Lysinoalanine formation and conformational characteristics of rice dreg protein isolates by multi-frequency countercurrent S-type sonochemical action

The influences of multi-frequency countercurrent S-type ultrasound (MFSU), with various frequency modes, on lysinoalanine (LAL) formation and conformational characteristics of rice dreg protein isolates (RDPI) were investigated. The ultrasonic operating mode with dual-frequency combination (20/40 kHz) indicated lower LAL content and higher protein dissolution rate of RDPI compared with that of other ultrasound operating modes. Under the dual-frequency ultrasound mode of 20/40 kHz, acoustic power density of 60 W/L, time of 20 min, and temperature of 35 °C, the relative reduction rate of LAL of RDPI reached the highest with its value of 26.95%, and the protein dissolution rate was 71.87%. The changes in chemical interactions between protein molecules indicated that hydrophobic interactions and disulfide bonds played a considerable role in the formation of LAL of RDPI, especially the reduction of g-g-g and g-g-t disulfide bond. Alterations in microstructure showed that ultrasonication loosened the protein structure and created more uniform protein fragments of RDPI. In conclusion, using MFSU in treating RDPI was an efficacious avenue for minimizing LAL content and modifying the conformational characteristics of RDPI.     

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.     

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

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

Improvement in enzymolysis efficiency and changes in conformational attributes of corn gluten meal by dual-frequency slit ultrasonication action

The influences of dual-frequency slit ultrasound (DFSU) pretreatment with various working parameters on the enzymolysis efficiency and conformational characteristics of corn gluten meal (CGM) were studied. Results indicated that under the conditions of ultrasonic power density of 80 W/L, time of 30 min, ultrasonic intermittent ratio of 5:2 s/s, temperature of 30 °C, and substrate concentration of 50 g/L, the relative enzymolysis efficiency (REE) of CGM reached a maximum of 21.05%, and the protein dissolution rate was 68.50%. In addition, ultrasonication had considerable impact on the conformation of CGM and consequently improved the susceptibility to alcalase proteolysis. Changes in free sulfhydryl (SH_F) and disulfide bonds (SS) groups indicated spatial conformation of CGM was altered following sonication (sonochemical) treatment. Fourier Transform Infrared Spectrum (FITR) analysis showed a reduction in α-helix and β-turn content; and an increase in β-sheet and random coil content of CGM. Alterations in the particle size, particle size distribution, microstructure and surface roughness (R_a, R_q) indicated generation of smaller and more uniform protein fragments of CGM by sonochemical pretreatment. The proposed mechanism of sonicated CGM was elaborated. Our findings suggest that using DFSU in pretreating CGM may be an efficacious approach to enhance proteolysis.     

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.     

Influence of ultrasound treatment on the physicochemical and antioxidant properties of mung bean protein hydrolysate

This study aimed to investigate influence of ultrasonic treatment on physicochemical and antioxidant properties of mung bean protein hydrolysate (MPH). Physicochemical properties of MPH were evaluated by Tricine-SDS-PAGE, particle size distribution, fourier transform infrared spectroscopy (FTIR) and fluorescence spectroscopy, among others. Radicals scavenging activities of ABTS, hydroxyl, superoxide anion, Fe²⁺ chelating ability and reducing power characterized antioxidant activities of MPH. MPH contained four bands of 25.6, 12.8, 10.6 and 4.9 kDa, in which 4.9 kDa was the most abundant. Ultrasonic treatment increased the contents of aromatic and hydrophobic amino acids in MPH. Ultrasonic treatment decreased the content of α-helix of MPH and increased β-sheet and β-turn compared to MPH. MPH-546 W (ultrasonic treatment 546 W, 20 min) had the lowest average particle size (290.13 nm), zeta potential (-36.37 mV) and surface hydrophobicity (367.95 A.U.). Antioxidant activities of ultrasonicated-MPH increased with the ultrasonic power, achieving the lowest IC₅₀ (mg/mL) of 0.1087 (ABTS), 1.796 (hydroxyl), 1.003 (superoxide anion) and 0.185 (Fe²⁺ chelating ability) in 546 W power. These results indicated ultrasonic treatment would be a promising method to improve the antioxidant properties of MPH, which would broaden the application scope of MPH as bioactive components in the food industry.     

Effect of multiple-frequency ultrasound-assisted transglutaminase dual modification on the structural,functional characteristics and application of Qingke protein

Qingke protein rich in restricted amino acids such as lysine, while the uncoordination of ratio of glutenin and gliadin in Qingke protein has a negative impact on its processing properties. In this study, the effect of multiple-frequency ultrasound combined with transglutaminase treatment on the functional and structural properties of Qingke protein and its application in noodle manufacture were investigated. The results showed that compared with the control, ultrasound-assisted transglutaminase dual modification significantly increased the water and oil holding capacity, apparent viscosity, foaming ability, and emulsifying activity index of Qingke protein, which exhibited a higher storage modulus G' (P < 0.05). Meanwhile, ultrasound combined with transglutaminase treatment enhanced the cross-linking degree of Qingke protein (P < 0.05), as shown by decreased free amino group and free sulfhydryl group contents, and increased disulfide bond content. Moreover, after the ultrasound-assisted transglutaminase dual modification treatment, the fluorescence intensity, the contents of α-helix and random coil in the secondary structure of Qingke protein significantly decreased, while the β-sheet content increased (P < 0.05) compared with control. SDS-PAGE results showed that the bands of Qingke protein treated by ultrasound combined with transglutaminase became unclear. Furthermore, the quality of Qingke noodles made with Qingke powder (140 g/kg dual modified Qingke protein mixed with 860 g/kg extracted Qingke starch) and wheat gluten 60–70 g/kg was similar to that of wheat noodles. In summary, multiple-frequency ultrasound combined with transglutaminase dual modification can significantly improve the physicochemical properties of Qingke protein and the modified Qingke proteins can be used as novel ingredients for Qingke noodles.     

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.     

High intensity ultrasound treatment of protein isolate extracted from dephenolized sunflower meal: Effect on physicochemical and functional properties

The influence of high intensity ultrasound (HIUS) on physicochemical and functional properties of sunflower protein isolates was investigated. Protein solutions (10% w/v) were treated with ultrasound probe (20 kHz) and ultrasound bath (40 kHz) for 5, 10, 20 and 30 min. Thermal stability of protein isolates was reduced as indicated by differential scanning calorimetry. Minimum thermal stability was observed at 20 min of sonication and increased further with increase in treatment time indicating aggregation at prolonged sonication. SDS-PAGE profile of proteins showed a significant reduction in molecular weight. Further, surface hydrophobicity and sulfhydryl content increased after HIUS treatment indicating partial unfolding of proteins and reduction in the intermolecular interactions. The particle size analysis showed that HIUS treatment reduced the particle size. Less turbid solution were observed largely due to reduction in particle size. HIUS decreased the available lysine content in protein isolates. Solubility, emulsifying capacity, emulsion stability, foaming capacity, foam stability and oil binding capacity were improved significantly, while as, water binding capacity was decreased. The effect of HIUS on physicochemical and functional properties of sunflower protein isolates was more pronounced in probe sonication rather than bath sonication. Protein isolates with improved functional properties can be obtained using high intensity ultrasound technology.     

Effects of thermoultrasonic treatment on characteristics of micro-nano particles and flavor in Greenland halibut bone soup

In order to investigate the effects of thermoultrasonic treatment (TUT) on the formation of colloidal micro-nano particles (MNPs) and the quality of halibut bone soup, nutrients, particle characteristics, and flavor characteristics were analyzed. The morphology of MNPs was studied using an optical microscope. Results showed that TUT could increase the nutrient content (total sugars, 22.15 mg/100 mL; water soluble proteins, 173.24 mg/mL; fatty acids, 1779.7 mg/100 mL; solids, 3.16 g/100 mL), reduce the particle size (605.92 nm) and interfacial tension. Meanwhile, TUT make the halibut bone soup has better emulsifying characteristics and stability. The contents of flavor substances, such as esters, 5′-nucleotides, organic acids in the halibut bone soup were more abundant, while the contents of hexanal and 1-octen-3-ol and fishy off-flavor were reduced in TUT group. The overall odor and taste outline were more harmonious. Therefore, TUT can be used in the production of high quality fish bone soup, and TUT could be considered as a good deep processing technology for halibut bone and improve economic efficiency.     

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.     

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.     

Ultrasound-assisted green synthesis of gold nanoparticles using citrus peel extract and their enhanced anti-inflammatory activity

Ultrasound and plant extract are two green approaches that have been used to synthesize gold nanoparticles (AuNPs); however, how the combination of ultrasound and citrus peel extract (CPE) affects the structure characteristics and the bioactivity of AuNPs remains unknown. Here we investigated the effects of ultrasound conditions on the particle size, stability, yield, phenolic encapsulation efficacy, and the anti-inflammatory activity of AuNPs. The results showed that temperature was positively correlated to the particle size and the anti-inflammatory activity of synthesized AuNPs. Increasing the power intensity significantly decreased the particle size, while increased the change of total phenolic content (ΔTPC) in the reaction mixture. The increase of ΔTPC caused the enhanced anti-inflammatory activity of AuNPs. The AuNPs synthesized with or without ultrasound treatment were characterized using UV–Vis, DLS, SEM, TEM, EDS, XRD, and FT-IR. The result verified the formation of negatively charged, spherical, stable, and monodispersed AuNPs. AuNPs synthesized with ultrasound (AuNPs-U) has smaller particle size (13.65 nm vs 16.80 nm), greater yield and anti-inflammatory activity (IC₅₀, 82.91 vs 157.71 μg/mL) than its non-ultrasound counterpart (AuNPs-NU). HPLC analysis showed that hesperidin was the key reductant for the synthesis of AuNPs. AuNPs-U also inhibited the mRNA and protein expression of iNOS and COX-2 in the LPS-induced Raw 264.7 cells. Our research elucidates the relationship between the reaction conditions and the structure characteristics and the anti-inflammatory activity of AuNPs synthesized using CPE with the help of ultrasound, thereafter, provides a feasible and economic way to synthesize AuNPs that can be used to ameliorate inflammation.     

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

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

Effect of ultrasonic power on properties of edible composite films based on rice protein hydrolysates and chitosan

Rice protein hydrolysates (RPH) are incapable of film formation by self-crosslinking due to low molecular mass. Hence, we used chitosan (CS) as a modifier and developed rice protein hydrolysates/chitosan (RPH/CS) edible composite films by means of ultrasound. Results showed that ultrasound treatment decreased the particle size and the viscosity of film-forming solutions. The value of elongation at break of composite films was increased by 125% at 400 W compared with untreated film. The peroxide value of soybean oil was significantly reduced from 16.99 ± 0.78 meq/kg to 2.23 ± 0.09 meq/kg with the increase of ultrasonic power. Ultrasound treatment was efficient in keeping smooth on surface, and the films at ultrasound treatment of 200 W had better compatibility. Moreover, hydrogen bonds and covalent interactions were probably the main forces between RPH and CS and contributed to film formation under ultrasound treatment, which supported by analyses of Fourier transform infrared spectroscopy and X-ray diffraction. These results suggested that ultrasound was an effective method to improve the properties of edible composite films.     

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.     

Structural and functional modification of proteins from black soybean Aquasoya via ultrasonication

Plant-based proteins obtained from agricultural by-products have garnered growing interest in response to consumer awareness of health and environmental issues. This study aimed to improve the functionalities of the proteins recovered from black soybean Aquasoya (PBSA) by modifying their structure via ultrasonication. PBSA was ultrasonicated with a frequency of 40 kHz at 350 W for different time periods (0, 20, 40, and 60 min), and its structural characteristics, physicochemical properties, and functional properties were investigated. Ultrasonication left the primary structure intact but altered the secondary and tertiary structures of the PBSA; α-helix and β-sheet contents decreased, random coil contents increased, and buried non-polar amino acid residues were exposed. Moreover, ultrasound promoted an increase in free sulfhydryl content and a reduction in particle size. Consequently, functional properties, such as solubility, emulsion stability, and foaming performance were improved by modifying the structure and physicochemical properties of PBSA. This work demonstrates the potential of ultrasound, which is favorable for modifying the spatial conformation and related functionalities of proteins, thus meeting the needs of manufacturers to use function-enhanced proteins as food additives.     

Ultrasound pretreatment prior to spray drying improve the flowability and water sorption properties of micellar casein concentrate

This research investigated the effect of ultrasound (US) pretreatment prior to spray drying on the powder flow and moisture sorption behaviour of micellar casein concentrate (MCC). MCC produced from skim milk microfiltration was sonicated at energy intensity of 0 (control), 47 J/mL (S-2000), 62 J/mL (S-3000) and 76 J/mL (S-4000). The results revealed that US pretreatment significantly increased the average particle size (D50) from 82.46 μm to 100.73 μm and reduced the surface fat content from 19.2% to 13.8%, resulting in decreased basic flow energy, cake energy and cohesion. Besides, the US treated samples showed relatively poor ability to acquire the moisture from the atmosphere than the control. Protein structure analysis showed that α-helix decreased with enhanced US power, while β-sheet and surface hydrophobicity increased, implying hydrophobic groups were exposed and water sorption rate was impeded. As a result, US pretreatment can improve the powder flow and potentially reduce the negative effect of cake formation at high humidity.     

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.     

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.