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.     

Fabrication of emulsions prepared by rice bran protein hydrolysate and ferulic acid covalent conjugate: Focus on ultrasonic emulsification

The aim of the paper was to investigate the effect of ultrasonic emulsification treatment on the fabrication mechanism and stability of the emulsion. The covalent conjugate made with rice bran protein hydrolysate (RBPH) and ferulic acid (FA) was used as the emulsifier. The effects of high intensity ultrasound (HIU) power with different level (0 W, 150 W, 300 W, 450 W and 600 W) on the stability of emulsion were evaluated. The results showed that ultrasonic emulsification can significantly improve the stability of the emulsions (p < 0.05). The emulsion gained better stability and emulsifying property at 300 W. It was able to fabricate emulsion with smaller particle size, more uniform distribution and higher interfacial protein content. It was confirmed by fluorescent microscopy and cryo-scanning electron microscopy (cryo-SEM) furtherly. And it was also proved that the emulsion treated by proper HIU treatment at 300 W had better storage stability. Excessive HIU treatment (450 W, 600 W) had negative effects on the stability of emulsion. The stability of emulsion (300 W) against different environmental stresses was further explored, which established a theoretical basis for the industrial application of emulsion in food 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-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.     

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 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.     

Physicochemical characterization of black seed oil-milk emulsions through ultrasonication

The ultrasonic formation of stable emulsions of a bioactive material, black seed oil, in skim milk was investigated. The incorporation of 7% of black seed oil in pasteurised homogenized skim milk (PHSM) using 20 kHz high intensity ultrasound was successfully achieved. The effect of sonication time and acoustic power on the emulsion stability was studied. A minimum process time of 8 min at an applied acoustic power of 100 W was sufficient to produce emulsion droplets stable for at least 8 days upon storage at 4 ± 2 °C, which was confirmed through creaming stability, particle size, rheology and color analysis. Partially denatured whey proteins may provide stability to the emulsion droplets and in addition to the cavitation effects of ultrasound are responsible for the production of smaller sized emulsion droplets.     

Study on the emulsification and oxidative stability of ovalbumin-pectin-pumpkin seed oil emulsions using ovalbumin solution prepared by ultrasound

Pumpkin seed oil (PSO), which is a valuable compound with high nutritional value used for the prevention of various chronic diseases, is prone to oxidation. In this work, small and uniform (su) ovalbumin (OVA) and pectin (PEC) were used to stabilize PSO in the form of an emulsion. The results showed that suOVA-PEC-PSO emulsion with a droplet size of 9.82 ± 0.05 μm was successfully self-assembled from PSO, PEC, and suOVA solution (with a droplet size of 230.13 ± 14.10 nm) treated with 300 W ultrasound, owing to the formation of a more stable interfacial film on the surface of droplets. The interfacial, rheological, emulsifying, and antioxidant properties of the suOVA-PES-PSO emulsions were excellent, owing to the synergistic effects between PEC and suOVA solution. Moreover, the physical stability of the suOVA-PEC-PSO emulsions to salt stress, a freeze-thaw cycle, and heat treatment was also increased and the oxidation of linolenic acid was notably delayed. These results have extended the food-related applications of OVA and PSO, and provide a promising foundation for further exploration of the self-assembly of composite emulsions by small and uniform proteins.     

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.     

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.     

Emulsions stabilised by casein and hyaluronic acid: Effects of high intensity ultrasound on the stability and vitamin E digestive characteristics

This study aimed to prepare an emulsion stabilised by an ultrasound-treated casein (CAS)-hyaluronic acid (HA) complex and to protect vitamin E during in vitro digestion. It was found that high-intensity ultrasound (HIU) treatment significantly changed the hydrogen bonding, electrostatic interaction and hydrophobic interaction between CAS and HA, reduced the particle size of the CAS-HA complex, increased the intermolecular electrostatic repulsion, and thus significantly improved the emulsifying properties of the CAS-HA complex. Meanwhile, the creaming index (CI) and confocal laser scanning microscopy images showed that the stability of the CAS-HA-stabilised emulsion was the best when treated at 150 W for 10 min, which could be attributed to the enhanced adsorption capacity of the CAS-HA complex at the oil–water interface and the viscosity of the formed emulsion. In vitro digestion experiments revealed that the emulsion stabilised by the ultrasound-treated CAS-HA complex had a good protective effect on vitamin E. This study is significant for the development of emulsions for the delivery of lipophilic nutrients.     

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.     

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

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

Effect of 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.     

Laccase cross-linking of sonicated α-Lactalbumin improves physical and oxidative stability of CLA oil in water emulsion

α-lactalbumin was modified by ultrasound (US, 20 kHz, 43 ± 3.4 W/cm⁻²) pre-treatments (0, 15, 30 and 60 min) and laccase cross-linking of sonicated α-lactalbumin was used to evaluate the physical and oxidative stability of conjugated linoleic acid (CLA) emulsions. The emulsions prepared with laccase cross-linking US-α-lactalbumin (α-lactalbumin treated with US pre-treatment) and US-α-lactalbumin were scrutinized for oxidative and physical stability at room temperature for two weeks of storage. Laccase cross-linking US-α-lactalbumin (Lac-US-α-lactalbumin) revealed improved physical stability in comparison with US-α-lactalbumin, specified by droplet size, structural morphology, adsorbed protein, emulsifying properties and creaming index. SDS-PAGE analysis showed that there was formation of polymers in Lac-US-α-lactalbumin emulsion. Surface hydrophobicity of Lac-US-α-lactalbumin was higher than that of US-α-lactalbumin, and gradually enhanced with the increase of ultrasound time. More importantly, the measurements of peroxide values and conjugated dienes were used to study the oxidative stability of the CLA emulsions. The Lac-US-α-lactalbumin emulsion proved to be reducing the synthesis of fatty acid hydroperoxides and less conjugated dienes compared to the native and US-α-lactalbumin emulsions. This study revealed that the combination of US pre-treatment and laccase cross-linking might be an effective technique for the modification of CLA emulsions.     

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.     

Structural characteristics and emulsifying properties of myofibrillar protein-dextran conjugates induced by ultrasound Maillard reaction

In this study, we investigated the effect of the ultrasound-assisted Maillard reaction on the structural and emulsifying properties of myofibrillar protein (MP) and dextran (DX) conjugates with different molecular weights (40, 70 and 150 kDa). Compared with classical heating, mild and moderate ultrasound-assisted methods (100–200 W) could accelerate the later stage of the Maillard reaction, which increased the degree of graft (DG) and the content of advanced Maillard reaction products (MPRs). Structural analysis revealed conjugates obtained by Maillard reaction induced the loss of ordered secondary structures (α-helix, β-sheets) and red-shift of maximum emission wavelength of intrinsic fluorescence spectrum. The conjugate containing 40 kDa DX exhibited higher extent of Maillard reaction compared to those containing 70 kDa and 150 kDa DX under various treating methods. Moreover, the ultrasound-assisted Maillard reaction could effectively improve the emulsifying behaviors. 100 W ultrasound-induced conjugates grafted by 70 kDa DX produced the smallest emulsion size with optimum storage stability. Confocal laser scanning microscopy and analytical centrifugal analyzer further confirmed MP grafted by 70 kDa DX with the assistance of 100 W ultrasound field could produce the smallest and most homogeneous MP-base emulsion with no flocculation. Our study demonstrated that mild ultrasound treatment resulted in well-controlled Maillard reaction, and the related glycoconjugate grafted with 70 kDa DX showed the greatest improvements in emulsifying ability and stability. These findings provided a theoretical foundation for the development of emulsion-based foods with excellent characteristics.     

Structural and physicochemical properties of lotus seed starch nanoparticles prepared using ultrasonic-assisted enzymatic hydrolysis

Lotus seed starch nanoparticles were prepared by ultrasonic (ultrasonic power: 200 W, 600 W, 1000 W; time: 5 min, 15 min, 25 min; liquid ratio (starch: buffer solution): 1%, 3%, 5%) assisted enzymatic hydrolysis (LS-SNPs represent lotus seed starch nanoparticles prepared by enzymatic hydrolysis and U-LS-SNPs represent lotus seed starch nanoparticles prepared by high pressure homogenization-assisted enzymatic hydrolysis). The structure and physicochemical properties of U-LS-SNPs were studied by laser particle size analysis, scanning electron microscope, X-ray diffraction, Raman spectroscopy, nuclear magnetic resonance and gel permeation chromatography system. The results of scanning electron microscopy showed that the surface of U-LS-SNPs was cracked and uneven after ultrasonic-assisted enzymolysis, and there was no significant difference from LS-SNPs. The results of particle size analysis and gel permeation chromatography showed that the particle size of U-LS-SNPs (except 5% treatment group) was smaller than that of LS-SNPs. With the increase of ultrasonic power and time, the weight average molecular gradually decreased. The results of X-ray diffraction and Raman spectroscopy showed that ultrasonic waves first acted on the amorphous region of starch granules. With the increase of ultrasonic power and time, the relative crystallinity of U-LS-SNPs increased first and then decreased. The group (600 W, 15 min, 3%) had the highest relative crystallinity. The results of nuclear magnetic resonance studies showed that the hydrogen bond and double helix structure of starch were destroyed by ultrasound, and the double helix structure strength of U-LS-SNPs was weakened compared with LS-SNPs. In summary, U-LS-SNPs with the small-sized and the highest crystallinity can be prepared under the conditions of ultrasonic power of 600 W, time of 15 min and material-liquid ratio of 3%.     

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

The denaturation and lower solubility of commercial potato proteins generally limited their industrial application. Effects of high-intensity ultrasound (HIU) (200, 400, and 600 W) and treatment time (10, 20, and 30 min) on the physicochemical and functional properties of insoluble potato protein isolates (ISPP) were investigated. The results revealed that HIU treatment induced the unfolding and breakdown of macromolecular aggregates of ISPP, resulting in the exposure of hydrophobic and R–SH groups, and reduction of the particle size. These active groups contributed to the formation of a dense and uniform gel network of ISPP gel and insoluble potato proteins/egg white protein (ISPP/EWP) hybrid gel. Furthermore, the increase of solubility and surface hydrophobicity and the decrease of particle size improved the emulsifying property of ISPP. However, excessive HIU treatment reduced the emulsification and gelling properties of the ISPP. Meanwhile, HIU treatment changes the secondary structure of ISPP. It could be speculated that the formation of a stable secondary structure of ISPP initiated by cavitation and shearing effect might play a dominant role on gel strengthens and firmness. Meanwhile, the decrease in relative content of β-turn had a positive effect on the formation of small particle to improve emulsifying property of ISPP.     

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.