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.     

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

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

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.     

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

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

Effect of ultrasound-assisted resting on the quality of surimi-wheat dough and noodles

In this study, the influence of ultrasound-assisted resting at different power on the rheological properties, water distribution and structural characteristics of dough with 50 % surimi as well as the texture, cooking and microstructure characteristics of the surimi-wheat noodles were investigated. Compared with the fermentation control (FC) noodles, the microstructure, cooking and texture characteristics of noodles (≤24.00 W/L) were significantly (p < 0.05) improved after ultrasonic treating. As the increasing of ultrasonic power, compared to FC, the creep strain, recovery strain, semi-bound water, and free sulfhydryl (SH) contents of surimi-wheat dough decreased at first and then increased significantly (p < 0.05). The α-helix and β-turn content of dough increased at first and then decreased after ultrasonic treatment, while the β-sheet was reversed. The surimi-wheat dough network structure was improved by ultrasonic treatment, with the densest and continuous pore size in 21.33 W/L, but the dough structure was broken and loose (>21.33 W/L), which consisted of the hardness, elasticity, chewiness, resistant and cooked quality of surimi-wheat noodles. This work elucidated the effect of ultrasonic power on the performance of surimi-wheat dough, and the optimal ultrasound power was obtained, thereby improving the nutritional properties and the quality of surimi-wheat noodles.     

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 of ultrasound-assisted sodium bicarbonate treatment on gel characteristics and water migration of reduced-salt pork batters

To study the potential usefulness of ultrasound (0, 30, and 60 min) and sodium bicarbonate (0 % and 0.2 %) combination on the reduced-salt pork batters, the changes in water holding capacity, gel properties, and microstructure were investigated. The pH, salt-soluble proteins solubility, cooking yield, and b* values of reduced-salt pork batters significantly increased (P < 0.05) with the increase in ultrasound time and the addition of sodium bicarbonate, leading to the hardness, springiness, cohesiveness, and chewiness significantly increased (P < 0.05). Furthermore, the use of ultrasound-assisted sodium bicarbonate treatment caused the reduced-salt pork batters to form a typical spongy structure with more evenly cavities. Due to the initial relaxation time of T₂₁ and T₂₂ were shorter, and the peak ratio of P₂₁ was increased and P₂₂ was decreased after ultrasound-assisted sodium bicarbonate treatment, implying that the mobility of water was reduced. Thus, the use of ultrasound-assisted sodium bicarbonate treatment enabled reduced-salt pork batters to have better gel characteristics and higher cooking yield.     

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

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

Effects of high intensity unltrasound on structural and physicochemical properties of myosin from silver carp

Myosin from silver carp was sonicated with varying power output (100, 150, 200 and 250 W) for 3, 6, 9, and 12 min. The changes in the structure and physicochemical properties of myosin were evaluated by dynamic light scattering, SDS-PAGE and some physicochemical indexes. The ultrasound treatments induced a significant conversion of myosin aggregates to smaller ones with a more uniform distribution, and obvious enhancement in solubility. The structure of myosin was also notably changed by sonication, with a decrease in Ca²⁺-ATPase activity and SH content, and an increase in surface hydrophobicity. Furthermore, SH groups were oxidized, leading to a decrease in reactive SH and total SH contents. SDS-PAGE analysis revealed that ultrasound could induce the degradation of myosin heavy chain and change the protein fraction of myosin. Collectively, the ultrasonic treatment of 100 W for 3 min showed slight influence on the SH content, S₀-ANS, and electrophoretic patterns, and the extent of changes in myosin structure and physicochemical properties tended to increase with ultrasonic power and time. The integrated data indicate that ultrasonic treatment can facilitate the improvement of the solubility and dispersion of myosin, but the choice of a suitable ultrasonic condition to avoid oxidation and degradation of myosin is very important.     

Effects of ultrasound pretreatment on the quality,nutrients and volatile compounds of dry-cured yak meat

The objective of the present study was to assess the effects of ultrasound pretreatment on the quality of dry-cured yak meat. The ultrasonic power with 0, 200, 300 and 400 W (ultrasonic frequency of 20 kHz) were used to assist processing of dry-cured yak meat. The meat quality, nutrient substances, sensory quality, electronic nose, electronic tongue and volatile compounds of dry-cured yak meat were determined. The results indicated that the moisture content and hardness value of ultrasonic treatment group was significantly lower compared to the control group (P < 0.05). Ultrasonic treatment increased the value of b*, and decreased the value of L*, a*, pH, chewiness, melting temperature and enthalpy. Springiness value significantly increased from control group to 300 W of ultrasonic power group. Shear force significantly decreased with the increase of ultrasonic power (P < 0.05). Ultrasonic treatment had no effect on the TVB-N content, but it could increase the TBARS content. Ultrasonic treatment could significantly increase the essential FAA (EFAA) and total FAA (P < 0.05). In addition, the saturated fatty acid (SFA) content significantly increased with the increase of ultrasonic power (P < 0.05). Ultrasound treatment negatively affected the meat’s color, smell, and taste but increased its tenderness and the overall acceptability. It also significantly increased alcohols and aldehydes contents (P < 0.05), which were consistent with the measurement of electronic nose and electronic tongue. The results demonstrated that the the appropriate ultrasonic power assisted in the processing improves quality of dry-cured yak meat, particularly for the power of 300 W.     

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 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.     

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.     

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.     

Modification of rapeseed protein by ultrasound-assisted pH shift treatment: Ultrasonic mode and frequency screening,changes in protein solubility and structural characteristics

We investigated the effect of ultrasound-assisted pH shift treatment on the micro-particle, molecular, and spatial structure of rapeseed protein isolates (RPI). Various ultrasonic frequency modes (fixed, and sweep) was used. Protein characterization by the indexes: particle size, zeta potential, sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), scanning electron microscopy (SEM), free sulfhydryl (SH), surface hydrophobicity (Ho), Fourier transform infrared Spectrum (FTIR) and fluorescence intensity was studied to elucidate the changes in solubility and structural attributes of RPI. The results showed that ultrasonic frequency and working modes substantially altered the structure, and modified the solubility of RPI. Ultra + pH mode at fixed frequency of 20 kHz had the best effect on the solubility of RPI. Under the condition of ultra + pH mode, 20 kHz at pH 12.5, solubility, compared to control, increased from 8.90% to 66.84%; and the change in molecular structure of RPI was characterized by smaller particles (from 330.90 to 115.77 nm), high zeta potential (from −17.95 to −14.43 mV, p < 0.05), and increased free sulfhydryl (from 11.63 to 24.50 µmol/g) compared to control. Likewise, surface hydrophobicity increased (from 2053.9 to 2649.4, p < 0.05), whilst ɑ-helix and random coil decreased (p < 0.05), compared to control. The fluorescence spectroscopy and FTIR spectroscopy showed that the secondary and tertiary structure of the RPI were altered. These observations revealed that changes in RPI structure was the direct factor affecting solubility. In conclusion, ultrasound assisted pH shift treatment was proven to be an effective method for the modification of protein, with promising application in food industry.     

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.     

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

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

Effect of high-intensity ultrasound on 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.     

Effects of multi-frequency power ultrasound on the enzymolysis and structural characteristics of corn gluten meal

The aim of this study was to investigate the effect of multi-frequency power ultrasound (sweeping frequency and pulsed ultrasound (SFPU) and sequential dual frequency ultrasound (SDFU)) on the enzymolysis of corn gluten meal (CGM) and on the structures of the major protein fractions (zein, glutelin) of CGM. The results showed that multi-frequency power ultrasound pretreatments improved significantly (P < 0.05) the degree of hydrolysis and conversion rate of CGM. The changes in UV–Vis spectra, fluorescence emission spectra, surface hydrophobicity (H₀), and the content of SH and SS groups indicated unfolding of zein and glutelin by ultrasound. The circular dichroism analysis showed that both pretreatments decreased α-helix and increased β-sheet of glutelin. The SFPU pretreatment had little impact on the secondary structure of zein, while the SDFU increased the α-helix and decreased the β-sheet remarkably. Scanning electron microscope indicated that both pretreatments destroyed the microstructures of glutelin and CGM, reduced the particle size of zein despite that the SDFU induced aggregation was observed. In conclusion, multi-frequency power ultrasound pretreatment is an efficient method in protein proteolysis due to its sonochemistry effect on the molecular conformation as well as on the microstructure of protein.     

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.