Ultrasound-assisted alkaline proteinase extraction enhances the yield of pecan protein and modifies its functional properties

To enhance the extraction yield of pecan protein and modify its functional properties, this study investigated whether both ultrasound and enzyme have a synergistic impact on the extraction of pecan (Carya illinoinensis (Wangenh.) K. Koch) protein. The highest protein extraction rate (25.51%) was obtained under the conditions of 1415.43 W^.cm⁻², 15 min, pH 10.0, 50 °C, and 1% (w/w) alkaline proteinase. Owing to its high shear, mechanical energy and cavitation, the ultrasound process increased the solubility of the substrate making it readily accessible to the enzyme, thereby accelerating the chemical reaction and improving the yield of the protein. The optimized ultrasound-assisted enzymatic method (400 W, 20 kHz, 5 s/3s) effectively changed the secondary and tertiary structure of the pecan protein. The results of surface hydrophobicity, intrinsic fluorescence spectra, sulfhydryl content and scanning electron microscopy all indicated the unfolding of protein and exposure of hydrophobic groups and sulfhydryl groups. Moreover, the protein obtained by this method showed higher solubility (70.77%), higher emulsifying activity (120.56 m²/g), smaller particle size (326.7 nm), and better dispersion (0.305) than single ultrasound and non-ultrasound methods (p < 0.05). To conclude, ultrasound-assisted enzymatic method could be an appropriate technique to improve the yield and quality of the pecan protein. The study also provides a theoretical basis for the application of pecan protein in food processing.     

Effects of multi-frequency ultrasound pretreatment under low power density on the enzymolysis and the structure characterization of defatted wheat germ protein

The effects of ultrasonic frequency mode, power density, pretreatment time and other parameters under low power density on the degree of hydrolysis (DH) of defatted wheat germ protein (DWGP) and angiotensin-I-converting enzyme (ACE) inhibitory activity of DWGP hydrolysate were studied in this research. Ultraviolet–visible (UV–Vis) spectra, free sulfhydryl (SH), disulfide bond (SS), surface hydrophobicity and hydrophobic protein content of ultrasound-pretreated protein and hydrophobic amino acid (HAA) content of alcalase-hydrolysate of DWGP were measured under optimized ultrasonic condition. The ultrasonic frequency mode with dual-fixed frequency combination of 28/40 kHz showed higher ACE inhibitory activity of DWGP hydrolysate compared with that of other ultrasound frequency modes and all the ultrasonic frequency combinations involving in 28 kHz showed higher ACE inhibitory activity. Under the dual-fixed frequency ultrasound mode of 28/40 kHz, ultrasonic power density of 60 W/L, pretreatment time of 70 min, temperature of 60°C and substrate concentration of 60 g/L, the ACE inhibitory activity of DWGP hydrolysate was the highest with its value of 74.75% (increased by 62.30% compared to control). However, all the ultrasonic pretreatment did not increase the DH of DWGP significantly (p > 0.05). The changes in UV–Vis spectra, SH and SS groups, surface hydrophobicity and hydrophobic protein content indicated that the structure of DWGP unfolded after ultrasound pretreatment. The HAA content of hydrolysate from the pretreated DWGP increased significantly (p < 0.05). The results proved that ultrasound pretreatment loosed the protein structure and exposed more HAA residues of protein to be attacked easily by alcalase. This resulted in the increase in the HAA content which related to the ACE inhibitory activity.     

Impacts of sonication and high hydrostatic pressure on the structural and physicochemical properties of quinoa protein isolate dispersions at acidic,neutral and alkaline pHs

Herein, 1 wt% quinoa protein isolate (QPI) was exposed to sonication using a 20 kHz ultrasonicator equipped with a 6 mm horn (14.4 W, 10 mL, up to 15 min) or high hydrostatic pressure (HHP, up to 600 MPa, 15 min) treatments at pH 5, pH 7, and pH 9. The changes to physicochemical properties were probed by SDS-PAGE, FTIR, free sulfhydryl group (SH), surface hydrophobicity (H₀), particle size and solubility. As revealed by SDS-PAGE, substantial amounts of 11S globulin participated in the formations of aggregates via SS bond under HHP, particularly at pH 7 and pH 9. However, protein profiles of QPI were not significantly affected by the sonication. Free SH groups and surface hydrophobicity were increased after the sonication treatment indicating protein unfolding and exposure of the embedded SH and/or hydrophobic groups. An opposite trend was observed in HHP treated samples, implying aggregation and reassociation of structures under HHP. HHP and sonication treatments induced a decrease in ordered secondary structures (random coil and β-turn) accompanied with an increase in disordered secondary structures (α-helix and β-sheet) as probed by FTIR. Finally, the sonication treatment induced a significant improvement in the solubility (up to ∼3 folds at pH 7 and ∼2.6 folds at pH 9) and a reduction in particle sizes (up to ∼3 folds at pH 7 and ∼4.4 folds at pH 9). However, HHP treatment (600 MPa) only slightly increased the solubility (∼1.6 folds at pH 7 and ∼1.2 folds at pH 9) and decreased the particle size (∼1.3 folds at pH 7 and ∼1.2 folds at pH 9). This study provides a direct comparison of the impacts of sonication and HHP treatment on QPI, which will enable to choose the appropriate processing methods to achieve tailored properties of QPI.     

Effects of ultrasound pretreatment with different frequencies and working modes on the enzymolysis and the structure characterization of rice protein

The effects of ultrasound pretreatment with different frequencies and working modes, including mono-frequency ultrasound (MFU), dual-frequency ultrasound (DFU) and tri-frequency ultrasound (TFU), on the degree of hydrolysis (DH) of rice protein (RP) and angiotensin-I-converting enzyme (ACE) inhibitory activity of RP hydrolysate were investigated. Ultraviolet–visible (UV) spectroscopy, fourier transform infrared (FTIR) spectroscopy, surface hydrophobicity and scanning electron microscopy (SEM) of RP pretreated with ultrasound were measured. The results showed that ultrasound pretreatment did not increase DH of RP significantly (p > 0.05). However, all the ultrasound pretreatment increased the ACE inhibitory activity of RP hydrolysate significantly (p < 0.05). The MFU of 20 kHz showed higher ACE inhibitory activity compared to that of other MFU. The ACE inhibitory activity of sequential DFU was higher than that of simultaneous with the same frequency combination. Sequential TFU of 20/35/50 kHz produced the highest increase in ACE inhibitory activity in contrast with other ultrasound frequencies and working modes. All the results under ultrasound pretreatment showed that ultrasound frequencies and working modes were of great effect on the ACE inhibitory activity of RP. The changes in UV–Vis spectra and surface hydrophobicity indicated the unfolding of protein and exposure of hydrophobic groups by ultrasound. The FTIR analysis showed that all the ultrasound pretreatment with different frequencies and working modes decreased α-helix, β-turn content and increased β-sheet, random coil content of RP. The SEM results indicated that ultrasound pretreatment resulted in the deformation of RP. In conclusion, the frequency selection of ultrasound pretreatment of RP is essential for the preparation of ACE inhibitory peptide.     

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

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

Effects of ultrasonic-assisted pH shift treatment on physicochemical properties of electrospinning nanofibers made from rapeseed protein isolates

Electrospinning nanofibers (NFs) made from natural proteins have drawn increasing attention recently. Rapeseed meal is a by-product that rich in protein but not fully utilized due to poor properties. Therefore, modification of rapeseed protein isolates (RPI) is necessary to expand applications. In this study, pH shift alone or ultrasonic-assisted pH shift treatment was adopted, the solubility of RPI, along with the conductivity and viscosity of the electrospinning solution were detected. Moreover, the microstructure and functional characteristics of the electrospinning NFs, as well as the antibacterial activity of clove essential oil loaded-NFs were investigated. The tested parameters were remarkably improved after different treatments compared with the control, and synergistic effects were observed, especially under alkaline conditions. Hence, pH_12.5 + US showed the maximum value of solubility, conductivity, and viscosity, which was more than 7-fold, 3-fold, and almost 1-fold higher than the control respectively. Additionally, SEM and AFM images showed a finer and smoother surface of NFs after treatments, and the finest diameter of 216.7 nm was obtained after pH_12.5 + US treatment in comparison with 450.0 nm in control. FTIR spectroscopy of NFs demonstrated spatial structure changes of RPI, and improved thermal stability and mechanical strength of NFs were achieved after different treatments. Furthermore, an inhibition zone with a diameter of 22.8 mm was observed from the composite NFs. This study indicated the effectiveness of ultrasonic-assisted pH shift treatment on the physicochemical properties improvement and functional enhancement of NFs made from RPI, as well as the potential antibacterial application of the composite NFs in the future.     

Structural and physicochemical characterization of modified starch from arrowhead tuber (Sagittaria sagittifolia L.) using tri-frequency power ultrasound

Sagittaria sagittifolia L. is a well-known plant, belongs to the Alismataceae family. Sonication can improve the functional properties of starch; hence, the aim of this study was to develop ultrasonically modified arrowhead starch (UMAS) using a sophisticated and eco-friendly tri-frequency power ultrasound (20/40/60 kHz) method at 300, 600, and 900 W for 15 and 30 min. Significant (p < 0.05) increases in swelling power, solubility, and water and oil holding capacities were achieved. FTIR spectroscopy corroborated the ordered, amorphous, and hydrated crystals of the sonicated samples. Increases in sonication frequency and power led to significant (p < 0.05) increases in onset gelatinization temperatures. Scanning electron microscopic analysis of sonicated samples showed superficial cracks and roughness on starch granules appeared in a sonication power-dependent manner compared with that of untreated sample. Overall, the ultrasonically-treated samples showed improved physicochemical properties, which could be useful for industrial applications.     

Effects of power ultrasound on oxidation and structure of beef proteins during curing processing

The aim of this study was to evaluate the effects of power ultrasound intensity (PUS, 2.39, 6.23, 11.32 and 20.96 W cm⁻²) and treatment time (30, 60, 90 and 120 min) on the oxidation and structure of beef proteins during the brining procedure with 6% NaCl concentration. The investigation was conducted with an ultrasonic generator with the frequency of 20 kHz and fresh beef at 48 h after slaughter. Analysis of TBARS (Thiobarbituric acid reactive substances) contents showed that PUS treatment significantly increased the extent of lipid oxidation compared to static brining (P < 0.05). As indicators of protein oxidation, the carbonyl contents were significantly affected by PUS (P < 0.05). SDS–PAGE analysis showed that PUS treatment increased protein aggregation through disulfide cross-linking, indicated by the decreasing content of total sulfhydryl groups which would contribute to protein oxidation. In addition, changes in protein structure after PUS treatment are suggested by the increases in free sulfhydryl residues and protein surface hydrophobicity. Fourier transformed infrared spectroscopy (FTIR) provided further information about the changes in protein secondary structures with increases in β-sheet and decreases in α-helix contents after PUS processing. These results indicate that PUS leads to changes in structures and oxidation of beef proteins caused by mechanical effects of cavitation and the resultant generation of free radicals.     

Ultrasound driven conformational and physicochemical changes of soy protein hydrolysates

The effect of ultrasound on the conformational and physicochemical properties of soy protein isolate hydrolysates (SPHs) was investigated. SPHs were prepared at hydrolysis times of 20 min, 60 min, and 180 min, then treated with ultrasound for 10 min, 20 min, and 30 min at a frequency of 20 kHz and output powers of 150 W and 450 W. The structural properties and antioxidant capacities of the aqueous layer of SPHs (ASPHs) after sonication were evaluated by Fourier-transform infrared spectroscopy (FTIR), intrinsic fluorescence, DPPH radical scavenging activity assays, and microscopy observations. Results obtained showed that ultrasound treatment significantly disrupted the peptide aggregates formed during protein hydrolysis. The protein solubility was significantly increased after sonication (by up to 18.33%), as did the percentage of proteins with MW < 1 kDa in ASPHs. The antioxidant capacity of ASPHs also increased, as measured by DPPH assay. FTIR analysis of ASPHs indicated that the protein secondary structures were different, with an increase in β-sheet and a decrease in α-helix and β-turn. Furthermore, the changes in fluorescence spectra of ASPHs showed the transition of protein tertiary structure with a greater exposure of Trp residues in the side chains. Scanning electron microscope (SEM) and atomic force microscope (AFM) observations of the morphological structure of ASPHs further confirmed the significant effect of sonication on disrupting peptide aggregates. In conclusion, ultrasound can be used as an efficient treatment to promote the solubility of protein hydrolysates.     

Effects of ultrasonic and graft treatments on grafting degree,structure, functionality,and digestibility of rapeseed protein isolate-dextran conjugates

Rapeseed protein isolate (RPI) and dextran conjugates were prepared by traditional and ultrasonic assisted wet-heating. The effects on the grafting degree (GD), structure, functionality, and digestibility of conjugates were studied. Ultrasonic frequency, temperature, and time all significantly affected the GD. Under the optimum conditions (temperature of 90 °C and time of 60 min), compared to traditional wet-heating, ultrasonic treatment at 28 kHz significantly increased the GD by 2.12 times. Compared to RPI, surface hydrophobicities of conjugates were significantly decreased by graft and ultrasonic treatments. Sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS-PAGE) and amino acid composition results confirmed that traditional graft reaction involved cysteine (Cys) and lysine (Lys) whereas the ultrasonic assisted one involved only Cys. Both were from the 12S globulin subunit and cruciferin. Fourier transform infrared spectrum (FT-IR) and circular dichroism (CD) results showed that graft treatment significantly changed secondary structure and ultrasonic treatment had the greatest impact on the decrease in the β-sheet (19.1%) and the increase in the random coil (49.6%). Graft and ultrasonic treatments both made surface structure looser and more porous. The two treatments also caused molecular weight to become bigger, and ultrasonic treatment had the greatest effect on the increase (68.2%) in 110–20.5 kDa. Structural modifications of RPI by grafting to dextran caused improvements of solubility (at pH 5–6), emulsifying activity (at pH 4–10), emulsion stability (at pH 4–5 and 9–10), and thermal stability (at temperature 90–100 °C). The digestibility of conjugates was decreased by graft and ultrasonic treatments and the conjugates were mainly digested in the intestinal phase. The ultrasonic assisted wet-heating was an efficient and safe method for producing RPI-dextran conjugates and improving the utilization value of rapeseed meal.     

Modifying the physicochemical properties of pea protein by pH-shifting and ultrasound combined treatments

The effect of a pH-shifting and ultrasound combined process on the functional properties and structure of pea protein isolate (PPI) was investigated. PPI dispersions were adjusted to pH 2, 4, 10, or 12, treated by power ultrasound for 5 min, and incubated for 1 h before the sample pH was brought back to neutral. After treatment, water solubility, protein aggregate size, solution turbidity, surface hydrophobicity (Ho), free sulfhydryl content (SH), and sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) of the soluble PPI were determined. pH-shifting at pH 12 and ultrasound combined treatment (pH12-US) significantly improved protein properties, while property modification of the samples treated under acidic conditions was less pronounced. The pH12-US treated PPI had a solubility seven times higher than the control, reaching an average particle size of 45.2 nm. In addition, the pH12-US treated PPI significantly improved Ho due to disulfide bonds disruption, and produced more protein sub-units than other treatments. The soluble PPI obtained through this process may be a promising emulsifier for the enrichment of fat-soluble nutrients in foods.     

Effects of dual-frequency slit ultrasound on the enzymolysis of high-concentration hydrolyzed feather meal: Biological activities and structural characteristics of hydrolysates

Ultrasound-assisted enzymolysis has been applied to improve conventional enzymolysis, while there are rare reports on the application of ultrasound to high-concentration feather protein enzymolysis. Therefore, the feasibility of dual-frequency slit ultrasound (DFSU) for enzymolysis of high-concentration hydrolyzed feather meal (HFM), as well as the biological activities and structural characteristics of hydrolysates were investigated. The single-factor test was used to optimize the ultrasonic processing parameters: substrate concentration, frequency mode, intermittent ratio, power density, and time. The results showed that protein recovery rate and conversion rate increased by 6.08% and 18.63% under the optimal conditions (200 g/L, 28/80 kHz, 5:2 s/s, 600 W/L, and 3 h) compared with conventional enzymolysis, respectively. The macromolecular proteins in hydrolysates were converted into micromolecular peptides (< 500 Da) when treated by DFSU, and antioxidant activity and angiotensin-I-converting enzyme (ACE) inhibitory activity of hydrolysates were increased. Scanning electron microscopy (SEM) and atomic force microscopy (AFM) images illustrated the microstructure changes of feather protein particles in the ultrasound-assisted enzymatic hydrolysates of HFM (UEH), including more porous, smaller, and more uniform. Additionally, the conformation of protein molecules was significantly affected (P < 0.05), including the increase in free sulfhydryl (SH), the decrease in disulfide bond (SS) and surface hydrophobicity (H₀). Fourier transform infrared (FTIR) spectra analysis further showed that the secondary structure of feather proteins was modified with a reduction in α-helix, β-turn, and β-sheet, while an increase in random coil content was observed. These results indicated that DFSU could be a promising method to enhance high-concentration HFM for preparing peptide-rich hydrolysates with high antioxidant activity and ACE inhibitory activity.     

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.     

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

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

Multi-mode S-type ultrasound-assisted protein extraction from walnut dregs and in situ real-time process monitoring

This study aimed to investigate the impact of multi-mode S-type ultrasound treatment on the protein extraction level of walnut dregs. The structural properties of the walnut protein (WP) were characterized, and the correlation between protein structure and extraction level was analyzed. The in situ real-time monitoring model for the ultrasound-assisted WP extraction process was established by a miniature fiber near-infrared (NIR) spectrometer. Results showed that the protein yield, purity, and comprehensive extraction index (CEI) of extracted WP were 71.07 %, 72.69 %, and 71.72, respectively, under optimal conditions (dual-frequency 20/28 kHz, ultrasonic treatment duration 30 min, and ultrasound power density 120 W/L). The secondary structure of extracted WP displayed that the proportion of α-helix and β-sheet reduced, while the contents of β-turn and random coil increased after ultrasonic treatment. Besides, sonication decreased the disulfide bond content and increased free sulfhydryl (-SH) and surface hydrophobicity compared to the control. The microstructures of WP confirmed that appropriate sonication could unfold the protein aggregates and reduce the particle size. The extraction level of WP is positively correlated with the -SH content (p < 0.01). The quantitative prediction model of Si-PLS for -SH content in the ultrasound-assisted WP extraction process was established and performed a good correction and prediction performance (Rc = 0.9736; RMSECV = 0.446 μmol/L; Rp = 0.9342; RMSEP = 0.807 μmol/L). This study exploited a high-efficiency way for the WP extraction industry, and provided theoretical support for the development of the intelligent system in industrial protein extraction process.     

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.     

Thermosonication-induced structural changes and solution properties of mung bean protein

Mung bean protein is considered a highly nutritive food ingredient, but its solution properties are not well defined. In this study, suspensions of mung bean protein isolate (MPI, 10%, w/v) were subjected to high intensity ultrasound (20 kHz, 30% amplitude) at varied durations (5, 10, 20, and 30 min) with controlled temperatures (30, 50, and 70 °C) to determine the effects of thermosonication treatment on physical properties of the protein solution. Results showed that thermosonication treatment significantly reduced the particle size and free sulfhydryl content of MPI in a time-dependent manner. Ultrasound increased surface hydrophobicity, and the exposure of nonpolar groups led to the formation of soluble aggregates. Changes in secondary structure of MPI were minimal at 30 and 50 °C but were significant at 70 °C. The dissociation of native components followed by reaggregation into soluble particles following ultrasound treatment at 70 °C resulted in remarkable improvements of protein solubility (>2 fold), clarity, and stability of the MPI suspensions. The findings indicated that thermosonication could be a promising technology for the processing of mung bean protein beverage.     

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.     

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

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

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

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