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.     

Effect of high intensity ultrasound on gelation properties of silver carp surimi with different salt contents

Surimi from silver carp with different salt contents (0–5%) was obtained treated by high intensity ultrasound (HIU, 100 kHz 91 W·cm⁻²). The gelation properties of samples were evaluated by puncture properties, microstructures, water-holding capacity, dynamic rheological properties and intermolecular interactions. As the salt content increased from 0 to 5%, gel properties of surimi without HIU significantly improved. For samples with low-salt (0–2% NaCl) content, HIU induced obvious enhancement in breaking force and deformation. HIU promoted the protein aggregation linked by SS bonds, hydrophobic interactions and non-disulfide covalent bonds in surimi gels with low-salt content. Moreover, microstructures of HIU surimi gels with low-salt content were more compact than those of the corresponding control samples. HIU also improved the gelation properties of surimi with 3% NaCl to an extent. However, for high-salt (4–5% NaCl) samples, HIU decreased the breaking force and deformation of surimi gels due to the degradation of proteins suggested by increased TCA-soluble peptides. In conclusion, HIU effectively improved the gelation properties of surimi with low-salt content (0–2% NaCl), but was harmful for high-salt (4–5% NaCl) surimi. This might provide the theoretical basis for the production of low-salt surimi gels.     

Effect of high intensity ultrasound on transglutaminase-catalyzed soy protein isolate cold set gel

The effects of high intensity ultrasound (HIU, 105–110 W/cm² for 5 or 40 min) pre-treatment of soy protein isolate (SPI) on the physicochemical properties of ensuing transglutaminase-catalyzed soy protein isolate cold set gel (TSCG) were investigated in this study. The gel strength of TSCG increased remarkably from 34.5 to 207.1 g for TSCG produced from SPI with 40 min HIU pre-treatment. Moreover, gel yield and water holding capacity also increased after HIU pre-treatments. Scanning electron microscopy showed that HIU of SPI resulted in a more uniform and denser microstructure of TSCG. The content of free sulfhydryl (SH) groups was higher in HIU TSCG than non-HIU TSG, even though greater decrease of the SH groups present in HIU treated SPI was observed when the TSCG was formed, suggesting the involvement of disulfide bonds in gel formation. Protein solubility of TSCG in both denaturing and non-denaturing solvents was higher after HIU pretreatment, and changes in hydrophobic amino acid residues as well as in polypeptide backbone conformation and secondary structure of TSCG were demonstrated by Raman spectroscopy. These results suggest that increased inter-molecular ε-(γ-glutamyl) lysine isopeptide bonds, disulfide bonds and hydrophobic interactions might have contributed to the HIU TSCG gel network. In conclusion, HIU changed physicochemical and structural properties of SPI, producing better substrates for TGase. The resulting TSCG network structure was formed with greater involvement of covalent and non-covalent interactions between SPI molecules and aggregates than in the TSCG from non-HIU SPI.     

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.     

Positive effects and mechanism of ultrasound on chitin preparation from shrimp shells by co-fermentation

The objective of this study is to explore the effect and mechanism of ultrasound on chitin extraction from shrimp shells powder (SSP) by the co-fermentation of Bacillus subtilis and Acetobacter pasteurianus. After pre-treating the SSP with high-intensity ultrasound (HIU) at 800 W, the protease activity in the fermentation solution reached 96.9 U/mL on day 3, which was significantly higher than for SSP that had not been pre-treated with ultrasound (81.8 U/mL). The fermentation time of the chitin extraction process was 5.0 d without ultrasound pre-treatment, while it was shortened to 4.5 d when using ultrasound at 800 W to treat SSP. However, there were no obvious differences when we applied ultrasound at low power (200 W, 400 W). Furthermore, chitin purified from shrimp shells pre-treated with HIU at 800 W exhibited lower molecular weight (11.2 kDa), higher chitin purity (89.8%), and a higher degree of deacetylation (21.1%) compared to SSP with no ultrasound pre-treatment (13.5 kDa, 86.6%, 18.5%). Results indicate that HIU peels off the protein/CaCO₃ matrix that covers the SSP surface. About 9.1% of protein and 4.7% of Ca²⁺ were released from SSP pre-treated with HIU at 800 W. These figures were both higher than with no ultrasound pre-treatment (4.5%, 3.2%). Additionally, the amount of soluble protein extracted from SSP through HIU at 800 W was 50% higher than for the control sample. SDS-PAGE analysis indicated that the soluble protein was degraded to the micromolecule. It also revealed that HIU (600, 800 W) induced the secondary and tertiary structure destruction of protein extracted from SSP. In conclusion, HIU-induced degradation and structural damage of protein enhances the protein/CaCO₃ matrix to be peeled off from SSP. Also, in the co-fermentation process, an increase of protease activity further accelerates deproteinization.     

Evaluation of the postmortem ageing process of beef M. semitendinosus based on ultrasound-assisted l-histidine treatment

This paper aimed to investigate the postmortem ageing process of beef M. semitendinosus (ST, just slaughtered muscles) using ultrasound-assisted l-histidine treatment. The treatments with different concentrations of l-histidine solutions (0.1%, 0.15%, and 0.2%, w/v) at 4 °C for 60 min were labeled “LH”, “MH” and “HH”, respectively. Furthermore, the corresponding treatments with the above l-histidine solutions for 55 min after ultrasound pretreatment for 5 min were labeled “ULH”, “UMH” and “UHH”, respectively. The results showed that the UMH group had the lowest Warner-Bratzler shear stress. The pH value of the HH and UHH groups was higher than that of the other groups (HH: 6.39 ± 0.02, UHH: 6.52 ± 0.03, P < 0.05). The MH and UMH groups showed large fiber spacing, cavities and fractures as well as obviously damaged myofibrils. In the UMH group, the soluble protein concentration (SPC) and caspase-3 activity were the highest, and the turbidity of actomyosin was the lowest. Surprisingly, the Ca²⁺-ATPase activity of actomyosin increased gradually with increasing concentrations of l-histidine solution. Therefore, the UMH treatment promoted the process of meat ageing, exhibiting the potential to be used by beef or other meat manufacturers to improve the production efficiency.     

Effect of high intensity ultrasound on the structure and solubility of soy protein isolate-pectin complex

In this study, a soy protein isolate (SPI)-pectin (PC) complex was prepared, and the effects of different high intensity ultrasound (HIU) powers on the structure and solubility of the complex were studied. Fourier transform infrared (FTIR) spectroscopy analysis exhibited that with increasing HIU power, the α-helix content of the SPI in the complex was significantly reduced, and the random coil content increased; however, an opposite trend appeared after higher power treatments. Fluorescence spectra showed that HIU treatment increased the fluorescence intensity of the complex, and the surface hydrophobicity was increased. The trend of the protein structure studied by Raman spectroscopy was similar to that of FTIR and fluorescence spectroscopy. When the HIU treatment was performed for 15 min and at 450 W power, the particle size of the complex was 451.85 ± 2.17 nm, and the solubility was 89.04 ± 0.19 %, indicating that the HIU treatment caused the spatial conformation of the protein to loosen and improved the functional properties of the complex. Confocal laser scanning microscopy (CLSM) revealed that the complex after HIU treatment exhibited improved dispersibility in water and smaller particle size. Gel electrophoresis results indicated that HIU treatment did not affect the protein subunits of the complex. Therefore, the selection of a suitable HIU treatment power can effectively improve the structural properties and solubility of SPI in the complex, and promote the application of the SPI-PC complex in food processing and industries.     

High intensity ultrasound-assisted quality enhancing of the marinated egg: Gel properties and in vitro digestion analysis

In this study, high intensity ultrasonication (HIU) was employed as an efficient tool to improve the gel property and in vitro digestibility of marinated egg (ME). The effects of HIU treatment at 100 W and 200 W for a series of time periods (0.5 h, 1 h, and 2 h) on the textural profiles, structural changes, and microstructures were also studied. After HIU treatment, the springiness and gumminess of ME white were enhanced. The water holding capacity reached the highest point (66.6%) when 0.5 h 200 W HIU was used. It was observed that 100 W HIU led to the highest zeta potential (-12.0 mV) and hydrophobicity (175.35 μg) of ME, indicating a high degree of electrostatic repulsion prevented agglomeration. HIU treatment at 100 W affected the dynamic rheological behaviors by boosting non-covalent bonds, which maintains the gel network's homogeneity. Meanwhile, the decreasing formation of α-helix, in contrast to β-turn, altered the aggregation behaviors of egg white gel. The microstructure of the 200 W HIU treated samples had porous colloidal network structures, and the in vitro digestibility (>75%) was increased after HIU. This work demonstrated that HIU could be a green and cost-effective tool for processing the egg product with high quality.     

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.     

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

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

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.     

Post-mortem ultrasound and freezing of rabbit meat: Effects on the physicochemical quality and weight loss

High intensity ultrasound (HIU) is a technique with the potential to improve meat quality, however, more research is needed on its application within the chain of cold storage and freezing. This study evaluates the effect of HIU (40 kHz, 9.6 W/cm², 20 and 40 min) and post-mortem development on the yield and physicochemical quality of rabbit meat in samples treated with HIU pre- and post-storage in a freezer (120 h at −20 °C). Twenty rabbit carcasses were vacuum packed 12 h post-mortem, placed in a fridge at 4 °C for 24 h, and divided in two groups (HIU application before or after freezing), before assigning the treatments. The results show that HIU before freezing produced intense and bright orange-yellow colours, whereas its application after freezing resulted in pale red tones. HIU application accelerates rigor mortis resolution when it is applied before freezing and causes a significant decrease in pH immediately following the HIU treatment. Post-freezing application of HIU is not recommended because it considerably increased weight loss and toughening of the meat when long exposure times were used (40 min). In contrast, a short treatment duration with HIU mitigated the effects of freezing and produced significant increases in water-holding capacity (WHC) after cold storage. The yield (weight loss) of the rabbit meat was not affected when HIU was applied pre-freezing. The application of HIU pre-freezing constitutes a promising technology because it increased the tenderness and the WHC of rabbit meat. However, more research is needed to improve the appearance before scaling up to industrial levels.     

Synergistic effect of preheating and different power output high-intensity ultrasound on the physicochemical,structural, and gelling properties of myofibrillar protein from chicken wooden breast

The effects of preheating to 50 ℃ and the subsequent application of high-intensity ultrasound (HIU, 20 kHz) at 200, 400, 600, and 800 W on the physicochemical, structural, and gelling properties of wooden breast myofibrillar protein (WBMP) were studied. Results suggested that the WBMP structure expanded to the balanced state at 600 W, and rheological properties exhibit that 600 W HIU (P < 0.05) significantly improved the storage modulus (G′) of WBMP. Notably, the WBMP gel (600 W) had the best hardness (65.428 ± 0.33 g), springiness (0.582 ± 0.01), and water-holding capacity (86.11 ± 0.83%). Raman spectra and low-field NMR indicated that 600 W HIU increased the β-fold content (37.94 ± 0.04%) and enlarged the immobilized-water proportion (93.87 ± 0.46%). Scanning electron micrographs confirmed that the gel was uniform and dense at 600 W. Therefore, preheating to 50 ℃ followed by HIU (600 W) helped form a superior WBMP gel.     

Evaluation of ultrasound and microbubbles effect on pork meat during brining process

In this study combined effect of ultrasound-induced acoustic cavitation and microbubbles during meat brining on pork loin (Longissimus dorsi) was evaluated. Cylindrical shape (diameter 15 mm, height 80 mm) pork loin samples were cut and immersed in 200 g L^-1 NaCl brine and treated with the following brining methods for 180 min: static brining (SB), ultrasound assisted brining (US) and ultrasound combined with microbubbles in brine (USMB). Ultrasound was generated with 20 kHz frequency, 5,09 W/cm² maximum intensity and 100 W maximum power. Microbubbles in brine were produced by a gas–liquid mixing pump. Effect of ultrasound and microbbubles on NaCl content and diffusion in pork loin, mass balance, water binding capacity (WBC), protein denaturation and meat tissue microstructure were evaluated. The US and USMB brinings enhanced the NaCl diffusion into meat compared to meat brined under static conditions. The constant diffusion coefficient (D) model precisely described the NaCl diffusion kinetics during brinings. The ultrasound and microbbubles resulted in microscopic pores on the surface of myofibers. Decreasing WBC was observed for all brining methods. Myosin was not detectable in any of the brining methods. Denaturation temperature of actin showed a decreasing tendency with increasing brining time independently the brining methods.     

Evaluation of ultrasound-assisted L-histidine marination on beef M. semitendinosus: Insight into meat quality and actomyosin properties

This paper aimed to evaluate the effects of ultrasound-assisted _L-histidine marination (UMH) on meat quality and actomyosin properties of beef M. semitendinosus. Our results found that UMH treatment effectively avoided excessive liquid withdrawal, and disrupted myofibril integrity by modifying the water distribution and weakening connection of actin-myosin with increased muscle pH. The ultrasound-treated sample provided more opportunity for the filtration of _L-histidine to intervene the isoelectric point and conformation of muscle protein. The activated caspase-3 and changes of ATPase activity in UMH-treated meat accelerated the postmortem ageing, and _L-histidine might competitively inhibit the actin-myosin binding by the imidazole group. UMH decreased the surface hydrophobicity by shielding hydrophobic area and unfolding the actomyosin structure. In addition, the increased actomyosin solubility with smaller particle size enhanced the SH content for better cross-linking of myosin tail, and formation of heat-set gelling protein structure. Therefore, UMH treatment manifested the potential to improve beef quality.     

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.     

High-intensity ultrasound promoted the aldol-type condensation as an alternative mean of synthesizing pyrazines in a Maillard reaction model system of D-glucose-13C6 and L-glycine

This study evaluated how the generation of pyrazines was promoted by high-intensity ultrasound (HIU) in a Maillard reaction (MR) model system of glucose-glycine. Carbohydrate module labeling (CAMOLA) technique was adopted using D-glucose-¹³C₆ to elucidate the carbon skeleton of both intermediate and final MR products (MRPs). In the D-glucose-¹³C₆-glycine HIU-MR model system, the concentration of 11 types of pyrazines was significantly higher than their counterparts in the thermal MR. Results of CAMOLA analysis showed that a significantly lower proportion of [M]⁺ in pyrazines with long-length side chains was observed when compared with the pyrazines generated in thermal MR. This phenomenon may suggest the aldol-type condensation was promoted by the HIU, which is a conversion from pyrazines with short-length side chains to those with long-length side chains involving carbonyl compounds. Furthermore, the analysis of isotopomers distribution in 2,3-dimethyl-quinoxaline as the o-phenylenediamine-derivatized 2,3-butanedione indicated that the increased proportion of [M + 4]⁺ in 2,3-dimethyl-quinoxaline (15.74% ± 0.11%) was attributed to a cleavage of D-glucose-¹³C₆ promoted by the HIU. The above-mentioned findings elucidate that the aldol-type condensation and cleavage of D-glucose contribute to the promoted synthesis of pyrazines. The HIU would generate an extremely high temperature and pressure environment that is favored by the aldol-type condensation as a high-pressure favored reaction. The HIU, therefore, can be further developed as a promising technique to promote flavor generation through the MR.     

High-intensity ultrasound improves the physical stability of myofibrillar protein emulsion at low ionic strength by destroying and suppressing myosin molecular assembly

The specific molecular behavior of myofibrillar proteins (MPs) in low-salt media limits the development of muscle protein-based emulsions. This study aimed to evaluate the potential of high-intensity ultrasound (HIU; 150, 300, 450, and 600 W) to improve the physical stability of MP emulsion at low ionic strength and decipher the underlying mechanism. According to the physical stability analysis, HIU pretreatment, especially at 450 W power, significantly improved the physical stability of MP emulsions, as evidenced by the reduced particle size, enhanced inter-droplet interactions, and increased uniformity of the droplet size distribution (p < 0.05). The results of interfacial protein composition, Fourier transform infrared spectroscopy analysis, and microscopic morphology observation of the aqueous MP suspension suggested that HIU induced the depolymerization of filamentous myosin polymers and inhibited the subsequent self-assembly behavior. These effects may facilitate protein adsorption and molecular rearrangement at the oil–water interface, forming a complete interfacial layer and, thus, droplet stabilization. Confocal laser scanning microscopy observations further confirmed these results. In conclusion, these findings provide direct evidence for the role of HIU in improving the physical stability of MP emulsions at low ionic strength.     

Second-order non-linear optical studies on CdS microcrystallite-doped alkali borosilicate glasses

CdS microcrystal-doped alkali borosilicate glasses were prepared by conventional fusion and heat-treatment method. Utilizing Maker fringe method, second-harmonic generation (SHG) was both observed from CdS-doped glasses before and after certain thermal/electrical poling. While because the direction of polarization axes of CdS crystals formed in the samples is random or insufficient interferences of generated SH waves occur, the fringe patterns obtained in samples without poling treatments showed no fine structures. For the poled samples, larger SH intensity has been obtained than that of the samples without any poling treatments. It was considered that the increase of an amount of hexagonal CdS in the anode surface layer caused by the applied dc field increased the SH intensity. The second-order non-linearity χ⁽²⁾ was estimated to be 1.23 pm/V for the sample poled with 2.5 kV at 360 °C for 30 min.