Physicochemical properties and microstructure of composite surimi gels: The effects of ultrasonic treatment and olive oil concentration

This study was conducted to evaluate the effects of extra virgin olive (EVO) oil incorporation on the physicochemical properties and microstructure of surimi gels subjected to ultrasound-assisted water-bath heating. As the oil content was increased from 0 to 5 g/100 g, the breaking force and gel strength of the surimi gels significantly decreased, while the whiteness level exhibited the opposite tendency irrespective of the heating method. Compared with the traditional water-bath heating method, the ultrasonic heating promoted the unfolding of the α-helix structure and intensified the formation of β-sheet content and non-covalent bonds (ionic bonds, hydrogen bonds, and disulfide bonds), especially disulfide bonds, which contributed to the further crosslinking of the proteins and to gelation, thereby improving the gels’ strength. In addition, smaller cavities and compact microstructures were observed in the low-oil (≤3 g/100 g) surimi gels under ultrasonic treatment, which effectively prevented water migration in the gel network and resulted in a high water holding capacity and uniform water distribution. However, the ultrasonic treatment barely remedied the poor microstructures of the high-oil (>3 g/100 g) surimi gels owing to oil coalescence, which weakened the protein–protein interaction. In conclusion, ultrasonic treatment combined with water-bath heating significantly improved the gelation properties of the low-oil surimi gels, although it did not remarkably improve those of the high-oil gels. The choice of a suitable oil concentration could be of great importance for the production and functioning of surimi products via ultrasound-assisted treatments.     

Synergistic effects of oat β-glucan combined with ultrasound treatment on gel properties of silver carp surimi

The effect of oat β-glucan (OG) combined with ultrasound treatment on the gelation properties of silver carp surimi with different salt contents was investigated. The results demonstrated that the gelation properties of surimi gels at high salt concentration were superior than those at low salt level. The addition of OG or ultrasound treatment could significantly enhance the texture properties, gel strength and water holding capacity (WHC) of gel samples, regardless of salt contents. The ultrasound treatment improved the whiteness of surimi gels, whereas the OG addition slightly declined the whiteness. Both OG addition and ultrasound treatment markedly reduced the total sulfhydryl content (total SH) and strengthened the hydrophobic interactions, forming the more uniform and denser gel network structures, hence more water was captured in network structures and became immobilized. Moreover, the combined treatment of OG and ultrasound showed synergic action on the gelation properties of surimi, and the gel strength and WHC of low-salt surimi gel treated by the combination of OG and ultrasound were even superior than that of high-salt gel without OG by traditional heating.     

Improvement of gelation properties of silver carp surimi through ultrasound-assisted water bath heating

The present work investigated the effects of water bath heating coupled with different ultrasound treatments on the gel properties, protein conformation, microstructures and chemical interactions of silver carp surimi at low/high salt levels. Results showed that the gel strength, hardness, springiness and water holding capacity (WHC) of surimi gels at low salt concentration were inferior to those at high salt content, regardless of the treatments. Compared with the traditional water bath heating, ultrasonic-assisted treatments significantly improved the gelation properties of surimi at the same salt level. In fact, ultrasound treatment also facilitated the unfolding of α-helix structure of the protein, with the resulting exposure of internal groups further enhancing hydrophobic interactions and hydrogen bonds between protein molecules, thereby leading to the formation of denser microstructures with smaller holes. Furthermore, the most noteworthy ultrasonic treatment group was ultrasound-assisted preheating (U + W) group, whose gelation performance under low salt condition, was comparable with that of the traditional two-stage heating (W + W) group with high salt content. Overall, ultrasound-assisted water bath preheating proved to be a feasible approach to improve the gel properties and microstructures of low-salt surimi gels.     

Diacylglycerol pre-emulsion prepared through ultrasound improves the gel properties of golden thread surimi

This study determined the influence of diacylglycerol (DAG) pre-emulsion on the gel properties and microstructure of golden thread surimi gels. DAG emulsion stabilized using sodium caseinate was pre-emulsified through ultrasound. The average particle size of DAG pre-emulsion decreased from 1324.15 nm to 41.19 nm, with notable improvements in apparent viscosity and storage stability. The surimi gels with different amounts (0%, 1%, 3%, 5%, and 7% w/w) of DAG pre-emulsion were prepared under heat induction. The whiteness of the composite gels markedly increased with the incorporation of DAG pre-emulsion. The peak T₂₂ value of immobilized water, the gel strength, and water-holding capacity increased gradually, but it slightly decreased with the addition of 7% pre-emulsion. The curve of G′ and G″ kept climbing as the concentration of pre-emulsion, and the microstructure of the gel network tended to become denser and more orderly. Principal component analysis (PCA) of electronic nose results showed that the surimi gels containing pre-emulsion could be clearly distinguished from the control group. In conclusion, the addition of 5% DAG pre-emulsion to surimi not only improved gel properties to the highest extent but also be compensated for lipid loss during the rinsing of surimi.     

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.     

Physicochemical properties of tilapia (Oreochromis niloticus) actomyosin subjected to high intensity ultrasound in low NaCl concentrations

Effects of high intensity ultrasound (HIU) on physicochemical properties of tilapia (Oreochromis niloticus) actomyosin in low NaCl concentrations were investigated. The protein content extracted in low NaCl concentrations (0.1–0.3 M NaCl) increased with increasing HIU intensity up to 20.62 W/cm² (p < 0.05). The effect of HIU on actomyosin extractability in high NaCl concentrations (0.6 and 1.2 M NaCl) was less obvious. Ca²⁺-ATPase activity and total sulfhydryl (SH) group content decreased in both 0.2 and 0.6 M NaCl. HIU showed more pronounced effect on oxidation of the SH groups in 0.6 M NaCl, while the reactive SH content at 0.2 M NaCl increased after a prolonged exposure to HIU, suggesting conformational changes induced by HIU. Surface hydrophobicity of actomyosin in 0.6 M NaCl increased with increasing ultrasonic intensity and exposure time to a higher degree than that in 0.2 M NaCl. A greater absolute value of the zeta potential of actomyosin subjected to HIU were also observed. The HIU treatments decreased the turbidity of actomyosin incubated at 40 and 60 °C. A drastic increase in the solubility of myosin heavy chain (MHC) and actin with 0.2 M NaCl were evident when HIU treatments were applied, but degradation of MHC occurred in both 0.2 and 0.6 M NaCl. Based on particle size and microstructure, actomyosin in 0.6 M NaCl underwent more disruption by HIU than that in 0.2 M NaCl. HIU induced protein unfolding and protein dissociation, enabling better extraction in a lower NaCl concentration.     

Transglutaminase-induced gelation properties of soy protein isolate and wheat gluten mixtures with high intensity ultrasonic pretreatment

Soy protein isolate (SPI) and wheat gluten (WG) are widely used in commercial food applications in Asia for their nutritional value and functional properties. However, individually each exhibits poor gelation. In this study, we examined the microbial transglutaminase (MTGase)-induced gelation properties of SPI and WG mixtures with high intensity ultrasonic pretreatment. Ultrasonic treatment reduced the particle size of SPI/WG molecules, which led to improvements in surface hydrophobicity (H_o) and free sulfhydryl (SH) group content. However, MTGase crosslinking facilitated the formation of disulfide bonds, markedly decreasing the content of free SH groups. Ultrasonic treatment improved the gel strength, water holding capacity, and storage modulus and resulted in denser and more homogeneous networks of MTGase-induced SPI/WG gels. In addition, ultrasonic treatment changed the secondary structure of the gel samples as determined by Fourier transform infrared spectroscopic analysis, with a reduction in α-helices and β-turns and an increase in β-sheets and random coils. Thus, ultrasound is useful in facilitating the gelation properties of MTGase-induced SPI/WG gels and might expand their utilization in the food protein gelation industry.     

Ultrasound-assisted processing: Changes in gel properties,water-holding capacity,and protein aggregation of low-salt Hypophthalmichthys molitrix surimi by soy protein isolate

The effects of ultrasound combined (25 kHz, 400 ± 20 W/L, ultrasonic time of 5, 10 and 15 min) with soy protein isolate processing on gelling properties of low-salt silver carp surimi, aggregation and conformation of myofibrillar protein were investigated. The results revealed that, compared with only adding soy protein isolate components, ultrasound-assisted soy protein isolate had a more obvious effect on the protein structure in low-salt surimi, leading to the decrease in α-helix and total sulfhydryl contents, and the increase in β-sheet content and protein solubility. As a result, more proteins participated in the formation of the gel network, and significant improvements in hardness, gel strength and water-holding capacity of the low-salt surimi gel were observed, while the myosin heavy chain in SDS-PAGE was weakened. The low-field NMR results showed that the initial relaxation time of T₂ was apparently shorter, the free water content decreased and the bound water content increased under the action of ultrasound. Scanning electron microscope observation found that the surimi gel treated by ultrasound exhibited smaller holes, and had a more stable and denser network structure. In conclusion, the results of our work demonstrated that ultrasound combined with soy protein isolate can significantly improve the gel quality properties of low-salt silver carp.     

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.     

Gelation Rheology and Water Absorption Behavior of Semi-Interpenetrating Polymer Networks of Polyacrylamide and Carboxymethyl Cellulose

Gelation rheology and swelling behavior of novel semi-interpenetrating polymer network (semi-IPN) hydrogels based on polyacrylamide are described. These hydrogels were prepared by solution cross-linking of partially hydrolyzed polyacrylamide and carboxymethyl cellulose (CMC), using chromium triacetate. Effects of CMC content on the gelation process and swelling behavior in tap water and different electrolyte solutions were investigated. Study of the gelation behavior using dynamic rheometery showed that the limiting storage modulus of the semi-IPN gels increased with increasing CMC content. Enhancement of storage modulus was more than two times for the semi-IPN gels containing 50 wt% CMC. It was also found that increasing the CMC content decreased the loss factor, indicating that the elastic properties of this gelling system increase more strongly than the viscous properties. The swelling ratio of the semi-IPN gels in tap water, NaCl and CaCl₂ solutions, and synthetic oil reservoir water slightly decreased as the concentration of the CMC increased. The improved storage modulus and slightly decreased swelling capacity in oil reservoir water make these semi-IPN hydrogels potentially good candidates for excess water treatment in oil recovery applications.     

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.     

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.     

Diffusion limited cluster aggregation with irreversible slippery bonds

Irreversible diffusion limited cluster aggregation (DLCA) of hard spheres was simulated using Brownian cluster dynamics. Bound spheres were allowed to move freely within a specified range, but no bond breaking was allowed. The structure and size distribution of the clusters was investigated before gelation. The pair correlation function and the static structure factor of the gels were determined as a function of the volume fraction and time. Slippery bonds led to local densification of the clusters and the gels, with a certain degree of order. At low volume fractions densification of the clusters occurred during their growth, but at higher volume fractions it occurred mainly after gelation. At very low volume fractions, the large-scale structure (fractal dimension), size distribution and growth kinetics of the clusters was found to be close to that known for DLCA with rigid bonds. Restructuring of the gels continued for long times, indicating that aging processes in systems with strong attraction do not necessarily involve bond breaking. The mean-square displacement of particles in the gels was determined. It is shown to be highly heterogeneous and to increase with decreasing volume fraction.     

Enhanced gelling properties of myofibrillar protein by ultrasound-assisted thermal-induced gelation process: Give an insight into the mechanism

Effects of the incorporation of ultrasound with varied intensities (0–800 W) into the thermal-induced gelation process on the gelling properties of myofibrillar protein (MP) were explored. In comparison with single heating, ultrasound-assisted heating (<600 W) led to significant increases in gel strength (up to 17.9%) and water holding capacity (up to 32.7%). Moreover, moderate ultrasound treatment was conducive to the fabrication of compact and homogenous gel networks with small pores, which could effectively impair the fluidity of water and allow redundant water to be entrapped within the gel network. Electrophoresis revealed that the incorporation of ultrasound into the gelation process facilitated more proteins to get involved in the development of gel network. With the intensified ultrasound power, α-helix in the gels lowered pronouncedly with a simultaneous increment of β-sheet, β-turn, and random coil. Furthermore, hydrophobic interactions and disulfide bonds were reinforced by the ultrasound treatment, which was in support of the construction of preeminent MP gels.     

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.     

Influence of sonication,temperature, and agitation,on the physical properties of a palm-based fat crystallized in a continuous system

High-intensity ultrasound (HIU) has been used in the past to change fat crystallization and physical properties of fat crystalline networks. The objective of this work was to evaluate how HIU placed on different positions in a scraped surface heat exchanger (SSHE) using different processing conditions affect the physical properties of an interesterified palm olein. The sample was crystallized at two temperatures (20 °C and 25 °C) and two agitation rates (344/208 rpm and 185/71 rpm, barrels/pin worker). HIU (12.7 mm-diameter tip, 50% amplitude, 5 s pulses) was placed at three different positions within the SSHE. After processing, samples were stored at 25 °C for 48 h and analyzed according to the crystal morphology, solid fat content (SFC), oil binding capacity (OBC), melting behavior, viscoelasticity, and hardness. Physical properties were affected by crystallization conditions, by sonication, and by HIU position. The greatest improvement obtained was at 20 °C using low agitation when HIU was placed at the beginning of the SSHE. These conditions result in a sample with 98.9% of OBC, 274 kPa of viscoelasticity and 31 N of hardness. These results show that HIU can be used as an additional processing tool to improve physical properties of a palm-based fat and that the best improvement was obtained as a combination of crystallization conditions and HIU position.     

Effects of ultrasonic–microwave combination treatment on the physicochemical,structure and gel properties of myofibrillar protein in Penaeus vannamei (Litopenaeus vannamei) surimi

The objective of this study was to evaluate the effects of single ultrasound (360 W, 20 min), single microwave (10 W/g, 120 s) and ultrasonic–microwave combination treatment on shrimp surimi gel properties. The structure and physicochemical properties of myofibrillar protein (MP) were also determined. Low-field nuclear magnetic resonance showed that the fluidity of water molecules and the moisture content decreased, the stability and water holding capacity (WHC) increased after single ultrasound, single microwave and ultrasonic–microwave combination treatment. Compared with the traditional water bath treatment, ultrasound and microwave treatment reduced the total sulfhydryl content and promoted the formation of intermolecular disulfide bonds and hydrophobic interactions, which improved the compactness of the network structure of shrimp surimi gel. Moreover, Fourier transform infrared spectroscopy and sodium dodecyl sulfate–polyacrylamide gel electrophoresis analysis revealed that these treatments not only inhibited the degradation of MP, but also decreased the α-helix content and increased the β-sheet content. The three treatments also significantly reduced the particle size and decreased the solubility of MP. Overall, the effect of ultrasonic–microwave combination treatment was superior to that of either single treatment.     

Study on the Dynamic Rheometry and Swelling Properties of the Polyacrylamide/Laponite Nanocomposite Hydrogels in Electrolyte Media

Polyacrylamide/laponite/chromium triacetate nanocomposite (NC) hydrogels were prepared by incorporation of the laponite nanoparticles in partially hydrolyzed polyacrylamide followed by cross-linking of their aqueous solutions with chromium triacetate. Influence of nanoparticle, cross-linker, polymer concentrations, and gelation media (water) temperature, salinity, and rheometer frequency on the viscoelastic behavior of the NC hydrogels were studied by probing the network properties. In addition, swelling behaviors of these NC gels in tap and oil reservoir water were evaluated. According to dynamic rheometry of the gelation process, the limiting storage modulus of the NC gels increased with increasing laponite content. The addition of laponite into the polyacrylamide gelling system increased their viscous properties more strongly than the elastic properties. The ultimate elastic modulus of the NC gels increased with increasing water salinity and temperature. Increasing rheometer frequency during gelation retarded the sol–gel transition and decreased the ultimate elastic modulus. The equilibrium swelling ratio of the NC hydrogels in tap water decreased with increasing laponite content. The salt sensitivity of the NC gels in oil reservoir water slightly decreased with increasing laponite content. These results suggest the superiority of the hydrolyzed polyacrylamide (HPAM)/chromium acetate/laponite NC hydrogels for water shut-off applications in oil reservoirs as compared with unfilled HPAM gels.     

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.     

Effect of ultrasonic pretreatment on the rheology and structure of grass pea (Lathyrus sativus L.) protein emulsion gels induced by transglutaminase

In this study, emulsion gels were prepared by sonicated grass pea protein isolates (GPPI) at different ultrasonic amplitudes (25, 50 and 75 %) and times (5, 10 and 20 min). Formation of emulsion gels was induced by transglutaminase. Enzymatic gelation of emulsions stabilized by sonicated GPPI occurred in two stages. A relatively fast stage led to the formation of a weak gel which was followed by a slow stage that strongly reinforced the gel structure. Emulsion gels fabricated by sonicated GPPIs showed a homogeneous and uniform droplet distribution with higher elastic modulus compared to the native protein. A stiffer emulsion gel with a higher G' was formed after the protein was treated at 75 % amplitude for 10 min. After sonication of GPPI, the water holding capacity (WHC) of emulsion gels increased in accordance with the mechanical properties. Higher intermolecular cross-linking within the gel network increased the thermal stability of emulsion gels fabricated by sonicated GPPI. Although sonicated-GPPI emulsion gels clearly displayed homogenous microstructure in comparison to that made with native GPPI, the microstructures of these gels were nearly identical for all sonication amplitudes and times.