the denaturation temperature reached 131.9 ℃ from 128.2 ℃ when treated at 450 W. The chemical stability and bioaccessibility of β-carotene in the emulsion gels were improved significantly after HIU treatment during simulated in vitro digestion.     

Effect of high-intensity ultrasonic treatment on the emulsion of hemp seed oil stabilized with hemp seed protein

In this study, hemp seed oil (HSO) emulsions stabilized with hemp seed protein (HPI) were prepared and treated with high intensity ultrasonic (HIU). The effects of different treatment powers (0, 150, 300, 450, 600 W) on the properties, microstructure and stability of emulsions were investigated. HIU-treated emulsions showed improved emulsifying activity index and emulsifying stability index, reduced particle size, and increased absolute values of ζ-potential, with the extreme points of these indices occurring at a treatment power of 450 W. Here, the emulsion showed the best dispersion and the smallest particle size in fluorescence microscopy observation, with the highest adsorbed protein content (30.12%), and the highest tetrahydrocannabinol (THC) retention rate (87.64%). The best thermal and oxidative stability of the emulsions were obtained under HIU treatment with a power of 450 W. The D₄₃ and the peroxide values (POV) values after 30 d storage were the smallest at 985.74 ± 64.89 nm and 4.6 μmol/L, respectively. Therefore, 450 W was optimal HIU power to effectively improve the properties of HPI-stabilized HSO emulsion and promote the application of HSO and its derivatives in food processing production.     

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.     

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

This study evaluated the effects of high intensity ultrasonication (HIU, 100, 150, 200, and 250 W) and treatment time (0, 3, 6, 9, and 12 min) on the structure and emulsification properties of myofibrillar proteins (MPs) from Coregonus peled. These investigations were conducted using an ultrasonic generator at a frequency of 20 kHz (ultrasonic probe). Analysis of the carbonyl content and total number of sulfhydryl groups showed that HIU significantly improved the oxidative modification of MPs (P < 0.05). SDS-PAGE profiling showed significant degradation of the myosin heavy chain (P < 0.05). In addition, Fourier transformed infrared spectroscopy (FTIR) revealed that HIU altered these treated MP secondary structures, this was due to molecular unfolding and stretching, exposing interior hydrophobic groups. Particle size analysis showed that HIU treatment reduced particle sizes. Solubility, emulsification capacity, and emulsion stability were improved significantly, and each decreased with an increase in treatment time (up to 12 min), indicating aggregation with prolonged sonication. These results indicate that HIU could improve the emulsification properties of MPs from C. peled, demonstrating a promising method for fish protein processing.     

High-intensity ultrasound improves the physical stability of myofibrillar protein emulsion at low ionic strength by destroying and suppressing myosin molecular assembly

The specific molecular behavior of myofibrillar proteins (MPs) in low-salt media limits the development of muscle protein-based emulsions. This study aimed to evaluate the potential of high-intensity ultrasound (HIU; 150, 300, 450, and 600 W) to improve the physical stability of MP emulsion at low ionic strength and decipher the underlying mechanism. According to the physical stability analysis, HIU pretreatment, especially at 450 W power, significantly improved the physical stability of MP emulsions, as evidenced by the reduced particle size, enhanced inter-droplet interactions, and increased uniformity of the droplet size distribution (p < 0.05). The results of interfacial protein composition, Fourier transform infrared spectroscopy analysis, and microscopic morphology observation of the aqueous MP suspension suggested that HIU induced the depolymerization of filamentous myosin polymers and inhibited the subsequent self-assembly behavior. These effects may facilitate protein adsorption and molecular rearrangement at the oil–water interface, forming a complete interfacial layer and, thus, droplet stabilization. Confocal laser scanning microscopy observations further confirmed these results. In conclusion, these findings provide direct evidence for the role of HIU in improving the physical stability of MP emulsions at low ionic strength.     

Synergistic modification of pea protein structure using high-intensity ultrasound and pH-shifting technology to improve solubility and emulsification

The most important factors restricting research and application in the food industry are the poor solubility and emulsification of pea protein isolate (PPI). This study investigates the effect of high-intensity ultrasound (HIU, 0–600 W) and pH-shifting treatment, alone or combined, on the structure, solubility, and emulsification of PPI, as well as its potential mechanism. The results revealed that the PPI solubility significantly increases when treated with the combination, corresponding to a decrease in the protein particle size, especially at 500 W of HIU power (p < 0.05). Correspondingly, the emulsion prepared from it was less prone to phase separation during storage. According to the structural analysis, the structural changes caused by protein unfolding (i.e., the exposure of hydrophobic and polar sites and the loss of the α-helix) seemed to be the primary reasons for increased PPI solubility. In addition, confocal laser scanning microscopy indicated that the combination treatment accelerated the adsorption of PPI at the oil/water interface and strengthened the compactness of the interface film. Improved interfacial properties and intermolecular forces played a critical role in the resistance to droplet coalescence in PPI emulsion. In conclusion, ultrasound and pH-shifting treatments have a synergistic effect on improving the solubility and emulsification of PPI.     

Solubilization and stable dispersion of myofibrillar proteins in water through the destruction and inhibition of the assembly of filaments using high-intensity ultrasound

The insolubility and poor dispersion of myofibrillar proteins (MPs) in water have always been the primary factors limiting the development of novel meat-based products. This study aimed to explore the mechanisms by which high-intensity ultrasound (HIU) at various power settings (0, 150, 300, 450 and 600 W) improved the solubility and dispersion stability of MPs in water. According to the solubility analysis, HIU significantly increased the water solubility of MPs (p < 0.05). The MPs treated with 450 W exhibited the best dispersion stability in water, which corresponded to the highest zeta-potential, smallest particle size and most uniform distribution (p < 0.05). Based on the circular dichroism and fluorescence spectroscopy and surface hydrophobicity analysis, the loss of the MP superhelix and subsequent random dissociation of the filamentous myosin structure appeared to be the main mechanism of MP solubilization. In addition, according to the zeta-potential, SDS-PAGE and Nano LC-ESI-MS/MS analyses, the increase in surface charge and the formation of soluble oligomers may provide additional forces to inhibit filament assembly, thereby improving the stability of the aqueous MP suspension. Atomic force microscopy (AFM) observations further confirmed these results. In conclusion, an HIU treatment effectively improves the solubility and dispersion stability of MP in water.     

Effect of ultrasonic power on the stability of low-molecular-weight oyster peptides functional-nutrition W1/O/W2 double emulsion

Ultrasonic-assisted treatment is an eco-friendly and cost-effective emulsification method, and the acoustic cavitation effect produced by ultrasonic equipment is conducive to the formation of stable emulsion. However, its effect on the underlying stability of low-molecular-weight oyster peptides (LOPs) functional-nutrition W₁/O/W₂ double emulsion has not been reported. The effects of different ultrasonic power (50, 75, 100, 125, and 150 W) on the stability of double emulsions and the ability to mask the fishy odor of LOPs were investigated. Low ultrasonic power (50 W and 75 W) treatment failed to form a well-stabilized double emulsion, and excessive ultrasound treatment (150 W) destroyed its structure. At an ultrasonic power of 125 W, smaller particle-sized double emulsion was formed with more uniform distribution, more whiteness, and a lower viscosity coefficient. Meanwhile, the cavitation effect generated by 125 W ultrasonic power improved storage, and oxidative stabilities, emulsifying properties of double emulsion by reducing the droplet size and improved sensorial acceptability by masking the undesirable flavor of LOPs. The structure of the double emulsion was further confirmed by optical microscopy and confocal laser scanning microscopy. The ultrasonic-assisted treatment is of potential value for the industrial application of double emulsion in functional-nutrition foods.     

Effect of ultrasound on the preparation of soy protein isolate-maltodextrin embedded hemp seed oil microcapsules and the establishment of oxidation kinetics models

In this study, microcapsules were prepared by spray drying and embedding hemp seed oil (HSO) with soy protein isolate (SPI) and maltodextrin (MD) as wall materials. The effect of ultrasonic power on the microstructure and characteristics of the composite emulsion and microcapsules was studied. Studies have shown that ultrasonic power has a significant impact on the stability of composite emulsions. The particle size of the composite emulsion after 450 W ultrasonic treatment was significantly lower than the particle size of the emulsion without the ultrasonic treatment. Through fluorescence microscopy observation, HSO was found to be successfully embedded in the wall materials to form an oil/water (O/W) composite emulsion. The spray-dried microcapsules showed a smooth spherical structure through scanning electron microscopy (SEM), and the particle size was 10.7 μm at 450 W. Fourier transform infrared (FTIR) spectroscopy analysis found that ultrasonic treatment would increase the degree of covalent bonding of the SPI-MD complex to a certain extent, thereby improving the stability and embedding effect of the microcapsules. Finally, oxidation kinetics models of HSO and HSO microcapsules were constructed and verified. The zero-order model of HSO microcapsules was found to have a higher degree of fit; after verification, the model can better reflect the quality changes of HSO microcapsules during storage.     

Exploring the influence of ultrasound on the antibacterial emulsification stability of lysozyme-oregano essential oil

A lysozyme-oregano essential oil (Lys-OEO) antibacterial emulsion was developed via ultrasonic treatment. Based on the general emulsion materials of ovalbumin (OVA) and inulin (IN), the addition of Lys and OEO successfully inhibited the growth of E. coli and S. aureus, two representatives of which were Gram-negative and Gram-positive bacteria respectively. The emulsion system in this study was designed to compensate for the limitation that Lys could only act on Gram-positive bacteria, and the stability of the emulsion was improved using ultrasonic treatment. The optimal amounts among OVA, Lys and OEO were found to be the mass ratio of 1:1 (Lys to OVA) and 20% (w/w) OEO. The ultrasonic treatment at the power of 200, 400, 600, and 800 W and time length of 10 min improved the stability of emulsion, in which the surface tension was below 6.04 mN/m and the Turbiscan stability index (TSI) did not exceed 10. The multiple light scattering showed that sonicated emulsions were less prone to delamination; salt stability and pH stability of emulsions were improved, CLSM image showed emulsion as oil-in-water type. In the meantime, the particles of the emulsions were found to become smaller and more uniform with ultrasonic treatment. The best dispersion and stability of the emulsion were both achieved at 600 W with a zeta potential of 7.7 mV, the smallest particle size and the most uniform particle distribution.     

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

In this study, scallop mantle protein was treated by ultrasound at different powers, and then analyzed by ANS fluorescent probes, circular dichroism spectroscopy, endogenous fluorescence spectrum, DNTB colorimetry and in-vitro digestion model to elucidate the structure–function relationship. The results indicated that ultrasound can significantly affect the secondary structure of scallop mantle protein like enhancing hydrophobicity, lowering the particle size, increasing the relative contents of α-helix and decreasing contents of β-pleated sheet, β-turn and random coil, as well as altering intrinsic fluorescence intensity with blue shift of maximum fluorescence peak. But ultrasound had no effect on its primary structure. Moreover, the functions of scallop mantle protein were regulated by modifying its structures by ultrasound. Specifically, the protein had the highest performance in foaming property and in-vitro digestibility under ultrasonic power of 100 W, oil binding capacity under 100 W, water binding capacity under 300 W, solubility and emulsification capacity under 400 W, and emulsion stability under 600 W. These results prove ultrasonic treatment has the potential to effectively improve functional properties and quality of scallop mantle protein, benefiting in comprehensive utilization of scallop mantles.     

Effect of slit dual-frequency ultrasonic emulsification technology on the stability of walnut emulsions

A highly hygienic walnut emulsion beverage was prepared by using a slit dual-frequency emulsification technique. The optimal ultrasonic parameters were studied as a model system: the ultrasonic time of 50 min, the ultrasonic power density of 260 W/L, and a dual-frequency ultrasonic combination of 28/68 kHz. Walnut emulsion with an average mean volume diameter of 2.05 µm, a Zeta potential absolute value of 40 mV was obtained after ultrasonic treatment, and the emulsion stability could be maintained for more than 14 days without phase separation. At the lowest ultrasonic energy input, the vibrating emulsion could promote droplet aggregation. However, excessive energy input could result in sample overtreatment and reduced emulsion activity. The laser scanning confocal microscope (LSCM) and transmission electron microscope (TEM) confirmed that walnut emulsion processed by slit dual-frequency ultrasonic had pretty high stability. Therefore, the slit dual-frequency ultrasonic emulsification technique was found to be well suited for the preparation of complex and fine oil-in-water food emulsions.     

Effect of high-intensity ultrasound on the technofunctional properties and structure of jackfruit (Artocarpus heterophyllus) seed protein isolate

The influence of high-intensity ultrasound (HIU) on the technofunctional properties and structure of jackfruit seed protein isolate (JSPI) was investigated. Protein solutions (10%, w/v) were sonicated for 15 min at 20 kHz to the following levels of power output: 200, 400, and 600 W (pulse duration: on-time, 5 s; off-time 1 s). Compared with untreated JSPI, HIU at 200 W and 400 W improved the oil holding capacity (OHC) and emulsifying capacity (EC), but the emulsifying activity (EA) and emulsion stability (ES) increased at 400 W and 600 W. The foaming capacity (FC) increased after all HIU treatments, as opposed to the water holding capacity (WHC), least gelation concentration (LGC), and foaming stability (FS), which all decreased except at pH 4 for FS. Tricine sodium dodecyl sulfate polyacrylamide gel electrophoresis (Tricine-SDS-PAGE) showed changes in the molecular weight of protein fractions after HIU treatment. Scanning electron microscopy (SEM) demonstrated that HIU disrupted the microstructure of JSPI, exhibiting larger aggregates. Surface hydrophobicity and protein solubility of the JSPI dispersions were enhanced after ultrasonication, which increased the destruction of internal hydrophobic interactions of protein molecules and accelerated the molecular motion of proteins to cause protein aggregation. These changes in the technofunctional and structural properties of JSPI could meet the complex needs of manufactured food products.     

Fabrication of bilayer emulsion by ultrasonic emulsification: Effects of chitosan on the interfacial stability of emulsion

In this study, the stable system of bilayer emulsion was fabricated by ultrasonic emulsification. The effect of chitosan (CS) addition (0.05 %-0.4 %, w/v) at pH 5.0 on the stability of rice bran protein hydrolysate-ferulic acid (RBPH-FA) monolayer emulsion was investigated. It was found that the addition of CS (0.3 %) could form a stable bilayer emulsion. The droplet size was 3.38 μm and the absolute ζ-potential value was 31.52 mV. The bilayer emulsion had better storage stability, oxidation stability and environmental stabilities than the monolayer emulsion. The results of in vitro simulations revealed the bilayer emulsion was able to deliver the β-carotene to the small intestine digestive stage stably and the bioaccessibility was increased from 22.34 % to 61.36 % compared with the monolayer emulsion. The research confirmed that the bilayer emulsion prepared by ultrasonic emulsification can be used for the delivery of hydrophobic functional component β-carotene.     

Improvement of structural,physicochemical, and rheological properties of porcine myofibrillar proteins by high-intensity ultrasound treatment for application as Pickering stabilizers

This study aimed to evaluate the potential of time-dependent (0, 15, 30, 60, 120 min) treatment of porcine-derived myofibrillar proteins (MPs) with high-intensity ultrasound (HIU) for utilizing them as a Pickering stabilizer and decipher the underlying mechanism by which HIU treatment increases the emulsification and dispersion stability of MPs. To accomplish this, we analyzed the structural, physicochemical, and rheological properties of the HIU-treated MPs. Myosin heavy chain and actin were observed to be denatured, and the particle size of MPs decreased from 3,342.7 nm for the control group to 153.9 nm for 120 min HIU-treated MPs. Fourier-transformed infrared spectroscopy and circular dichroism spectroscopy confirmed that as the HIU treatment time increased, α-helical content increased, and β-sheet decreased, indicating that the protein secondary/tertiary structure was modified. In addition, the turbidity, apparent viscosity, and viscoelastic properties of the HIU-treated MP solution were decreased compared to the control, while the surface hydrophobicity was significantly increased. Analyses of the emulsification properties of the Pickering emulsions prepared using time-dependent HIU-treated MPs revealed that the emulsion activity index and emulsion stability index of HIU-treated MP were improved. Confocal laser scanning microscopy images indicated that small spherical droplets adsorbed with MPs were formed by HIU treatment and that dispersion stabilities were improved because the Turbiscan stability index of the HIU-treated group was lower than that of the control group. These findings could be used as supporting data for the utilizing porcine-derived MPs, which have been treated with HIU for appropriate time periods, as Pickering stabilizers.     

Effects of ultrasound-assisted vacuum tumbling on the oxidation and physicochemical properties of pork myofibrillar proteins

The present research aimed to investigate the effects of high-intensity ultrasound (HIU, 20 kHz, 0 W, 100 W, 300 W and 500 W)-assisted vacuum tumbling (UVT) for 60 min and 120 min on the oxidation and physicochemical properties of the pork myofibrillar proteins (MPs). Compared with the vacuum tumbling (VT) groups without the HIU assistance, the carbonyl content increased, while the total sulfhydryl (SH) content was reduced with the increase of HIU power and treatment time (P < 0.05). The reactive SH content was increased significantly after treated by UVT with 300 W compared with the VT group (P < 0.05) regardless of the treatment time. Similarly, the surface hydrophobicity (S₀), the intrinsic tryptophan intensity, and the solubility in the UVT group (300 W) were remarkably higher than those of the VT group (P < 0.05). In contrast, the α-helix content and the particle size of MPs significantly decreased when the HIU power was at 100 W and 300 W (P < 0.05). The results suggest that UVT treatment could change the structure and physicochemical properties of MPs accompanied by protein oxidation.     

Effects of ultrasound on the structural and emulsifying properties and interfacial properties of oxidized soybean protein aggregates

Oxidative attack leads to the oxidative aggregation and structural and functional feature weakening of soybean protein. We aimed to investigate the impact of ultrasonic treatment (UT) with different intensities on the structure, emulsifying features and interfacial features of oxidized soybean protein aggregates (OSPI). The results showed that oxidative treatment could disrupt the native soy protein (SPI) structure by promoting the formation of oxidized aggregates with β1-sheet structures through hydrophobic interactions. These changes led to a decrease in the solubility, emulsification ability and interfacial activity of soybean protein. After low-power ultrasound (100 W, 200 W) treatment, the relative contents of β1-sheets, β2-sheets, random coils, and disulfide bonds of the OSPI increased while the surface hydrophobicity, absolute ζ-potential value and free sulfhydryl content decreased. Moreover, protein aggregates with larger particle sizes and poor solubility were formed. The emulsions prepared using the OSPI showed bridging flocculation and decreased protein adsorption and interfacial tension. After applying medium-power ultrasound (300 W, 400 W, and 500 W) treatments, the OSPI solubility increased and particle size decreased. The α-helix and β-turn contents, surface hydrophobicity and absolute ζ-potential value increased, the structure unfolded, and the disulfide bond content decreased. These changes improved the emulsification activity and emulsion state of the OSPI and increased the protein adsorption capacity and interfacial tension of the emulsion. However, after a high-power ultrasound (600 W) treatment, the OSPI showed a tendency to reaggregate, which had a certain negative effect on the emulsification activity and interfacial activity. The results showed that UT at an appropriate power could depolymerize OSPI and improve the emulsification and interfacial activity of soybean protein.     

Effect of ultrasonic pretreatment on the emulsification properties of Clanis Bilineata Tingtauica Mell protein

Clanis Bilineata Tingtauica Mell Protein (CBTMP) is a naturally high-quality insect protein resource, while its poor emulsification has limited its application in food industry. In order to change the present situation, in this research, the ultrasonic pretreatment (0 W, 200 W, 400 W, 600 W, and 800 W) method was used to improve the emulsification properties of CBTMP. Results indicated that ultrasound treatment especially at 400 W could significantly change the particle sizes, further increase the content of sulfhydryl group and surface hydrophobicity. The emulsification properties of emulsions were enhanced (from 4.16 ± 1.07 m²/g to 27.62 ± 2.20 m²/g) by sonicated CBTMP solution. Moreover, the physical stability of the emulsions to salt stress and centrifugation treatment was also promoted. Additionally, rheology revealed that a stronger network was formed at 400 W and all samples exhibited frequency-dependent and amplitude-dependent properties. The experiment demonstrated that ultrasound pretreatment was an effective means to improve the emulsification properties of CBTMP and it could provide a promising perspective for the application of CBTMP in food industry.     

Synergistic effect of preheating and different power output high-intensity ultrasound on the physicochemical,structural, and gelling properties of myofibrillar protein from chicken wooden breast

The effects of preheating to 50 ℃ and the subsequent application of high-intensity ultrasound (HIU, 20 kHz) at 200, 400, 600, and 800 W on the physicochemical, structural, and gelling properties of wooden breast myofibrillar protein (WBMP) were studied. Results suggested that the WBMP structure expanded to the balanced state at 600 W, and rheological properties exhibit that 600 W HIU (P < 0.05) significantly improved the storage modulus (G′) of WBMP. Notably, the WBMP gel (600 W) had the best hardness (65.428 ± 0.33 g), springiness (0.582 ± 0.01), and water-holding capacity (86.11 ± 0.83%). Raman spectra and low-field NMR indicated that 600 W HIU increased the β-fold content (37.94 ± 0.04%) and enlarged the immobilized-water proportion (93.87 ± 0.46%). Scanning electron micrographs confirmed that the gel was uniform and dense at 600 W. Therefore, preheating to 50 ℃ followed by HIU (600 W) helped form a superior WBMP gel.     

High intensity ultrasound-assisted quality enhancing of the marinated egg: Gel properties and in vitro digestion analysis

In this study, high intensity ultrasonication (HIU) was employed as an efficient tool to improve the gel property and in vitro digestibility of marinated egg (ME). The effects of HIU treatment at 100 W and 200 W for a series of time periods (0.5 h, 1 h, and 2 h) on the textural profiles, structural changes, and microstructures were also studied. After HIU treatment, the springiness and gumminess of ME white were enhanced. The water holding capacity reached the highest point (66.6%) when 0.5 h 200 W HIU was used. It was observed that 100 W HIU led to the highest zeta potential (-12.0 mV) and hydrophobicity (175.35 μg) of ME, indicating a high degree of electrostatic repulsion prevented agglomeration. HIU treatment at 100 W affected the dynamic rheological behaviors by boosting non-covalent bonds, which maintains the gel network's homogeneity. Meanwhile, the decreasing formation of α-helix, in contrast to β-turn, altered the aggregation behaviors of egg white gel. The microstructure of the 200 W HIU treated samples had porous colloidal network structures, and the in vitro digestibility (>75%) was increased after HIU. This work demonstrated that HIU could be a green and cost-effective tool for processing the egg product with high quality.