Formation of soybean protein isolate-hawthorn flavonoids non-covalent complexes: Linking the physicochemical properties and emulsifying properties

In recent years, more and more attention had been paid to the combination of proteins and flavonoids, and several flavonoids had been reported to improve the physicochemical and emulsifying properties of proteins. This study investigated the effects of ultrasonic treatment (450 W for 10 min, 20 min, and 30 min) on the physicochemical properties, antioxidant activity, and emulsifying properties of soy protein isolate (SPI) -hawthorn flavonoids (HF) non-covalent complexes. The results showed that the addition of HF to SPI and 20 min of ultrasound could reduce α-helix and random coil, increase β-sheet and β-turn, and enhance fluorescence quenching. In addition, it decreased the particle size, zeta potential, surface hydrophobicity, and turbidity to 88.43 or 95.27 nm, −28.80 mV, 1250.42, and 0.23, respectively. The protein solubility, free sulfhydryl group, antioxidant activity, emulsifying activity index, and emulsifying stability index all increased to 73.93%, 15.07 μmol/g, 71.00 or 41.91%, 9.81 m²/g, and 67.71%, respectively. Moreover, high-density small and low-flocculation droplets were formed. Therefore, the combined ultrasound treatment and addition of HF to SPI is a more effective method for protein modification compared to ultrasound treatment alone. It provides a theoretical basis for protein processing and application in the future.     

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.     

Ultrasound-assisted limited enzymatic hydrolysis of high concentrated soy protein isolate: Alterations on the functional properties and its relation with hydrophobicity and molecular weight

The effects of power ultrasound (US) pretreatment on the preparation of soy protein isolate hydrolysate (SPIH) prepared at the same degree of hydrolysis (DH) of 12 % were measured. Cylindrical power ultrasound was modified into mono-frequency (20, 28, 35, 40, 50 kHz) ultrasonic cup coupled with an agitator to make it applicable for high density SPI (soy protein isolate) solutions (14 %, w/v). A comparative study of the alterations of the hydrolysates molecular weight, hydrophobics, antioxidants and functional properties change as well as their relation were explored. The results showed that under the same DH, ultrasound pretreatment decelerated the degradation of protein molecular mass and the decrease rate of the degradation lessened with the increase of ultrasonic frequency. Meanwhile, the pretreatments improved the hydrophobics and antioxidants properties of SPIH. Both surface hydrophobicity (H₀) and relative hydrophobicity (RH) of the pretreated groups increased with the decrease of ultrasonic frequency. Lowest frequency (20 kHz) ultrasound pretreatment had the most improved emulsifying properties and water holding capacities, although decrease in the viscosity and solubility were found. Most of these alterations were correspondence toward the change in hydrophobics properties and molecular mass. In conclusion, the frequency selection of ultrasound pretreatment is essential for the alteration of SPIH functional qualities prepared at the same DH.     

Effect of ultrasound on the structural characteristics and oxidative stability of walnut oil oleogel coated with soy protein isolate-phosphatidylserine

In this study, the three-dimensional network system formed by rice bran wax (RBW) was used as the internal structure, and the external structure formed by soybean protein isolate (SPI) and phosphatidylserine (PS) was added on the basis of the internal structure to prepare walnut oil oleogel (SPI-PS-WOG). Ultrasonic treatment was applied to the mixed solution to make SPI-PS-WOG, on the basis, the effects of ultrasonic treatment on SPI-PS-WOG were investigated. The results showed that both β and β’ crystalline forms were present in all SPI-PS-WOG samples. When the ultrasonic power was 450 W, the first weight loss peak in the thermogravimetric (TGA) curve appeared at 326 °C, which was shifted to the right compared to the peak that occurred when the ultrasonic power was 0 W, indicating that the thermal stability of the SPI-PS-WOG was improved by the ultrasonic treatment. Moreover, when the ultrasonic power was 450 W, the oil holding capacity (OHC) reached 95.3 %, which was the best compared with other groups. Both confocal laser scanning microscopy (CLSM) and scanning electron microscopy (SEM) showed that the ultrasonic treatment of appropriate power succeeded in making the SPI-PS-WOG samples more evenly dispersed in the internal structure and denser in the external structure. In terms of oxidative stability, it was found that the peroxide value of SPI-PS-WOG remained at 9.8 mmol/kg oil for 50 days under 450 W ultrasonic power treatment, which was significantly improved compared with liquid walnut oil (WO). These results provide a new idea for the preparation of oleogels, and also lay a theoretical foundation for the application of ultrasonic treatment in oleogels.     

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.     

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.     

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.     

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.     

Effects of ultrasound pretreatment on functional property,antioxidant activity,and digestibility of soy protein isolate nanofibrils

Nanofibrils, an effective method to modulate the functional properties of proteins, can be promoted by ultrasound pretreatment. This study investigated the effect of ultrasound pretreatment on the structure, functional property, antioxidant activity and digestibility of soy protein isolate (SPI) nanofibrils. The results showed that high amplitude ultrasound had a significant effect on structure of SPI nanofibrils. SPI nanofibrils pretreated by 80% amplitude ultrasound showed a blueshift of the amide II band in Fourier transform infrared spectroscopy (FTIR), resulted in more tryptophan residues being buried and increased the crystallinity. Low amplitude ultrasound (20%) pretreatment significantly improved the solubility, emulsifying activity index (EAI) and water absorption capacity (WAC) of SPI nanofibrils, but 80% amplitude ultrasound pretreatment of SPI nanofibrils reduced emulsifying stability index (ESI). High amplitude ultrasound (60% and 80%) pretreatment of SPI nanofibrils improved the foaming capacity and foaming stability and decreased denaturation temperature. DPPH radical scavenging activity of SPI nanofibrils were significantly improved by ultrasound pretreatment. 20% amplitude ultrasound pretreatment improved DPPH, ABTS radical scavenging activity and ferric reducing antioxidant power of SPI nanofibrils. The digestion rate of 80% amplitude ultrasound-pretreated nanofibrils were consistently higher, and SPI nanofibrils pretreated by ultrasound were more fragmented and shorter after simulating gastrointestinal digestion. This study would expand the application of food-grade protein nanofibrils in the food industry.     

Dual-frequency multi-angle ultrasonic processing technology and its real-time monitoring on physicochemical properties of raw soymilk and soybean protein

To improve the soybean protein content (SPC), flavor and quality of soymilk, the effects of dual-frequency ultrasound at different angles (40 + 20 kHz 0°, 40 + 20 kHz 30°, 40 + 20 kHz 45°) on physicochemical properties and soybean protein (SP) structure of raw soymilk were mainly studied and compared with the conventional single-frequency (40 kHz, 20 kHz) ultrasound. Furthermore, the intensity of the ultrasonic field in real-time was monitored via the oscilloscope and spectrum analyzer. The results showed that 40 + 20 kHz 45° treatment significantly increased SPC. The ultrasonic field intensity of 40 + 20 kHz 0° treatment was the largest (8.727 × 10⁴ W/m²) and its distribution was the most uniform. The emulsifying stability of SP reached the peak value (233.80 min), and SP also had the largest particle size and excellent thermal stability. The protein solubility of 40 + 20 kHz 30° treatment attained peak value of 87.09%. 20 kHz treatment significantly affected the flavor of okara. The whiteness and brightness of raw soymilk treated with 40 kHz were the highest and the system was stable. Hence, the action mode of ultrasonic technology can be deeply explored and the feasibility for improving the quality of soymilk can be achieved.     

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.     

Acid-induced gelation behavior of soybean protein isolate with high intensity ultrasonic pre-treatments

High intensity ultrasonic (HUS, 20 k Hz, 400 W) pre-treatments of soybean protein isolate (SPI) improved the water holding capacity (WHC), gel strength and gel firmness (final elastic moduli) of glucono-δ-lactone induced SPI gels (GISG). Sonication time (0, 5, 20, and 40 min) had a significant effect on the above three properties. 20 min HUS-GISG had the highest WHC (95.53 ± 0.25%), gel strength (60.90 ± 2.87 g) and gel firmness (96340 Pa), compared with other samples. Moreover, SH groups and non-covalent interactions of GISG also changed after HUS pre-treatments. The HUS GISG had denser and more uniform microstructures than the untreated GISG. Rheological investments showed that the cooling step (reduce the temperature from 95 to 25 °C at a speed of 2 °C/min) was more important for the HUS GISG network formation while the heat preservation step (keep temperature at 95 for 20 min) was more important for the untreated GISG. HUS reduced the particle size of SPI and Pearson correlation test showed that the particle size of SPI dispersions was negatively correlated with WHC, gel strength and gel firmness.     

Improving the gel properties of salted egg white/cooked soybean protein isolate composite gels by ultrasound treatment: Study on the gelling properties and structure

In this study, the effects of ultrasound treatment on the texture, physicochemical properties and protein structure of composite gels prepared by salted egg white (SEW) and cooked soybean protein isolate (CSPI) at different ratios were investigated. With the increased SEW addition, the ζ-potential absolute values, soluble protein content, surface hydrophobicity and swelling ratio of composite gels showed overall declining trends (P < 0.05), while the free sulfhydryl (SH) contents and hardness of exhibited overall increasing trends (P < 0.05). Microstructural results revealed that composite gels exhibited denser structure with the increased SEW addition. After ultrasound treatment, the particle size of composite protein solutions significantly decreased (P < 0.05), and the free SH contents of ultrasound-treated composite gels were lower than that of untreated composite gels. Moreover, ultrasound treatment enhanced the hardness of composite gels, and promoted the conversion of free water into non-flowable water. However, when ultrasonic power exceeded 150 W, the hardness of composite gels could not be further enhanced. FTIR results indicated that ultrasound treatment facilitated the composite protein aggregates to form a more stable gel structure. The improvement of ultrasound treatment on the properties of composite gels was mainly by promoting the dissociation of protein aggregates, and the dissociated protein particles further interacted to form denser aggregates through disulfide bond, thus facilitating the crosslinking and reaggregation of protein aggregates to form denser gel structure. Overall, ultrasound treatment is an effective approach to improve the properties of SEW-CSPI composite gels, which can improve the potential utilization of SEW and SPI in food processing.     

Effect mechanism of ultrasound pretreatment on fibrillation Kinetics,physicochemical properties and structure characteristics of soy protein isolate nanofibrils

Self-assembly of soy proteins into nanofibrils is gradually considered as an effective method to improve their technical and functional properties. Ultrasound is a non-thermal, non-toxic and environmentally friendly technology that can modulate the formation of protein nanofibrils through controlled structural modification. In this research, the effect of ultrasound pretreatment on soy protein isolate nanofibrils (SPIN) was evaluated by fibrillation kinetics, physicochemical properties and structure characteristics. The results showed that the optimum ultrasound condition (20% amplitude, 15 min, 5 s on-time and 5 s off-time) could increase the formation rate of SPIN by 38.66%. Ultrasound reduced the average particle size of SPIN from 191.90 ± 5.40 nm to 151.83 ± 3.27 nm. Ultrasound could increase the surface hydrophobicity to 1547.67 in the initial stage of nanofibrils formation, and extend the duration of surface hydrophobicity increased, indicating ultrasound could expose more binding sites, creating more beneficial conditions for nanofibrils formation. Ultrasound could change the secondary and tertiary structure of SPIN. The reduction of α-helix content of ultrasound-pretreated soy protein isolate nanofibrils (USPIN) was 12.1% (versus 5.3% for SPIN) and the increase of β-sheet content was 5.9% (versus 3.5% for SPIN) during fibrillation. Ultrasound could accelerate the formation of SPIN by promoting the unfolding of SPI, exposure of hydrophobic groups and formation of β-sheets. Microscopic images revealed that USPIN generated a curlier and looser shape. And ultrasound reduced the zeta potential, free sulfhydryl groups content and viscosity of SPIN. SDS-PAGE results showed that ultrasound could promote the conversion of SPI into low molecular weight peptides, providing building blocks for the nanofibrils formation. The results indicated that ultrasound pretreatment could be a promising technology to accelerate SPIN formation and promote its application in food industry, but further research is needed for the improvement of the functional properties of SPIN.     

Preparation of allicin-whey protein isolate conjugates: Allicin extraction by water,conjugates’ ultrasound-assisted binding and its stability,solubility and emulsibility analysis

The instability of allicin makes it easily decomposed into various organic sulfur compounds, resulting in significant decrease in biological activity. In this study, allicin was firstly extracted with water, then bound with whey protein isolates (WPI) which were pretreated by ultrasound to form conjugates, and the stability, water solubility and emulsibility of conjugates were as well investigated. The research results showed that there were no significant differences in the extraction yields of allicin from water, 40% and 80% ethanol. Appropriate frequency (20/40 kHz), power (50 W/L) and time (20 min) of ultrasonic pretreatments significantly increased (P < 0.05) the sulfhydryl groups content of WPI by 35.05% over control, causing improvement in binding ability of protein to allicin. The binding process of allicin-WPI displayed good fit with Elovich kinetic model (R² = 0.9781). The mass retention rate of the conjugates (in 60% combination rate) with ultrasonic pretreating kept at 95.97% after 14 days of storage at 25 °C, whereas allicin’s mass retention rate was only 61.79% at same storage condition. The water solubility of the prepared conjugates was significantly higher than allicin. And with optimal condition ultrasonic pretreatment of WPI, the conjugates showed the highest emulsifying capacity and emulsion stability (49.56 m²/g, 10.06 min). In conclusion, the ultrasonically pretreated allicin-WPI conjugates exhibited better stability, water solubility and emulsifying properties compared to allicin, this expands the application field of allicin.     

Influence of ultrasound-assisted ionic liquid pretreatments on the functional properties of soy protein hydrolysates

In this work, the effect of dual-frequency ultrasound-assisted ionic liquids (ILs) pretreatment on the functional properties of soy protein isolate (SPI) hydrolysates was investigated. The degree of hydrolysis (DH) of SPI pretreated by ultrasound and [BMIM][PF₆] increased by 12.53% as compared to control (P < 0.05). More peptides with low molecular weight were obtained, providing support for the changes in DH. The trichloroacetic acid-nitrogen soluble index presented an increase, suggesting a better protein hydrolysate property. The increase in the calcium-binding activity showed the ultrasound-assisted ILs pretreatment could potentially improve bone health. The foaming capacity and stability of SPI hydrolysates pretreated by ultrasound-assisted [BMIM][PF₆] always increased remarkably as compared to ultrasound-assisted [BDMIM][Cl] pretreatment. However, the synergistic effect of ultrasound-assisted [BMIM][PF₆] on the emulsifying activity and antioxidant activities (DPPH and hydroxyl radical scavenging activity) was not as ideal as ultrasound-assisted [BDMIM][Cl] pretreatment, which may be affected by the structure of peptide. In conclusion, these results indicated the combination of dual-frequency ultrasound and ionic liquids would be a promising method to improve the functional properties of SPI hydrolysates and broaden the application scope of compound modification in proteolysis industry.     

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.     

High-power sonication of soy proteins: Hydroxyl radicals and their effects on protein structure

High-power sonication (HPS) is shown to alter protein structure, thus, its functionality, via intermolecular interactions. This study evaluated the effects of HPS on molecular structure of soy proteins in aqueous medium. Free radicals generated during HPS were quantitated using the 5,5-dimethyl-l-pyrrolin N-oxide (DMPO) spin trap method. Electron paramagnetic resonance (EPR) was used to identify them as mostly hydroxyl radicals. The minimum saturation concentration of spin trap solution was determined to be 500 mM of DMPO in water, when exposed to 5 W/cm³ ultrasound power density (PD) for 10 min; subsequently, this concentration was used for quantitating radicals generated in protein samples. Five aqueous soy protein systems, namely, 5% soy protein isolate (SPI), 5% SPI without isoflavonoids (NO-ISO SPI), subunit solutions 1% glycinin (11S) and 1% β conglycinin (7S), and 10% soy flakes (w/v), were sonicated at 2.5 and 5 W/cm³ PDs. Only adducts of hydroxyl radicals (DMPO-OH) were detected in all of these aqueous systems. The highest concentration (3.68 µM) of DMPO-OH adduct was measured in 11S subunit solution at 5 W/cm³, whereas, the lowest (0.67 µM) was in soy flakes solution at 2.5 W/cm³. PD 5 W/cm³ generated higher concentration of radicals in 7S subunit solution, NO-ISO SPI, and soy flakes protein, compared to sonication at PD 2.5 W/cm³. No change in the protein electrophoretic patterns were observed due to HPS. However, some changes due to HPS were observed in the estimated secondary and tertiary structures, and the contents of free sulfhydryl groups and disulfide bonds in proteins.     

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.     

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.