Lower Surface Hydrophobicity Research Articles

Differences in protein hydrolysis on quality of fermented milk: The changes in structure and processing characteristics

The functions and sensory properties of fermented dairy products are influenced by numerous factors, including the type of milk, the strain's degree of protein hydrolysis, and the additives of fermented milk. Currently, a large number of studies have demonstrated that the proteolytic ability of probiotics significantly affects the gel properties of fermented milk. However, few studies have examined the effects of probiotics with varying proteolytic abilities on the functions and sensory properties of fermented dairy products from the protein conformation perspective. Therefore, this study screened Lactobacillus helveticus KLDS1.8701 with a high protein hydrolysis rate and Lactobacillus helveticus KLDS1.0633 with a low hydrolysis rate to investigate the effects of varying degrees of protein hydrolysis on the gel properties, sensory properties and protein conformation of fermented milk. The results showed that the fermented milk containing Lactobacillus helveticus KLDS1.0633 with a low protein hydrolysis degree had high WHC, hardness and viscosity, a dense and uniform structure, abundant pores, and good texture and sensory properties. In addition, compared with fermented milk with high protein hydrolysis, low protein hydrolysis also increased the content of disulfide bonds, low surface hydrophobicity, and more hydrophilic structures such as a-helix. This study explains the impact of differences in protein hydrolysis degree among strains on fermented milk from a new perspective of protein secondary and tertiary conformations, which provides new insights for selecting suitable strains to produce fermented milk with better taste and nutrition.

Deciphering the mechanism underlying poor aqueous solubility of extracted quinoa proteins

This study aimed to decipher the mechanisms underlying poor solubility of quinoa proteins by investigating the form of quinoa proteins dispersed in water and how protein-protein interactions influenced the kinetic stability of proteins in the dispersions. Specifically, the relative solubility and the forms of quinoa proteins in 1–5 w/w% protein dispersions were determined by separating proteins via centrifugation and/or ultrafiltration. The kinetic stability of quinoa proteins in the supernatants over a 3-week storage period was characterized by determining the changes of concentration, composition and physicochemical properties of quinoa proteins and predicting protein-protein interactions. The results showed that quinoa proteins existed mainly as differently-sized protein aggregates in the dispersions, leading to low relative solubility. The coagulation of protein aggregates in the supernatants caused severe precipitation during the first week of storage whereas they were disassociated simultaneously. With further storage, the remaining proteins in the supernatants reached kinetic stability, which was contributed by stronger electrostatic repulsion and lower surface hydrophobicity. Moreover, 11S globulin and 2S albumin were precipitated and solubilized together during storage, which was ascribed to intermolecular interactions driven by multiple sites between 11S globulin and/or 2S albumin. This study lays a foundation for extensive utilization of quinoa proteins.

Optimizing β-Lactoglobulin antigenicity through single enzyme hydrolysis: Exploring structural changes and effects on linear epitopes

β-lactoglobulin (β-LG) is the major allergen in dairy products, but research on the optimal conditions for antigen reduction in β-LG using different enzymes remains limited. Therefore, this study aims to investigate the antigenicity, structural characteristics, and peptide distribution of advantageous protease hydrolysates capable of eliminating the allergenic epitopes of β-LG selected via bioinformatics tools. The results showed that under optimal enzymatic hydrolysis conditions, the antigen reduction rates for the four advantageous proteases acting on β-LG were 47.37 % (pepsin), 33.54 % (chymotrypsin A), 38.71 % (papain), and 45.91 % (stem bromelain), respectively. The four proteases effectively degraded β-LG, causing shorter peptide chain formation, reduced content of highly ordered α-helix, decreased fluorescence intensity, and lower surface hydrophobicity. Furthermore, they cleaved the linear epitopes of β-LG into peptides of varying sizes, leading to different antigen reduction rates among the hydrolysates. These findings provide a theoretical basis for developing targeted enzymatic hydrolysis technologies and low-allergenicity dairy-based materials.

Dynamic mechanism and structural property analysis of microfluidic-obtained pea protein fiber

Although protein-based fibers have been developed, the preparation of inexpensive, safe and environmentally friendly plant protein fibers is still a hot topic. Herein, we constructed the microfluidic chip to produce protein fiber using pea protein and a small amount of cellulose nanofibers. The results demonstrated that compared to pea protein alone, the pea protein-based fiber produced through microfluidic spinning exhibited a smooth and dense surface structure, good thermal stability, higher Zeta potential and antioxidant activity, and lower surface hydrophobicity and sensitization. Furthermore, we comprehensively revealed the dynamic formation mechanism of pea protein-based fiber. During the fiber preparation process, hydrodynamics led the protein and cellulose nanofibers to align gradually along the flow direction, enhancing their molecular orientation. Additionally, strong hydrodynamic shear force altered the protein structure, transitioning its spatial structure from random coil and α-helix to β-sheet, and promoting a binding of protein to cellulose nanofibers. This research may offer theoretical guidance for the application of pea protein-based fiber in the preparation of hypoallergenic protein-based fibers and the construction of foodborne delivery materials.

Physicochemical property characterization, amino acid profiling and sensory evaluation of plant-based ice cream incorporated with soy, pea and milk proteins

This study examined the effects of incorporating milk protein concentrate (MPC), pea or soy proteins isolates (PPI and SPI) on the physicochemical, sensorial properties, and amino acid composition of ice creams containing 7% protein, in comparison to dairy ice cream as a reference. As protein ingredients, PPI exhibited higher water and oil holding capacity but lower surface hydrophobicity than SPI and MPC. Viscosity of the mixes were proportional to the firmness of ice cream, and both were highest with use of PPI. MPC ice cream had most similar physical and sensory properties to reference. PPI and SPI ice cream mixes showed higher extent of fat coalescence than MPC and reference. PPI and SPI conferred structural stability to ice cream with lower melting rate and better shape retention, and ability to delay ice recrystallization during temperature flocculation as compared with SMP and MPC. Confocal laser scanning microscope images indicated that higher extent of protein aggregation and more air cells were found in PPI ice cream. Sensory and amino acid profile results revealed that PPI and SPI ice creams were inferior in taste, texture, and essential amino acids like methionine. This study offers insights for the development of high protein frozen desserts.

Formulations and evaluations of structural and physico-chemical properties of soy yogurts: Effect of incorporating soy protein isolate/chitosan complexed microgels

Novel complexed microgels with enhanced pH and ion stability were constructed using heat-denatured soy protein isolate (SPI) and Chitosan (CS). Their characteristics and their effects on the textural, rheological, and tribological properties of soy yogurt were investigated. The complexed microgels showed larger particle sizes, lower surface hydrophobicity, and higher turbidity than pure SPI microgels. Incorporating the SPI-CS complexed microgels into the yogurts increased their protein content from 3.94% to 5.07% and reduced their fat content from 2.17% to 1.99%. Additionally, incorporating the microgels enhanced the texture of the yogurts, including increased firmness, elasticity, and viscosity, alongside improved water holding capacity (WHC). The incorporation of 0.8% SPI-CS microgels led to the optimum physicochemical characteristics. Rheological analyses demonstrated that incorporating SPI-CS microgels led to an increase in apparent viscosity and shear modulus. Furthermore, the presence of the SPI-CS microgels significantly improved the lubrication properties. Microstructural analysis showed subtle differences in the gel structure of the yogurts after microgel addition. The three-dimensional network structure within the microgel-fortified yogurts was more compact than that in the control. Thus, SPI-CS microgels potentially improve the nutritional profile and quality attributes of plant-based yogurt products.

Euglena gracilis Protein: Effects of Different Acidic and Alkaline Environments on Structural Characteristics and Functional Properties.

Due to the growing demand for human-edible protein sources, microalgae are recognized as an economically viable alternative source of proteins. The investigation into the structural characteristics and functional properties of microalgin is highly significant for its potential application in the food industry as an alternative source of protein. In this research, we extracted protein from Euglena gracilis by using alkaline extraction and acid precipitation and investigated its structural characteristics and functional properties in different acidic and alkaline environments. The molecular weight distribution of Euglena gracilis protein (EGP), as revealed by the size exclusion chromatography results, ranges from 152 to 5.7 kDa. EGP was found to be rich in hydrophobic amino acids and essential amino acids. Fourier infrared analysis revealed that EGP exhibited higher α-helix structure content and lower β-sheet structure content in alkaline environments compared with acidic ones. EGP exhibited higher foaming properties, emulsifying activity index, solubility, free sulfhydryl, and total sulfhydryl in pH environments far from its isoelectric point, and lower fluorescence intensity (2325 A.U.), lower surface hydrophobicity, larger average particle size (25.13 µm), higher emulsifying stability index, and water-holding capacity in pH environments near its isoelectric point. In addition, X-ray diffraction (XRD) patterns indicated that different acidic and alkaline environments lead to reductions in the crystal size and crystallinity of EGP. EGP exhibited high denaturation temperature (Td; 99.32 °C) and high enthalpy (ΔH; 146.33 J/g) at pH 11.0, as shown by the differential scanning calorimetry (DSC) results. The findings from our studies on EGP in different acidic and alkaline environments provide a data basis for its potential commercial utilization as a food ingredient in products such as emulsions, gels, and foams.

Improved stability of sesame paste by peanut protein-flaxseed gum conjugation

The oil-water separation phenomenon in sesame paste poses a challenge for the storage of sauce products. In this study, soy protein isolate (SPI), peanut protein isolate (PPI) and flaxseed gum (FG) conjugates were prepared to stabilize the solid-liquid phases of sesame paste. The results indicated that the highest degree of grafting (25.07%) was observed in a ratio of PPI:FG = 4:1 (PF2). The interaction between proteins and FG generated the extension of the protein molecule and increased structural disorder. PPI-FG conjugates exhibited the lower surface hydrophobicity and higher thermal stability. The addition of 4% PF2 to sesame paste led to a reduction of 5.06% oil separation rate and showed higher storage modulus (G′), loss modulus (G″), apparent viscosity, and hardness. A stable and continuous three-dimensional network was created to physically entrap the oil, resulting in a more uniform distribution of oil droplets and a reduced particle interaction of sesame paste.

Proposing moderate unfolding of interfacial proteins to enhance the techno-functional features of complex microgel particles formed by whey protein-chitooligosaccharide conjugation

To elucidate the roles of interfacial protein microstructure in regulating techno-functional attributes of complex microgel, this work explored the effects of transglutaminase cross-linking alone or in combination with ultrasonication on conformation and functional properties of whey protein isolate-chitooligosaccharide microgel dispersion (WPI–COS). It was found that transglutaminase-crosslinked WPI-COS microgels presented improved interfacial properties when a moderate unfolding process was induced by sonication, validating the existence of optimum flexibility of complex Pickering particles during unfolding/refolding of interfacial proteins. Particularly, TG induced excessive crosslinking of WPI-COS to form aggregates, causing a lower surface hydrophobicity. In contrast, ultrasound was inclined to increase the surface hydrophobicity for TG-catalyzed and uncatalyzed samples, suggesting differential unfolding degrees of WPI induced by transglutaminase and ultrasonication. Correspondingly, interfacial properties of ultrasonicated WPI-COS complexes, as revealed by percentage of adsorbed protein, interfacial tension and three-phase contact angle and emulsifying properties, were improved significantly. Confocal laser scanning microscopy and transmission electron microscopy consistently observed WPI-COS tightly adsorbed at the oil-water interface, with smaller emulsion droplets, more uniform distribution and thicker interfacial films at the oil-water interface in WPI-COS microgel particles with sonication-induced unfolding. This investigation demonstrated the feasibility of conformational regulation of interfacial proteins in tuning techno-functional features of microgel particles.

Characterization of sodium caseinate derived from various sources: Unraveling the relationship between structure and functional properties

In this study, the structural and functional properties of laboratory-prepared sodium caseinate (L-SC) from yak Qula with three different sources of commercial products: yak milk, Qula, and milk sodium caseinate products (YM-SC, YQ-SC, M-SC) were compared. The physicochemical properties of different samples were analyzed, indicating significant fat content and color differences. The SDS-PAGE showed predominant protein subunits in the 25 kDa–35 kDa range, with M-SC having the highest κ-casein content and the least aggregation. M-SC exhibited the smallest particle size, lowest surface hydrophobicity (H0) and surface tension at the oil-water interface, with excellent functional properties, whereas YQ-SC exhibited contrast. FTIR suggested that the effect may be attributed to the decreased α-helix and β-sheet structure, and reduction in H0 and protein aggregation, resulting in a notable enhancement in protein solubility and surface activity. After optimizing the alkali extraction conditions and drying method, L-SC showed a reduced particle size of 135.0 nm, significantly improved foaming properties while the prepared emulsion had good stability and smaller d4,3. In addition, the relationship among the indicators was verified by the correlation analysis. These results could provide more information for the manufacturing of sodium caseinate in the food industry.

Insight into quality, microstructure, and protein physicochemical properties of Monopterus albus frozen with liquid nitrogen

Monopterus albus is highly susceptible to spoilage due to high protein and moisture contents while frozen storage can effectively prolong the shelf-life. To study the effect of liquid nitrogen freezing (LNF) on quality, microstructure of ice crystal and muscle fiber, and physicochemical properties of proteins, Monopterus albus was frozen at -20 °C by refrigerator (RF, control), -50 °C, -80 °C, and -110 °C by LNF, respectively. The -110 °C LNF exhibited the highest freezing rate among four groups, contributing to the formation of small ice crystals with more uniform distribution and alleviating the damage to muscle fiber. In -110 °C LNF group, protein secondary structure changed relatively subtle, resulting in high protein solubility, Ca2+-ATPase activity, and total sulfhydryl content, as well as low surface hydrophobicity and disulfide bond content. LNF retarded the rise of TVB-N value, prevented the loss of immobilized and free water, and maintained water holding capacity and shear force. In conclusion, -110 °C LNF was recommended a promising freezing process for frozen Monopterus albus due to less alteration of quality and alleviation of protein denaturation.

Lightweight and drift-free magnetically actuated millirobots via asymmetric laser-induced graphene

Millirobots must have low cost, efficient locomotion, and the ability to track target trajectories precisely if they are to be widely deployed. With current materials and fabrication methods, achieving all of these features in one millirobot remains difficult. We develop a series of graphene-based helical millirobots by introducing asymmetric light pattern distortion to a laser-induced polymer-to-graphene conversion process; this distortion resulted in the spontaneous twisting and peeling off of graphene sheets from the polymer substrate. The lightweight nature of graphene in combine with the laser-induced porous microstructure provides a millirobot scaffold with a low density and high surface hydrophobicity. Magnetically driven nickel-coated graphene-based helical millirobots with rapid locomotion, excellent trajectory tracking, and precise drug delivery ability were fabricated from the scaffold. Importantly, such high-performance millirobots are fabricated at a speed of 77 scaffolds per second, demonstrating their potential in high-throughput and large-scale production. By using drug delivery for gastric cancer treatment as an example, we demonstrate the advantages of the graphene-based helical millirobots in terms of their long-distance locomotion and drug transport in a physiological environment. This study demonstrates the potential of the graphene-based helical millirobots to meet performance, versatility, scalability, and cost-effectiveness requirements simultaneously.

In-situ observation of hydrogen nanobubbles formation on graphene surface by AFM-SECM

Gas bubble evolution is an important phenomenon in many electrochemical processes and it is highly sensitive to the surface properties. Here we visualize the gas bubble dynamics on the surface of different graphene substrates during hydrogen evolution reaction (HER) using atomic force microscopy combined with scanning electrochemical microscopy. The low overpotential and low surface hydrophobicity of few-layer graphene formed on C-phase SiC causes the uniform distribution of hydrogen nanobubbles, which easily depart from the surface during the reaction. Conversely, the high overpotential and more hydrophobic surface of HOPG induces hydrogen bubbles to linger on the surface for an extended duration, leading to its accumulation and the subsequent formation of microbubbles. This in-situ nanoscale electrochemical mapping of hydrogen bubble dynamics provides new insight into electrocatalytic HER that occurs on non-metal electrodes.

Effect of limited proteolysis and CaCl2 on the rheology, microstructure and in vitro digestibility of pea protein-carboxymethyl cellulose mixed gel

Limited proteolysis, CaCl2 and carboxymethyl cellulose (CMC) have individually demonstrated ability to increase the gel strength of laboratory-extracted plant proteins. However, the syneresis effects of their combination on the gelling capacity of commercial plant protein remains unclear. This was investigated by measuring the rheological property, microstructure and protein–protein interactions of gels formed from Alcalase hydrolyzed or intact pea proteins in the presence of 0.1 % CMC and 0–25 mM CaCl2. Sodium dodecyl-sulfate polyacrylamide gel electrophoresis (SDS-PAGE) showed the molecular weight of pea protein in the mixture were < 15 kDa after hydrolysis. The hydrolysates showed higher intrinsic fluorescence intensity and lower surface hydrophobicity than the intact proteins. Rheology showed that the storage modulus (G') of hydrolyzed pea protein (PPH)-based gels sightly decreased compared to those of native proteins. 5–15 mM CaCl2 increased the G’ for both PP and PPH-based gels and decreased the strain in the creep-recovery test. Scanning electron microscopy (SEM) showed the presence of smaller protein aggregates in the PPH-based gels compared to PP gels and the gel network became denser, and more compact and heterogenous in the presence of 15 and 25 mM CaCl2. The gel dissociation assay revealed that hydrophobic interactions and hydrogen bonds were the dominant forces to maintain the gel structure. In vitro digestion showed that the soluble protein content in PPH-based gels was 10 ∼ 30 % higher compared to those of the PP counterpart. CaCl2 addition reduced protein digestibility with a concentration dependent behavior. The results obtained show contrasting effects of limited proteolysis and CaCl2 on the gelling capacity and digestibility of commercial pea proteins. These findings offer practical guidelines for developing pea protein-based food products with a balanced texture and protein nutrition through formulation and enzymatic pre-treatment.

Migration of polydimethylsiloxane chain segments toward the surface of UV-cured waterborne poly(urethane-acrylate) films

Waterborne polyurethane (WPU) has poor water resistance and low surface hydrophobicity due to the incorporation of hydrophilic chain-extender. The water resistance and the surface hydrophobicity can be improved by incorporation of polydimethylsiloxane (PDMS), which is attributed to the migration of PDMS chain segments toward the surface of WPU film. However, whether the PDMS chain segments can migrate toward the surface of WPU film after UV-curing, resulting in higher hydrophobicity, needs further investigation? We prepared the different WPUA films by changing the molar ratio of aminopropyl-terminated polydimethylsiloxane (APT-PDMS) to hydroxyethyl acrylate (HEA), to deeply understand the migrating phenomenon of PDMS chain segments toward the surface of WPUA films. The migration cause of PDMS chain segments and the influence of chemical cross-linking on the migration were investigated by thermal annealing and solvent immersion of WPUA films. In addition, the migration activation energy and the relaxation time were studied by the migration rate of PDMS chain segments in the thermal annealing and the rheological behavior of WPUA film, aiming to elucidate the migration of PDMS chain segments depending on the chain motion and the fractional free volume. This investigation provides a simple and feasible strategy for improving the hydrophobicity of waterborne polyurethane.

Mechanism of the solubility increase of rice protein-ovalbumin co-assembly and its great potential as an emulsifier in high internal phase emulsion

The functionality (e.g., emulsifying ability) of rice protein (RP) is restricted largely by its low solubility. The formation of a co-assembly with RP and an exogenous protein through pH-cycle is one promising method, but the mechanism behind this has not been revealed. This study utilized ovalbumin (OVA) to improve the solubility of RP and investigated the effect of OVA on the physicochemical characteristics of RP, the interactions between RP-OVA co-assembly and water, the RP-OVA interactions, the key subunits related to the solubility improvement of RP, and the emulsifying capacity of the co-assembly. The formation of RP-OVA co-assembly considerably improved the solubility of RP (up to 73.12%), and the multi-level structure and surface property of RP were altered by OVA. The mechanism for the solubility increase was the hydrophobic interactions between OVA and RP, resulting in the exposure of some hydrophilic amino acids to protein surface and further generating a low surface hydrophobicity that allow more water molecules to permeate. Eight subunits in RP were critical for its solubility increase. The RP-OVA co-assembly prepared in this study showed an emulsifying ability even better than whey protein isolate (a commercial emulsifier) in high internal phase emulsion. This study may guide the solubility improvement of RP and widen the application of RP in the food industry as an emulsifier.

Modification of hordein by gallic acid in ethanol-free environments: Impact of covalent and non-covalent interactions on structure, physicochemical properties and self-assembly

The objectives of this study were to modify hordein with gallic acid (GA) in alcohol-free media and to compare the impact of covalent and non-covalent binding on the properties of hordein. Covalent hordein-GA complexes (H-GA) and non-covalent hordein/GA complexes (H/GA) were distinguished by molecular weight, free sulfhydryl groups and free amino groups. Isothermal titration calorimetry (ITC) demonstrated that physical mixing induced non-covalent binding of GA to hordein via hydrogen bonding and hydrophobic interactions, with a lower binding efficiency than covalent ones. Both complexation types led to a structural shift of hordein toward disorder, while grafting of oligomeric GA and alkaline treatment resulted in lower surface hydrophobicity and higher antioxidant activity of H-GA compared to H/GA. The nanoparticles assembled from H-GA had smaller particle sizes and higher physical stability than those formed from H/GA. The results of this study may provide new insights into the modification of hordein by polyphenols.

Cryoprotective effect of epigallocatechin gallate replacing sucrose on Hypophythalmichthys molitrix surimi during frozen storage.

The present study aimed to investigate the cryoprotective effect of epigallocatechin gallate (EGCG) replacing sucrose on surimi during frozen storage. Substitution or partial substitution of 0.1% EGCG for sucrose (1.5%) was added to surimi, and the surimi samples without and with commercial cryoprotectants (4% sucrose and 4% sorbitol) were used as the control group. The results obtained suggest that, with the increase in frozen storage time, the structural performance of surimi protein gradually weakened (e.g. the decrease in the surface hydrophobicity, the increase in the total sulfhydryl and solubility, and the protein myosin heavy chain bands became shallow) and surimi gel quality gradually deteriorated (e.g. the decrease in water-holding capacity, gel strength and all texture profile attributes). However, compared with the other three group surimi samples during the frozen period, the surimi proteins with partial replacement of sucrose by EGCG had a higher total sulfhydryl group content and solubility of proteins, as well as lower surface hydrophobicity of protein, suggesting that the addition of EGCG as a partial substitute for sucrose can enhance the antifreeze ability of surimi. Meanwhile, the surimi gel with the partial replacement of sucrose by EGCG had a higher water retention capacity, gel strength and texture attributes (e.g. hardness, springiness, cohesiveness, chewiness, and resilience), indicating that the addition of EGCG as a partial substitute for sucrose can inhibit the deterioration of surimi gel quality. Overall, EGCG partially replacing sucrose can play an alternative cryoprotectant with a lower sweetness to prevent the quality of surimi from deteriorating. © 2024 Society of Chemical Industry.

Structural, emulsifying and curcumin-embedded properties of arachin nanoparticles induced by ultrasound and heat

Different types of arachin (one of the major globulins in peanut proteins) nanoparticles were prepared by ultrasound (US) and heat treatments, respectively. The results showed that short-term US treatment induced large nanoparticles (named US200 and US500, ∼267 nm) that maintained a compact globular structure; long-term US treatment induced small nanoparticles (named US500L, ∼197 nm) with a moderately unfolded structure; heat treatment induced medium-sized nanoparticles with an unfolded structure. The large nanoparticles had significantly lower surface hydrophobicity, β-sheet content, and λmax but higher enthalpy of denaturation (ΔH) than other nanoparticles. US500L and US500 exhibited the highest emulsifying activity and stability indices, respectively. As for curcumin-embedded properties, both US and heat treatments enhanced the curcumin encapsulation efficiency (from 88.53 to 94.08–97.88%) and load amount (from 1.77 to 1.88–1.96 μg/mg) of arachin. However, only curcumin in large nanoparticles was effectively protected from damage by heat and light. In simulated digestion tests, curcumin in US500L and heat-induced nanoparticles showed higher stability and bioavailability, which was mainly attributed to the slower digestion of these nanocomplexes. We have established a simple method for the preparation of arachin nanoparticles by US and the nanoparticles have potential applications in the food industry due to their favorable bifunctional properties.

Modification mechanism of soybean protein isolate-soluble soy polysaccharide complex by EGCG through covalent and non-covalent interaction: Structural, interfacial, and functional properties

Soybean protein isolate was modified with polysaccharides and polyphenols to prepare a natural emulsifier with antioxidant capacity. Physicochemical, structural, interfacial, and functional properties of SPI-SSPS complex were investigated after covalent and non-covalent interacted with EGCG. SPI-SSPS-EGCG ternary complex with low EGCG concentrations (0.0625 and 0.125 mg/mL) showed a significant increase in absolute potential value and a decrease in turbidity. EGCG destroyed the original rigid structure of SPI-SSPS complex, and the covalent complexes had an ordered structure, while the non-covalent interaction resulted in disordered. The ternary complex with high EGCG concentrations (0.25 and 0.5 mg/mL) exhibited stronger EGCG binding capacity and lower surface hydrophobicity, which in turn affected its interfacial properties. The EAI and ESI of SPI-SSPS-EGCG covalent complex increased significantly, while the non-covalent complex had a significant change in EAI but no significant change in ESI with increasing EGCG concentration. The ternary complex showed significantly enhanced antioxidant capacity. The SPI-SSPS-EGCG ternary complex, with excellent antioxidant capacity and emulsifying property, making it suitable for emulsion delivery systems.