Improved water solubility of myofibrillar proteins by ultrasound combined with glycation: A study of myosin molecular behavior

The poor water solubility of myofibrillar proteins (MPs) limits their application in food industry, and is directly related to the molecular behavior associated with myosin assembly into filaments. This study aims to explore the effect of high-intensity ultrasound (HIU) combined with nonenzymatic glycation on the solubility, structural characteristics, and filament-forming behavior of MPs in low ionic strength media. The results showed that the HIU (200–400 W) application could promote the subsequent glycation reaction between MPs and dextran (DX) and interfere with the electrostatic balance between myosin rods, suppressing the formation of filamentous myosin polymers. Glycated MPs pretreated by 400 W HIU had the highest solubility, which corresponded to the smallest particle size, highest zeta potential, and optimum storage stability (P < 0.05). Structure analysis and microscopic morphology observations suggested that the loss of the MP superhelix and the depolymerization of filamentous polymers were the main mechanisms for MP solubilization. In conclusion, HIU combined with glycation can effectively improve the water solubility of MPs by destroying or suppressing the assembly of myosin molecules.     

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.     

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.     

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.     

Improvement of structural,physicochemical, and rheological properties of porcine myofibrillar proteins by high-intensity ultrasound treatment for application as Pickering stabilizers

This study aimed to evaluate the potential of time-dependent (0, 15, 30, 60, 120 min) treatment of porcine-derived myofibrillar proteins (MPs) with high-intensity ultrasound (HIU) for utilizing them as a Pickering stabilizer and decipher the underlying mechanism by which HIU treatment increases the emulsification and dispersion stability of MPs. To accomplish this, we analyzed the structural, physicochemical, and rheological properties of the HIU-treated MPs. Myosin heavy chain and actin were observed to be denatured, and the particle size of MPs decreased from 3,342.7 nm for the control group to 153.9 nm for 120 min HIU-treated MPs. Fourier-transformed infrared spectroscopy and circular dichroism spectroscopy confirmed that as the HIU treatment time increased, α-helical content increased, and β-sheet decreased, indicating that the protein secondary/tertiary structure was modified. In addition, the turbidity, apparent viscosity, and viscoelastic properties of the HIU-treated MP solution were decreased compared to the control, while the surface hydrophobicity was significantly increased. Analyses of the emulsification properties of the Pickering emulsions prepared using time-dependent HIU-treated MPs revealed that the emulsion activity index and emulsion stability index of HIU-treated MP were improved. Confocal laser scanning microscopy images indicated that small spherical droplets adsorbed with MPs were formed by HIU treatment and that dispersion stabilities were improved because the Turbiscan stability index of the HIU-treated group was lower than that of the control group. These findings could be used as supporting data for the utilizing porcine-derived MPs, which have been treated with HIU for appropriate time periods, as Pickering stabilizers.     

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.     

Synergistic modification of pea protein structure using high-intensity ultrasound and pH-shifting technology to improve solubility and emulsification

The most important factors restricting research and application in the food industry are the poor solubility and emulsification of pea protein isolate (PPI). This study investigates the effect of high-intensity ultrasound (HIU, 0–600 W) and pH-shifting treatment, alone or combined, on the structure, solubility, and emulsification of PPI, as well as its potential mechanism. The results revealed that the PPI solubility significantly increases when treated with the combination, corresponding to a decrease in the protein particle size, especially at 500 W of HIU power (p < 0.05). Correspondingly, the emulsion prepared from it was less prone to phase separation during storage. According to the structural analysis, the structural changes caused by protein unfolding (i.e., the exposure of hydrophobic and polar sites and the loss of the α-helix) seemed to be the primary reasons for increased PPI solubility. In addition, confocal laser scanning microscopy indicated that the combination treatment accelerated the adsorption of PPI at the oil/water interface and strengthened the compactness of the interface film. Improved interfacial properties and intermolecular forces played a critical role in the resistance to droplet coalescence in PPI emulsion. In conclusion, ultrasound and pH-shifting treatments have a synergistic effect on improving the solubility and emulsification of PPI.     

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 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.     

Physicochemical properties of tilapia (Oreochromis niloticus) actomyosin subjected to high intensity ultrasound in low NaCl concentrations

Effects of high intensity ultrasound (HIU) on physicochemical properties of tilapia (Oreochromis niloticus) actomyosin in low NaCl concentrations were investigated. The protein content extracted in low NaCl concentrations (0.1–0.3 M NaCl) increased with increasing HIU intensity up to 20.62 W/cm² (p < 0.05). The effect of HIU on actomyosin extractability in high NaCl concentrations (0.6 and 1.2 M NaCl) was less obvious. Ca²⁺-ATPase activity and total sulfhydryl (SH) group content decreased in both 0.2 and 0.6 M NaCl. HIU showed more pronounced effect on oxidation of the SH groups in 0.6 M NaCl, while the reactive SH content at 0.2 M NaCl increased after a prolonged exposure to HIU, suggesting conformational changes induced by HIU. Surface hydrophobicity of actomyosin in 0.6 M NaCl increased with increasing ultrasonic intensity and exposure time to a higher degree than that in 0.2 M NaCl. A greater absolute value of the zeta potential of actomyosin subjected to HIU were also observed. The HIU treatments decreased the turbidity of actomyosin incubated at 40 and 60 °C. A drastic increase in the solubility of myosin heavy chain (MHC) and actin with 0.2 M NaCl were evident when HIU treatments were applied, but degradation of MHC occurred in both 0.2 and 0.6 M NaCl. Based on particle size and microstructure, actomyosin in 0.6 M NaCl underwent more disruption by HIU than that in 0.2 M NaCl. HIU induced protein unfolding and protein dissociation, enabling better extraction in a lower NaCl concentration.     

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 physicochemical properties,microstructure, and stability of soy protein isolate-pectin emulsion

In this study, an emulsion stabilized by soy protein isolate (SPI)-pectin (PC) complexes was prepared to investigate the effects of high-intensity ultrasound (HIU) treatment (150–600 W) on the physicochemical properties, microstructure, and stability of emulsions. The results found that the emulsion treated at 450 W showed the best emulsion stability index (ESI) (25.18 ± 1.24 min), the lowest particle size (559.82 ± 3.17 nm), the largest ζ-potential absolute value (16.39 ± 0.18 mV), and the highest adsorbed protein content (27.31%). Confocal laser scanning microscopy (CLSM) and atomic force microscopy (AFM) revealed that the emulsion aggregation was significantly improved by ultrasound treatment, and the average roughness value (Rq) was the smallest (10.3 nm) at 450 W. Additionally, HIU treatment reduced the interfacial tension and apparent viscosity of the emulsion. Thermal stability was best when the emulsion was treated at 450 W, D₄₃ was minimal (907.95 ± 31.72 nm), and emulsion separation also improved. Consequently, the creaming index (CI) was significantly decreased compared to the untreated sample, indicating that the storage stability of the emulsion was enhanced.     

Effect of high-intensity ultrasound on the technofunctional properties and structure of jackfruit (Artocarpus heterophyllus) seed protein isolate

The influence of high-intensity ultrasound (HIU) on the technofunctional properties and structure of jackfruit seed protein isolate (JSPI) was investigated. Protein solutions (10%, w/v) were sonicated for 15 min at 20 kHz to the following levels of power output: 200, 400, and 600 W (pulse duration: on-time, 5 s; off-time 1 s). Compared with untreated JSPI, HIU at 200 W and 400 W improved the oil holding capacity (OHC) and emulsifying capacity (EC), but the emulsifying activity (EA) and emulsion stability (ES) increased at 400 W and 600 W. The foaming capacity (FC) increased after all HIU treatments, as opposed to the water holding capacity (WHC), least gelation concentration (LGC), and foaming stability (FS), which all decreased except at pH 4 for FS. Tricine sodium dodecyl sulfate polyacrylamide gel electrophoresis (Tricine-SDS-PAGE) showed changes in the molecular weight of protein fractions after HIU treatment. Scanning electron microscopy (SEM) demonstrated that HIU disrupted the microstructure of JSPI, exhibiting larger aggregates. Surface hydrophobicity and protein solubility of the JSPI dispersions were enhanced after ultrasonication, which increased the destruction of internal hydrophobic interactions of protein molecules and accelerated the molecular motion of proteins to cause protein aggregation. These changes in the technofunctional and structural properties of JSPI could meet the complex needs of manufactured food products.     

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.     

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.     

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.     

Ultrasound-assisted immersion freezing reduces the structure and gel property deterioration of myofibrillar protein from chicken breast

The effects of air freezing (AF), immersion freezing (IF) and ultrasound-assisted immersion freezing (UF) at different power levels (125, 165, 205 and 245 W) on the structure and gel properties of the myofibrillar protein (MP) of chicken breast were investigated. UF at 165 W (UF-165) had no obvious negative impact on the primary structure of the MP and effectively reduced the change in the secondary and tertiary structure. In addition, UF-165 significantly reduced the losses in the elastic modulus (G′), gel strength, and gel water holding capacity (P < 0.05). According to low field nuclear magnetic resonance analysis, the T₂₁ and T₂₂ of the UF-165 MP gels were shorter than those of the AF and IF samples, which meant that the UF-165 reduced the mobility of the immobilized water and free water in MP gel. A scanning electron microscopy analysis showed that the appropriate ultrasonic power promoted the formation of a compact and homogeneous protein gel network. These results suggested that the appropriate ultrasonic power maintained the MP structure and reduced the loss of gel quality.     

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.     

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

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