Effect of ultrasound on the techno-functional properties of food components/ingredients: A review

Ultrasound (US) has been used in many food systems and model systems, such as starch, whey protein concentrates and soy, to modify their chemical and techno-functional properties. At present, the use of ultrasound has yielded diverse results, ranging from potentiating the technological and functional properties of various foods to different operating conditions. Similarly, the results that were obtained vary according to the ultrasonic equipment used and the power, frequency and times of sonication, as well as the characteristics of the food system used. However, not all results have been favourable because US can cause damage to the structure of some food components, such as starch, and affect the technological and functional properties of the food. In the literature, there is little research on the effect of sonication on fibre; this gap in the literature is worrisome because fibre is found in a wide variety of foods and provides health benefits. Such research would represent an opportunity for researchers to make use of this technology for the generation of knowledge and improve the techno-functional properties in fibre, which could benefit the human population and the food industry. In this review, we present current results obtained with US in different treatments affecting processes of strong importance in the food industry, emphasizing the effects in the different model systems.     

Effects of high-energy ultrasound on the functional properties of proteins

In recent years, high-energy ultrasound has been used as an alternative to improve the functional properties of various proteins, such as from milk, eggs, soy and poultry. The benefits of implementing this technology depend on the inherent characteristics of the protein source and the intensity and amplitude of the ultrasound, as well as on the pH, temperature, ionic strength, time, and all of the variables that have an effect on the physicochemical properties of proteins. Therefore, it is necessary to establish the optimal conditions for each type of food. The use of ultrasound is a promising technique in food technology with a low impact on the environment, and it has thus become known as a green technology. Therefore, this review focuses on the application of high-energy ultrasound to food; its effects on the functional properties of proteins; and how different conditions such as the frequency, time, amplitude, temperature, and protein concentration affect the functional properties.     

Ultrasound-assisted processing: Science,technology and challenges for the plant-based protein industry

The present-day consumer is not only conscious of the relationship between food consumption and positive health, but also keen on environmental sustainability. Thus, the demand for plant-based proteins, which are associated with nutrition and environmental sustainability. However, the plant-based protein industry still demands urgent innovation due to the low yield and long extraction time linked with traditional extraction methods. Although ultrasound is an eco-innovative technique, there exist limited data regarding its impact with plant-based protein. In this paper, the scientific principles of ultrasonication with regards to its application in plant-based protein research were reviewed. After comparing the cavitational and shearing impacts of different ultrasonic parameters, the paper further reviewed its effects on extracted protein characteristics and techno-functional properties. Additionally, current technological challenges and future perspectives of ultrasonication for the plant-based protein industry were also discussed. In summary, this review does not only present the novelty and environmental sustainability of ultrasound as a plant-based protein assisted-extraction method, but also highlights on the correlation between protein source, structure and subsequent functional properties which are important crucial factors for maximum application of ultrasound in the growing plant-based protein market.     

Modifying the physicochemical properties,solubility and foaming capacity of milk proteins by ultrasound-assisted alkaline pH-shifting treatment

This study investigated the effects of different treatment of alkaline pH-shifting on milk protein concentrate (MPC), micellar casein concentrate (MCC) and whey protein isolate (WPI) assisted by the same ultrasound conditions, including changes in the physicochemical properties, solubility and foaming capacity. The solubility of milk proteins had a significant increase with gradual enhancement of ultrasound-assisted alkaline pH-shifting (p < 0.05), especially for MCC up to 99.50 %. Also, treatment made a significant decline in the particle size of MPC and MCC, as well as the turbidity of the proteins (p < 0.05). The foaming capacity of MPC, MCC, and WPI was all improved, especially at pH 11, and at this pH, the milk protein also showed the highest surface hydrophobicity. The best foaming capacity at pH 11 was the result of the combined effect of particle size, potential, protein conformation, solubility, and surface hydrophobicity. In conclusion, ultrasound-assisted pH-shifting treatment was found to be effective in improving the physicochemical properties and solubility and foaming capacity of milk proteins, especially MCC, with promising application prospect in food industry.     

Ultrasonication as an innovative approach to tailor the apple seed proteins into nanosize: Effect on protein structural and functional properties

In this study, protein was extracted from the apple seed flour using alkali-acid precipitation method. The main objective of this study was to evaluate the impact of ultrasonication on structural and techno-functional properties of apple seed protein. Both native (N-protein) and ultra-sonicated protein (US-protein) were characterized for size, zeta potential, structure, protein pattern, crystallinity, thermal stability and functional properties. The results revealed that the hydrodynamic diameter of N-protein and US-protein was 1.2 µm and 484 nm while zeta potential was −11 and −19 mV, respectively. Fourier transform infrared-spectroscopy and X-ray diffraction analysis showed change in the conformational characteristics and functional groups of proteins after nano-reduction. SEM revealed change in the surface morphology of protein molecule upon ultrasonication. Differential scanning calorimetry showed decreased denaturation temperature for US-protein compared to N-protein . SDS-PAGE depicted no change in protein pattern upon ultrasonication. Ultrasonicated protein exhibited increased functional properties like emulsification, foaming, hydrophobicity and oil absorbing properties and hence can be efficiently used as functional ingredient in food and nutraceutical industry.     

Recent advances in the application of ultrasound in dairy products: Effect on functional,physical, chemical,microbiological and sensory properties

Alternative methods for improving traditional food processing have increased in the last decades. Additionally, the development of novel dairy products is gaining importance due to an increased consumer demand for palatable, healthy, and minimally processed products. Ultrasonic processing or sonication is a promising alternative technology in the food industry as it has potential to improve the technological and functional properties of milk and dairy products. This review presents a detailed summary of the latest research on the impact of high-intensity ultrasound techniques in dairy processing. It explores the ways in which ultrasound has been employed to enhance milk properties and processes of interest to the dairy industry, such as homogenization, emulsification, yogurt and fermented beverages production, and food safety. Special emphasis has been given to ultrasonic effects on milk components; fermentation and spoilage by microorganisms; and the technological, functional, and sensory properties of dairy foods. Several current and potential applications of ultrasound as a processing technique in milk applications are also discussed in this review.     

Effects of ultrasound pretreatment on functional property,antioxidant activity,and digestibility of soy protein isolate nanofibrils

Nanofibrils, an effective method to modulate the functional properties of proteins, can be promoted by ultrasound pretreatment. This study investigated the effect of ultrasound pretreatment on the structure, functional property, antioxidant activity and digestibility of soy protein isolate (SPI) nanofibrils. The results showed that high amplitude ultrasound had a significant effect on structure of SPI nanofibrils. SPI nanofibrils pretreated by 80% amplitude ultrasound showed a blueshift of the amide II band in Fourier transform infrared spectroscopy (FTIR), resulted in more tryptophan residues being buried and increased the crystallinity. Low amplitude ultrasound (20%) pretreatment significantly improved the solubility, emulsifying activity index (EAI) and water absorption capacity (WAC) of SPI nanofibrils, but 80% amplitude ultrasound pretreatment of SPI nanofibrils reduced emulsifying stability index (ESI). High amplitude ultrasound (60% and 80%) pretreatment of SPI nanofibrils improved the foaming capacity and foaming stability and decreased denaturation temperature. DPPH radical scavenging activity of SPI nanofibrils were significantly improved by ultrasound pretreatment. 20% amplitude ultrasound pretreatment improved DPPH, ABTS radical scavenging activity and ferric reducing antioxidant power of SPI nanofibrils. The digestion rate of 80% amplitude ultrasound-pretreated nanofibrils were consistently higher, and SPI nanofibrils pretreated by ultrasound were more fragmented and shorter after simulating gastrointestinal digestion. This study would expand the application of food-grade protein nanofibrils in the food industry.     

Low-frequency and high-power ultrasound-assisted production of natural blue colorant from the milk and unripe Genipa americana L.

This study presents the production of a novel natural blue colorant obtained from the cross-linking between milk proteins and genipin assisted by low-frequency and high-power ultrasound technology. Genipin was extracted from unripe Genipa americana L. using milk as a solvent. Also, milk colloidal system was used as a reaction medium and carrier for the blue color compounds. The effects of ultrasound nominal power (100, 200, 300, and 400 W) on the blue color formation kinetics in milk samples were evaluated at 2, 24, and 48 h of cold storage in relation to their free-genipin content and color parameters. In addition, Fourier transform infrared (FTIR) spectrum, droplet size distribution, microstructure, and kinetic stability of the blue colorant-loaded milk samples were assessed. Our results have demonstrated that the ultrasound technology was a promising and efficient technique to obtain blue colorant-loaded milk samples. One-step acoustic cavitation assisted the genipin extraction and its diffusion into the milk colloidal system favoring its cross-linking with milk proteins. Ultrasound process intensification by increasing the nominal power promoted higher genipin recovery resulting in bluer milk samples. However, the application of high temperatures associated with intensified acoustic cavitation processing favored the occurrence of non-enzymatic browning due to the formation of complex melanin substances from the Maillard reaction. Also, the blue milk samples were chemically stable since their functional groups were not modified after ultrasound processing. Likewise, all blue colorant-loaded milk samples were kinetically stable during their cold storage. Therefore, a novel natural blue colorant with high-potential application in food products like ice creams, dairy beverages, bakery products, and candies was produced.     

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.     

Functionalised dairy streams: Tailoring protein functionality using sonication and heating

Ultrasound can be used to modify the functional interactions between casein and whey proteins in dairy systems. This study reports on ongoing developments in understanding the effect of ultrasound and heating on milk proteins in systems with modified casein-whey protein ratios (97:3, 80:20 and 50:50), prepared from milk protein concentrates that were fractionated by microfiltration, based on protein size. Heating of concentrated casein streams (9% w/w) at 80.0 °C for up to 9 min resulted in reduced gelation functionality and increased viscosity, even in the absence of added whey proteins. 20 kHz ultrasonication at 20.8 W calorimetric power for 1 min was able to break protein aggregates formed during heating, resulting in improved gelation and reduced viscosity. Interestingly, when heated whey protein was recombined with unheated casein the gelation properties were similar to unheated controls. In contrast, when heat treated casein streams were recombined with unheated whey protein, the gel forming functionality was reduced. This study therefore shows that using specific combinations of heat and/or ultrasound, fractionated dairy streams can be tailored for specific functional outcomes.     

Sustainable emerging high-intensity sonication processing to enhance the protein bioactivity and bioavailability: An updated review

High-intensity ultrasound (HIU) is considered one of the promising non-chemical eco-friendly techniques used in food processing. Recently (HIU) is known to enhance food quality, extraction of bioactive compounds and formulation of emulsions. Various foods are treated with ultrasound, including fats, bioactive compounds, and proteins. Regarding proteins, HIU induces acoustic cavitation and bubble formation, causing the unfolding and exposure of hydrophobic regions, resulting in functional, bioactive, and structural enhancement. This review briefly portrays the impact of HIU on the bioavailability and bioactive properties of proteins; the effect of HIU on protein allergenicity and anti-nutritional factors has also been discussed. HIU can enhance bioavailability and bioactive attributes in plants and animal-based proteins, such as antioxidant activity, antimicrobial activity, and peptide release. Moreover, numerous studies revealed that HIU treatment could enhance functional properties, increase the release of short-chain peptides, and decrease allergenicity. HIU could replace the chemical and heat treatments used to enhance protein bioactivity and digestibility; however, its applications are still on research and small scale, and its usage in industries is yet to be implemented.     

Influence of high-intensity ultrasound on physicochemical and functional properties of a guamuchil Pithecellobium dulce (Roxb.) seed protein isolate

In this study, the influence of ultrasound on the physicochemical and functional properties of guamuchil seed protein isolate (GSPI) was investigated. The GSPI was prepared by alkaline extraction and isoelectric precipitation method followed by treating with ethanol (95%), from defatted guamuchil seed flour. GSPI suspensions (10%) were sonicated with a probe (20 kHz) at 3 power levels (200 W, 400 W, 600 W) for 15 and 30 min, in addition, to control treatment without ultrasound. Moisture content, water activity, bulk and compact densities and the L*, a* and b* color parameters of the GSPI decreased due to the ultrasound. Glutelin (61.1%) was the main protein fraction in GSPI. Results through Fourier transform infrared and fluorescence spectroscopy showed that ultrasound modified the secondary and tertiary protein structures of GSPI, which increased the surface hydrophobicity, molecular flexibility and in vitro digestibility of GSPI proteins by up to 114.8%, 57.3% and 12.5%, respectively. In addition, maximum reductions of 11.9% in particle size and 55.2% in turbidity of GSPI suspensions, as well as larger and more porous aggregates in GSPI lyophilized powders were observed by ultrasound impact. These structural and physicochemical changes had an improvement of up to 115.5% in solubility, 39.8% in oil absorption capacity, while the increases for emulsifying, foaming, gelling, flow and cohesion properties of GSPI were 87.4%, 74.2%, 40.0%, 44.4%, and 8.9%, respectively. The amelioration of the functional properties of GSPI by ultrasound could represent an alternative for its possible use as a food ingredient in industry.     

Covalent binding of ultrasound-treated japonica rice bran protein to catechin: Structural and functional properties of the complex

Due to the existence of many disulfide bonds in japonica rice bran protein (JRBP) molecules, their solubility is poor, which seriously affects other functional properties. To improve the functional characteristics of JRBP molecules, they were processed by ultrasound technology, and JRBP-catechin (CC) covalent complex was prepared. The structural and functional properties of indica and japonica rice bran proteins and their complexes were compared; furthermore, the changes in the structural and functional properties of JRBP-CC under different ultrasound conditions were investigated. The results showed that compared with indica rice bran protein (IRBP), the secondary structure of JRBP-CC was very different, the water holding capacity (WHC) was higher, and the emulsification performance was better. Different ultrasound conditions had different effects on the functional properties of JRBP-CC. When the ultrasound power was 200 W, the λ_max redshift of the JRBP-CC complex was the most significant, the particle size was the smallest, the absolute value of the zeta potential was the largest, and the hydrophobicity and microstructure of the JRBP-CC complex were the best. Concurrently, the maximum WHC and oil holding capacity (OHC) of JRBP-CC under these conditions were 7.54 g/g and 6.87 g/g, respectively. Moreover, the emulsifying activity index (EAI) and emulsifying stability index (ESI) were 210 m²/g and 47.8 min, respectively, and the scavenging activities of 1,1-diphenyl-2-picrylhydrazyl (DPPH) and ABTS⁺ were 71.96 % and 80.07 %, respectively.     

Structural and physicochemical properties of the different ultrasound frequency modified Qingke protein

There is a burgeoning demand for modified plant-based proteins with desirable physicochemical and functional properties. The cereal Qingke is a promising alternative protein source, but its use has been limited by its imperfect functional characteristics. To investigate the effect of ultrasound treatment on Qingke protein, we applied single- (40 kHz), dual- (28/40 kHz), and tri- (28/40/50 kHz) frequency ultrasound on the isolated protein and measured subsequent physicochemical and structural changes. The results showed that the physicochemical properties of proteins were modified following ultrasound treatment, and many of these changes significantly increased with increasing frequency. Compared with the native Qingke protein (control), the solubility, foaming activity, stability, and water or oil holding capacity of tri-frequency ultrasound modified Qingke protein increased by 43.54%, 20.83%, 20.51%, 28.9%, and 45.2%, respectively. Furthermore, ultrasound treatment altered the secondary and tertiary structures of the protein resulting in more exposed chromophoric groups and inner hydrophobic groups, as well as reduced β-sheets and increased random coils, relative to the control. Rheological and texture characterization indicated that the values of G' and G'', hardness, gumminess, and chewiness decreased after ultrasound treatment. This study could provide a theoretical basis for the application of multi-frequency ultrasonic technology for modification of Qingke protein to expand its potential use as an alternative protein source.     

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 modified the functional properties of Neosalanx taihuensis myofibrillar protein and improved its emulsion stability

This study aimed to investigate the effects of high-intensity ultrasound treatment on the functional properties and emulsion stability of Neosalanx taihuensis myofibrillar protein (MP). The results showed that the carbonyl groups, emulsification properties, intrinsic fluorescence intensity, and surface hydrophobicity of the ultrasound treated MP solution were increased compared to the MP without ultrasound treatment. The results of secondary structure showed that the ultrasound treatment could cause a huge increase of β-sheet and a decline of α-helix of MP, indicating that ultrasound induced molecular unfolding and stretching. Moreover, ultrasound reduced the content of total sulfhydryl and led to a certain degree of MP cross-linking. The microscopic morphology of MP emulsion indicated that the emulsion droplet decreased with the increase of ultrasound power. In addition, ultrasound could also increase the storage modulus of the MP emulsion. The results for the lipid oxidation products indicated that ultrasound significantly improved the oxidative stability of N. taihuensis MP emulsions. This study offers an important reference theoretically for the ultrasound modification of aquatic proteins and the future development of N. taihuensis deep-processed products represented by surimi.     

Modifications to functional and biological properties of proteins of cowpea pulse crop by ultrasound-assisted extraction

Natural resource depletion, negative environmental effects and the challenge to secure global food security led to the establishment of the Sustainable Development Goals (SDGs). In need to explore underutilized sustainable protein sources, this study aims at isolating protein from cowpea by ultrasound-assisted extraction (UAE), where the techno-functional characteristics of the protein isolates were studied at different sonication conditions i.e., 100 W and 200 W at processing times ranging from 5 to 20 min. The US at 200 W-10 min produced the optimal results for all properties. In this process combination, there was an increase in protein yield, solubility, water-holding capacity, foaming capacity and stability, emulsion activity and stability, zeta-potential, and in-vitro protein digestibility from 31.78% to 58.96%, 57.26% to 68.85%, 3.06 g/g to 3.68 g/g 70.64% to 83.74%, 30.76% to 60.01%, 47.48% to 64.26%, 56.59% to 87.71%, –32.9 mV to −44.2 mV and 88.27% to 89.99%, respectively and particle size dropped from 763 nm to 559 nm in comparison to control. The microstructure and secondary-structure alterations of proteins caused by sonication were validated by SEM images, SDS-PAGE, and FTIR analyses. Sonication leads to acoustic cavitation and penetrate the cell walls, improving extraction from the solid to liquid phase. After sonication, the hydrophobic protein groups were exposed and proteins were partially denatured which increased its functionality. The findings demonstrated that UAE of cowpea protein improved yield, modify characteristics to fit the needs of the food industry, and contribute to achieving SDGs 2, 3, 7, 12, and 13.     

Effects of ultrasound-assisted basic electrolyzed water (BEW) extraction on structural and functional properties of Antarctic krill (Euphausia superba) proteins

A novel protein extraction method of ultrasound-assisted basic electrolyzed water (BEW) was proposed, and its effects on the structural and functional properties of Antarctic krill proteins were investigated. Results showed that BEW reduced 30.9% (w/w) NaOH consumption for the extraction of krill proteins, and its negative redox potential (−800 ~ −900 mV) protected the active groups (carbonyl, free sulfhydryl, etc.) of the proteins from oxidation compared to deionized water (DW). Moreover, the ultrasound-assisted BEW increased the extraction yield (9.4%), improved the solubility (8.5%), reduced the particle size (57 nm), favored the transition of α-helix and β-turn to β-sheet, promoted the surface hydrophobicity and disulfide bonds formation of krill proteins when compared to BEW without ultrasound. These changes contributed to the enhanced foam capacity, foam stability and emulsifying capacity of the krill proteins. Notably, all the physicochemical, structural and functional properties of the krill proteins were comparable to those extracted by the traditional ultrasound-assisted DW. This study suggests that the ultrasound-assisted BEW can be a potential candidate to extract proteins, especially offering an alternative way to produce marine proteins with high nutritional quality.     

Ultrasound-assisted modification of functional properties and biological activity of biopolymers: A review

In this review, the recent applications of power ultrasound technology in improving the functional properties and biological activities of biopolymers are reviewed. The basic principles of ultrasonic technology are briefly introduced, and its main effects on gelling, structural, textural, emulsifying, rheological properties, solubility, thermal stability, foaming ability and foaming stability and biological activity are illustrated with examples reviewing the latest published research papers. Many positive effects of ultrasound treatment on these functional properties of biopolymers have been confirmed. However, the effectiveness of power ultrasound in improving biopolymers properties depends on a variety of factors, including frequency, intensity, duration, system temperature, and intrinsic properties of biopolymers such as macromolecular structure. In order to obtain the desired outcomes, it is best to apply optimized ultrasound processing parameters and use the best conditions in terms of frequency, amplitude, temperature, time, pH, concentration and ionic strength related to the inherent characteristics of each biopolymer. This will help employ the full potential of ultrasound technology for generating innovative biopolymers functionalities for various applications such as food, pharmaceuticals, and other industries.     

Ultrasonic pretreatment improves the gelation properties of low-salt Penaeus vannamei (Litopenaeus vannamei) surimi

The effects of different ultrasonic pretreatments (120–600 W, 20 min; 360 W, 10–30 min) on the gel properties of shrimp surimi were investigated. Gel properties and protein functional properties were analysed to clarify the mechanism of action of ultrasound. The gel strength, water holding capacity and surface hydrophobicity of shrimp surimi gel increased initially and then decreased with the increase in ultrasound power or time, but the change in total sulfhydryl content showed the opposite trend, which indicated that proper ultrasound pretreatment could improve the gel properties of shrimp surimi, expand the protein to a greater extent and expose more SH groups and hydrophobic groups. According to scanning electron microscopy observation, ultrasound made shrimp surimi gel form a denser gel network. Fourier transform infrared analysis indicated that the α-helix content in shrimp surimi gel decreased initially and then increased with the increase of in ultrasound power or time, whereas the change in β-sheet content showed the opposite trend. And the protein was the most stable in 360 W/20 min pretreatment. SDS-PAGE patterns showed that proper ultrasound inhibited the degradation of actin and troponin C. In addition, dynamic rheology illustrated that the G′ values of the ultrasonic pretreatment group were higher than that of the control group, indicating that ultrasound could improve the elasticity and stability of shrimp surimi gel. The results suggested that the shrimp surimi gel pretreated by 360 W/20 min ultrasound showed the best gel properties. Furthermore, the correlation between the indexes affecting the properties of the gel was analyzed. This study provides a new technical means to improve the gel properties of shrimp surimi.