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In order to obtain food packaging film with better performance, whey protein concentrate (WPC) and egg white protein (EWP) were used as film‐forming substrates, and its film properties were modified by transglutaminase (TG). Then the effect of TG on the mechanical, physical, barrier, and microstructural properties of the WPC/EWP composite biodegradable film was investigated, and its preliminary application potential was explored. Compared to WPC and EWP films, WPC/EWP composite film had higher transmittance, tensile strength (TS), and thermal stability. Fluorescence results showed that the film experienced fluorescence quenching after TG treatment. Fourier transform infrared and x‐ray diffraction results showed that WPC and EWP had good compatibility in the biodegradable film, the hydrogen bond interaction of film was increased due to TG, resulting in an increase in TS. Meanwhile, the water vapor permeability and contact angle of WPC/EWP film treated with TG at 5 U/g protein increased by 28% and 76.1%, respectively. Besides, the WPC/EWP biodegradable film modified by TG (TG‐W/E) was applied as a coating film on cherry tomatoes, effectively reducing the weight loss rate during storage from 14.2% to 10.8%. Furthermore, indexes, such as solid content, spoilage rate, hardness, pH, and lycopene, showed that the film had a good preservation effect on cherry tomatoes. To conclude, the appropriate addition of TG has a positive effect on the film properties of the WPC/EWP biodegradable film, which is beneficial to the development and utilization of protein‐based film. WPC/EWP biodegradable film modified by TG has a great application prospect in extending the shelf life of fruit and vegetable. [ABSTRACT FROM AUTHOR]

Summary: Vitamin A (VA) is a fat‐soluble compound that is essential for physiological functions including vision, fetal growth, immune response, cell differentiation and proliferation. However, its susceptibility to environmental conditions leading to poor stability limits its application in food. This study investigated the interaction between egg white protein (EWP) and VA by spectroscopy and molecular docking. The results indicated one EWP could bind 16.00 ± 0.89 VA molecules and the binding constant is (2.59 ± 0.71) × 105 m−1. What's more, there was a fluorescence resonance energy transfer between EWP and VA, and the Förster radius is 5.28 nm. In addition, VA enhanced the hydrophobic interactions with the EWP, resulting in protein aggregation, larger average particle size and more uniform particle size distribution. Finally, the combination of VA with EWP could significantly improve the photothermal stability and storage stability of VA. These studies indicate that EWP nanocomplexes can be used as ideal delivery carriers for bioactive substances. [ABSTRACT FROM AUTHOR]

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This study examined the effects of egg white protein (EWP) and konjac glucomannan (KGM) on the digestion and fermentation properties of shrimp (Trachypenaeus curvirostris) surimi gel (SSG) using in vitro models. The results showed that the in vitro protein digestibility of the SSG-EWP group increased first and then decreased with the increase in EWP concentration, and EWP increased the generation of peptides during SSG digestion. SSG with 4% added EWP had the highest in vitro digestibility, while neither the in vitro protein digestibility nor the peptide release of SSG was significantly influenced by KGM (P > 0.05). EWP and KGM increased the contents of essential amino acids in the digestion products of SSG. Antioxidant assay showed that EWP improved the Fe2+ chelating capacity of the digestion products, but decreased the 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical scavenging capacity. KGM increased the antioxidant activity of the digestion products in terms of both Fe2+ chelating capacity and DPPH radical scavenging capacity. Furthermore, gut microbiome study revealed that EWP played a more positive role in maintaining gut microbial diversity and regulating beneficial bacteria than KGM. Clusters of Orthologous Groups (COG) metabolic pathway analysis indicated 24 major metabolic pathways of intestinal microbes, mainly involving the transport and metabolism of carbohydrates, amino acids and other substances. This study provides technical guidance for the preparation of high-quality T. curvirostris surimi gel.

In this experiment, egg white protein microparticles (EWPM) were used as a lipid substitute matrix to investigate the effects of EWPM/xanthan gum (XG) blend concentration, pH, sodium chloride concentration, sugar concentration, and homogenization conditions on the rheological properties of ultra-low-fat salad dressing products. The results showed that XG had a significant thickening effect on EWPM-based ultra-low-fat salad dressing. However, excess XG led to a decrease in the resilience of low-fat salad dressing. The effects of basic seasoning components on the quality of ultra-low-fat salad dressing were significantly different. pH and salt concentration had a significant impact on the viscosity of the salad dressing system, while sugar addition had a relatively smaller impact on the viscosity. Moderate colloid mill homogenization speed and time reduced the particle size of the product, thereby increasing the internal uniformity and significantly improving the viscosity of ultra-low-fat salad dressing. This study provides a clearer direction for the optimization of low-fat salad dressing.

Aiming to improve the gel property of egg white proteins, in this research, taking egg white protein (EWP) as the research object, the changes in texture, water-holding ratio, molecular forces, Fourier transform infrared chromatography, circular dichroism spectrum, particle size, potential, sulphydryl content, surface hydrophobicity, and scanning electron microscopy were analyzed to explore the mechanism and structural changes of heat-induced gel of EWP after the treatments of Ultra-high Pressure (UHP), Transglutaminase (TG) and Ultra-high Pressure Synergistic Transglutaminase (UTG). The results showed that the hardness, elasticity and water holding capacity of UHP-EWP, TG-EWP and UTG-EWP were all improved, and hydrophobic interaction was the main force to maintain gel. The α-helix content of UHP-EWP, TG-EWP and UTG-EWP decreased, while the β-fold content increased. The average particle size and absolute potential of UHP-EWP decreased, while the changes of TG-EWP and UTG-EWP were opposite. The content of free sulfhydryl groups in UHP-EWP, TG-EWP, and UTG-EWP increased, the content of total sulfhydryl groups decreased, and the surface hydrophobicity increased. The gel structure was more compact and smooth, and the flatness was improved. This research provides a theoretical basis and research ideas for the heat induced gel modification of EWP.

The chemical interaction between egg white protein (EWP) and wheat gluten (WG) is significantly influenced by the amount of EWP added. Therefore, the effects of EWP addition on the gelling properties and chemical interactions of heat‐induced WG–EWP gels are thoroughly examined. The results demonstrate that the enhancement in gel strength of WG–EWP gels is positively correlated with the amount of EWP added. EWP addition improves protein–protein interactions by reducing the freedom of water. The enhanced aggregation between WG and EWP is likely due to a decrease in surface hydrophobicity and an increase in β‐sheet content. EWP enhances cross‐linking with low molecular weight glutenin subunit (LMW‐GS), high molecular weight glutenin subunit (HMW‐GS), and gliadin (Gli). Specifically, EWP primarily cross‐links with ω‐, α‐, and γ‐Glis through S–S bonds and interacts with GS through hydrophobic interactions and S–S bonds. This study provides a theoretical foundation for improving the WG network structure in wheat‐based food production. [ABSTRACT FROM AUTHOR]

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Copyright of Science & Technology of Food Industry is the property of Science & Technology of Food Industry Editorial Office and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

As a natural emulsifier, egg white protein (EWP) has great interfacial characteristics and high security, and has broad development prospects. This study explored the impact of ultrasound synergized citral (CI) treatment on the microstructure, molecular flexibility and emulsifying property of EWP, and predicted the interaction between CI and ovalbumin (the main protein in EWP) through molecular docking. The decrease in free amino content and the growth in molecular weight of EWP suggested that CI and proteins were successfully grafted. The results of physicochemical properties revealed that UCEWP (ultrasound synergized citral-treated EWP) had smaller particle size and larger ζ-potential absolute value, which meant that the stability of UCEWP system was enhanced. From the perspective of interfacial characteristics, UCEWP had lower interfacial tension, which remarkably improved its emulsifying property. The emulsifying activity index (EAI) and emulsifying stability index (ESI) of UCEWP were 1.99 times and 3.19 times higher than that of natural EWP (NEWP). Analysis of Fourier transform infrared spectroscopy (FT-IR) and fluorescence spectroscopy illustrated that the secondary and tertiary structures of UCEWP were more disordered and stretched than those of EWPs. Protein microstructure demonstrated that UCEWP presented loose small particle distribution, and correlation analysis reflected that the improvement of molecular flexibility was positively correlated with the enhancement of emulsifying property. These results elucidated that ultrasound synergized CI treatment is an effective mean to improve the molecular flexibility and emulsifying property of EWP, which provides a valuable reference for further application of EWP.

Protein binding to bile salts (BSs) reduces cholesterol levels, but the exact mechanism is unclear. In this study, we performed simulated gastrointestinal digestion of egg white protein hydrolysate (EWPHs) and included an unenzyme digestion group (CK) to investigate the changes in BSs binding capacity before and after digestion, as well as the relationship between egg white protein (EWP) structure and BSs binding capacity. In addition, peptidomics and molecular docking were used to clarify EWP's binding mechanism. We found that the BSs binding ability of EWPHs was slightly decreased after digestion, but significantly higher than that of the CK group and the digested CK group (D-CK). Particle size analysis and electrophoresis demonstrated that smaller particles and lower molecular weights exhibited enhanced binding capacity to BSs. Fourier Transform infrared spectroscopy (FTIR) results revealed that a disordered structure favored BS binding ability enhancement. Peptides FVLPM and GGGVW displayed hypocholesterolemic efficacy.

As a natural cationic peptide, Nisin is capable of widely inhibiting the growth of Gram-positive bacteria. However, it also has drawbacks such as its antimicrobial activity being susceptible to environmental factors. Nano-encapsulation can improve the defects of nisin in food applications. In this study, nisin-loaded egg white protein nanoparticles (AH-NEn) were prepared in fixed ultrasound-mediated under pH 3.0 and 90 °C. Compared with the controls, AH-NEn exhibited smaller particle size (112.5 ± 2.85 nm), smaller PDI (0.25 ± 0.01), larger Zeta potential (24 ± 1.18 mV), and higher encapsulation efficiency (91.82%) and loading capacity (45.91%). The turbidity and Fourier transform infrared spectroscopy (FTIR) results indicated that there are other non-covalent bonding interactions between the molecules of AH-NEn besides the electrostatic forces, which accounts for the fact that it is structurally more stable than the controls. In addition, by the results of fluorescence intensity, differential scanning calorimetry (DSC), and X-ray diffraction (XRD), it was shown that thermal induction could improve the solubility, heat resistance, and encapsulation of nisin in the samples. In terms of antimicrobial function, acid–heat induction did not recede the antimicrobial activity of nisin encapsulated in egg white protein (EWP). Compared with free nisin, the loss rate of bactericidal activity of AH-NEn was reduced by 75.0% and 14.0% following treatment with trypsin or a thermal treatment at 90 °C for 30 min, respectively. [ABSTRACT FROM AUTHOR]

The encapsulation of propolis has shown promising results for the protection of bioactive compounds, local and gradual release and masking the astringent taste. Ovoalbumin is a protein of animal origin found in large amounts in egg whites, which has good properties as a wall material for particles.The objective of this study was to microencapsulate propolis by spray drying. The best condition for microencapsulation was achieved with 4% ovalbumin at 120 °C, where there was the greatest encapsulation efficiency (88.20%) and spherical shape. However, the increase of ovalbumin concentration resulted lower yields (< 52%). As for the scanning electron microscopy (SEM), the increase of ovalbumin concentration caused an increase of the size with average diameter and formation of spherical microcapsules. The phenolic compounds were already released in the gastric fluid condition (stomach). [ABSTRACT FROM AUTHOR]

Ionizing radiation has its unique popularity as a non-thermal decontamination technique treating with protein-rich foodstuffs to ensure the microbial and sensory quality, particularly for shell eggs. However, the changes in the functional properties of egg protein fractions such as liquid egg white (LEW) with macro/microstructural information are still controversial. Hence, this study was designed to elaborate the foaming and heat-set gelation functionality of LEW following different γ-ray irradiation dose treatments (0, 1, 3 or 5 kGy). For such, the physicochemical properties (active sulfhydryl and the hydrophobicity of protein moieties), structural characteristics (through X-ray diffraction, Fourier-transform infrared spectroscopy and differential scanning calorimetry) and interfacial activities (rheological viscosity, interfacial tension, microrheological performance) were investigated. Then, the thermal gelation of LEW in relation to the texture profile and microstructure (by means of a scanning electron microscope) was evaluated followed by the swelling potency analysis of LEW gel in enzyme-free simulated gastric juice. The results indicated that irradiation significantly increased the hydrophobicity of liquid egg white proteins (LEWPs) (p < 0.05) by exposing non-polar groups and the interfacial rearrangement from a β-sheet to linear and smaller crystal structure, leading to an enhanced foaming capacity. Microstructural analysis revealed that the higher dose irradiation (up to 5 kGy) could promote the proteins' oxidation of LEW alongside protein aggregates formed in the amorphous region, which favored heat-set gelation. As evidenced in microrheology, ≤3 kGy irradiation provided an improved viscoelastic interface film of LEW during gelatinization. Particularly, the LEW gel treated with 1 kGy irradiation had evident swelling resistance during the times of acidification at pH 1.2. These results gave new insight into the irradiation-assisted enhancement of foaming and heat-set gelation properties of LEW. [ABSTRACT FROM AUTHOR]

Copyright of Food & Fermentation Industries is the property of Food & Fermentation Industries and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

The bioavailability and quality attributes of egg white proteins (EWPs) are vital for food products' final form and nutritional content. Heat treatment negatively affects these attributes. We investigated EWP's functional, rheological, and structural characteristics using dielectric barrier discharge cold atmospheric plasma (DBD-CAP) for its advantages to address this. EWP was exposed to different DBD-CAP treatment times (0, 60, 120, 180, 240, and 300 s) at 40 kV. Assessing functional attributes revealed increasing solubility and decreasing turbidity with longer plasma treatment. As plasma treatment time increased, foam and emulsion stabilities and capacities improved, along with enhanced water and oil-holding capacities. DBD-CAP influenced EWP's rheological attributes, showing alterations between native and treated EWP, with no significant differences within plasma treatment times. EWP's unfolding was confirmed by increased lipid oxidation, carbonyl content, hydrophobicity, and decreased sulfhydryl group. Particle sizes and zeta potential of plasma-treated EWP decreased with treatment time. FTIR-ATR and CD analyses revealed DBD-CAP's impact on EWP's conformation. CD indicated modifications in the secondary structure, increasing α-helix, β-sheets, and β-turns and decreasing random coils. These findings suggest that plasma-induced mild oxidation enhances EWP's attributes and structure, potentially benefiting its utilisation in the food industry. [ABSTRACT FROM AUTHOR]

Summary: High internal phase emulsions (HIPEs) are potential carriers of fat‐soluble nutrients due to their high loading capacity. In this study, egg white protein particles (EWPP) and rhamnolipid (Rha) were used to co‐emulsify oil/water HIPEs to carry curcumin (Cur). The results showed that the Cur loading efficiency, microstructure, protein composition, molecular distribution of protein hydrolysates, protein interfacial adsorption rate and Cur bioavailability were measured. The results showed that, incorporation with Rha was unhelpful for improving loading efficiency of Cur, which decreased from 80.8% to 73.7% at pH 3.8 after incorporation with Rha, due to the decreased viscosity and destroyed continuous interface membrane, while beneficial for restricting coalescence of oil droplets. As studied, Rha could effectively reduce the droplet size to slow down the speed of coalescence and form EWPP–Rha complex to inhibit proteolysis. Finally, Cur bioavailability in EWPP–Rha co‐emulsified HIPE was the highest (40.3%), indicating the synergistic effect of EWPP and Rha promoting the effective adsorption of Cur, related to the increased coalescence stability during digestion and participation of Rha in the micellisation reaction. In comparison, fibrous (pH 3.8) and granular (pH 7.0) EWPP stabilised HIPEs, showed no obvious difference in Cur bioavailability, due to the balance between the interfacial adsorption ability and the digestion resistance of EWPP with various morphologies. This study has important significance for the construction of lipid soluble nutrient 'carriers' with high load and high bioavailability. [ABSTRACT FROM AUTHOR]

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Some bioactive substances in food have problems such as poor solubility, unstable chemical properties and low bioavailability, which limits their application in functional food. Recently, many egg white protein-based delivery carriers have been developed to improve the chemical stability, biological activity and bioavailability of bioactive substances. This article reviewed the structure and properties of several major egg white proteins commonly used to construct bioactive substance delivery systems. Several common carrier types based on egg white proteins, including hydrogels, emulsions, micro/nanoparticles, aerogels and electrospinning were then introduced. The biological functions of common bioactive substances, the limitations, and the role of egg white protein-based delivery systems were also discussed. At present, whole egg white protein, ovalbumin and lysozyme are most widely used in delivery systems, while ovotransferrin, ovomucoid and ovomucin are less developed and applied. Egg white protein-based nanoparticles are currently the most commonly used delivery carriers. Egg white protein-based hydrogels, emulsions, and microparticles are also widely used. Future research on the application of various egg white proteins in developed new delivery systems will provide more choices for the delivery of various bioactive substances. [ABSTRACT FROM AUTHOR]

Copyright of Transactions of China Pulp & Paper is the property of China Pulp & Paper Magazines Publisher and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Food foams are highly industrially relevant systems, responsible for the visual appearance and organoleptic properties of many processed foods. Foam characteristics can be further improved by food-grade additives. This study investigates the influence of bacterial cellulose (BC) on the foaming capacity (FC) and foam stability (FS) of egg white protein (EWP) and soy protein isolate (SPI), important food foaming agents. The effects of pH, BC concentration and particle size on the FS and FC were analyzed. Compared to SPI, EWP demonstrated higher FC, an effect that is tentatively assigned to its lower molecular weight, hence faster diffusion to the interface. Adding 0.1 % BC to EWP (4 %, at pH 7.0) and to SPI (4 %, at pH 3.0) increased the FC by 1.6 and 1.5 times, respectively. The addition of BC also reduced the foam's liquid drainage, although not impacting the FS. Surprisingly, large flakes of BC (Dv(50) of 1104 µm) yielded higher FC values than smaller ones. We hypothesize that larger BC flakes may act as anchoring sites, stabilizing the air bubbles during whipping. BC flakes were observed in the plateau borders and nodes of EWP foams, clogging the water channels and preventing drainage. This work demonstrates the potential of BC as a food-grade foam enhancer, providing a new tool for the food engineer´s arsenal.

In this study, the moderation–excess interaction of epigallocatechin gallate (EGCG) and calcium ions (Ca2+) to the gelation performance of transparent egg white protein (EWP) gel (EWG) was explored. The oxidation of EGCG introduced a yellowish-brown EWG, whereas the weakening of Ca2+ ionic bonds caused a notable reduction in the hardness of EWG, from 120.67 g to 73.57 g. Achieving the optimal EGCG-to-Ca2+ ratio in EWG conferred enhanced water-holding capacity to 86.98%, while an excess of EGCG attributed to the creation of a three-dimensional structure within the void “walls”. The elevated presence of EGCG influenced the ionic bonds and hydrophobic interactions, thereby presenting a moderate–excess relationship with sulfhydryl and disulfide bonds, β-sheet, and α-helical structures. Notably, EGCG reduced the digestibility of EWG to 50.06%, while concurrently fostering the creation of smaller particle sizes. This study provides a scientific basis for the controllable preparation and quality regulation of transparent EWG.

Egg plays an important role in the food processing due to the high nutritional value,functional properties and participation in nonenzymatic browning reactions to enhance the aroma Egg plays an important role in the food processing due to the high nutritional value, functional properties and participation in nonenzymatic browning reactions to enhance the aroma and taste of the products. In this study, the effect of ultrasound power (0, 100, 200, 300, and 400 kW) on physicochemical and functional properties such as solubility, foaming properties, emulsifying properties, water and oil absorption capacity, viscosity, and particle size of freeze dried egg white powder was investigated in a completely randomized design with a 95% confidence level. The results showed that the foaming capacity of egg white powder ultrasonicated with the power of 300 and 400 kW increased compared to the control. The emulsifying activity and foam stability of the egg white powder ultrasonicated did not change compared to the control. Ultrasound and increasing its power had no significant effect on the solubility and viscosity of egg white powder. Egg white powder particle size was reduced at higher ultrasound powers (400 kW). The highest water absorption capacity and the lowest oil absorption capacity were related to egg white powder ultrasonicated with a power of 100 kW. Overall, the use of ultrasound was effective in improving the functional properties of egg white powder. In general, the application of high power ultrasound (300 and 400 kW) increased the ability to produce foam. Increasing the ultrasound power from 100 to 400 kW caused a significant reduction in the size of egg white powder particles.

Egg white protein is a high-quality protein with high nutritional value and a variety of functional properties. The oligosaccharide can be covalently bound to the egg white protein through the glycosylation reaction, and the functional properties of the conjugates were improved compared with the natural egg white protein. In this review, the gel mechanism of oligosaccharide-egg white protein conjugates was reviewed, and the influencing factors of oligosaccharide-modified egg albumin gels were discussed. Moreover, effects of oligosaccharides on the functional properties of egg albumins were summarized, and the processing and application of oligosaccharide-modified egg albumin were prospected. [ABSTRACT FROM AUTHOR]

Egg white protein has gelatinous, foaming, and emulsifying properties. In production and processing, the gelatinous properties and gelatinous stability of egg white protein are usually improved by modifying treatment. This paper reviewed the modification methods of egg white protein and the research status of the application of modified egg white protein in meat processing and prospected the innovation and application of modified egg white protein.

As a natural cationic peptide, Nisin is capable of widely inhibiting the growth of Gram-positive bacteria. However, it also has drawbacks such as its antimicrobial activity being susceptible to environmental factors. Nano-encapsulation can improve the defects of nisin in food applications. In this study, nisin-loaded egg white protein nanoparticles (AH-NEn) were prepared in fixed ultrasound-mediated under pH 3.0 and 90 °C. Compared with the controls, AH-NEn exhibited smaller particle size (112.5 ± 2.85 nm), smaller PDI (0.25 ± 0.01), larger Zeta potential (24 ± 1.18 mV), and higher encapsulation efficiency (91.82%) and loading capacity (45.91%). The turbidity and Fourier transform infrared spectroscopy (FTIR) results indicated that there are other non-covalent bonding interactions between the molecules of AH-NEn besides the electrostatic forces, which accounts for the fact that it is structurally more stable than the controls. In addition, by the results of fluorescence intensity, differential scanning calorimetry (DSC), and X-ray diffraction (XRD), it was shown that thermal induction could improve the solubility, heat resistance, and encapsulation of nisin in the samples. In terms of antimicrobial function, acid–heat induction did not recede the antimicrobial activity of nisin encapsulated in egg white protein (EWP). Compared with free nisin, the loss rate of bactericidal activity of AH-NEn was reduced by 75.0% and 14.0% following treatment with trypsin or a thermal treatment at 90 °C for 30 min, respectively.

Ionizing radiation has its unique popularity as a non-thermal decontamination technique treating with protein-rich foodstuffs to ensure the microbial and sensory quality, particularly for shell eggs. However, the changes in the functional properties of egg protein fractions such as liquid egg white (LEW) with macro/microstructural information are still controversial. Hence, this study was designed to elaborate the foaming and heat-set gelation functionality of LEW following different γ-ray irradiation dose treatments (0, 1, 3 or 5 kGy). For such, the physicochemical properties (active sulfhydryl and the hydrophobicity of protein moieties), structural characteristics (through X-ray diffraction, Fourier-transform infrared spectroscopy and differential scanning calorimetry) and interfacial activities (rheological viscosity, interfacial tension, microrheological performance) were investigated. Then, the thermal gelation of LEW in relation to the texture profile and microstructure (by means of a scanning electron microscope) was evaluated followed by the swelling potency analysis of LEW gel in enzyme-free simulated gastric juice. The results indicated that irradiation significantly increased the hydrophobicity of liquid egg white proteins (LEWPs) (p < 0.05) by exposing non-polar groups and the interfacial rearrangement from a β-sheet to linear and smaller crystal structure, leading to an enhanced foaming capacity. Microstructural analysis revealed that the higher dose irradiation (up to 5 kGy) could promote the proteins’ oxidation of LEW alongside protein aggregates formed in the amorphous region, which favored heat-set gelation. As evidenced in microrheology, ≤3 kGy irradiation provided an improved viscoelastic interface film of LEW during gelatinization. Particularly, the LEW gel treated with 1 kGy irradiation had evident swelling resistance during the times of acidification at pH 1.2. These results gave new insight into the irradiation-assisted enhancement of foaming and heat-set gelation properties of LEW.

The present work demonstrates the effect of hydrodynamic cavitation (HC) (2 mm Orifice plate) as a pretreatment for egg white protein hydrolysates (EWPH) production. The obtained EWPH was evaluated for various physiochemical (degree of hydrolysis), functional (emulsifying, foaming), structural and nutritional properties (antioxidant activity and in-vitro digestibility). The egg white solutions (5% solid content) were pretreated for 10, 15 and 20 min with HC and later hydrolyzed using papain enzyme for 90 min. The structural analysis revealed that HC unfolded the protein structure which was confirmed through the formation of β-sheet (from 15 to 46%) and loss of α-helix (34 to 14%) content with increasing treatment time. Through the exposure of hydrophobic bonds, the degree of hydrolysis and surface hydrophobicity increased, which eventually improved the nutritional and functional properties of EWPH. The HC-15 min treated samples had the highest zeta potential (-25.4 mV) with the lowest average particle size (346.5 nm) and denaturation temperature (70.67°C). Further increase in treatment time led to instability of hydrolysates. HC effectively improved the functional and nutritional properties of EWPH and a treatment time of 15 min is recommended for obtaining EWPH with improved properties.

The influence of pH, temperature, biopolymer ratio, total concentration, and ionic concentration on the interaction between egg white protein (EWP) and chitosan (CS) was investigated through turbidity, zeta potential, and state diagram in our research. In addition, phase behavior was observed under various conditions. The turbidity of EWP remained low (turbidity

Copyright of Journal of Research & Innovation in Food Science & Technology is the property of Research Institute of Food Science & Technology and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

The partial substitution of animal protein by plant protein is a new opportunity to produce sustainable food. Hence, to control the heat treatment of a composite protein ingredient, this work investigated the thermal behavior of mixtures of raw egg white (EW) and a laboratory-prepared pea protein isolate (PPI). Ten-percentage-by-weight protein suspensions prepared with different PPI/EW weight ratios (100/0, 75/25, 50/50, 25/75, 0/100) at pH 7.5 and 9.0 were analyzed by differential scanning calorimetry (DSC) and dynamic rheology in temperature sweep mode (T < 100 °C). The DSC data revealed changes in the thermal denaturation temperatures (Td) of ovotransferrin, lysozyme, and pea legumin, supposing interactions between proteins. Denaturation enthalpy (∆H) showed a high pH dependence related to pea protein unfolding in alkaline conditions and solubility loss of some proteins in admixture. Upon temperature sweeps (25–95 °C), the elastic modulus (G′) of the mixtures increased significantly with the EW content, indicating that the gel formation was governed by the EW protein. Two thermal sol–gel transitions were found in EW-containing systems. In particular, the first sol–gel transition shifted by approximately +2–3 °C at pH 9.0, probably by a steric hindering effect due to the presence of denatured and non-associated pea globulins at this pH. [ABSTRACT FROM AUTHOR]

Using egg white proteins as raw materials (EWPs), this study investigated the effects of glactooligosaccharides (GOS)-induced protein glycosylation by hydrothermal processing on the gelling properties and gel microstructures of EWPs, and characterized the gelling mechanisms. This article first studied the effects of GOS amounts and hydrothermal conditions on the hardness and elasticity of EWP-GOS conjugates (EGCs), then assessed the color differences, water-holding capacity, rheology, intermolecular forces and microstructure of EGCs using low-field nuclear magnetic resonance, rheometer, Fourier transform infrared spectroscopy and scanning electron microscope. The results showed that, GOS addition and heat induction conditions could significantly (P

A new antifreeze agent was prepared from Egg White Protein (EWP) and β-Cyclodextrin (β-CD). Through single factor experiments and response surface test, the preparation conditions of EWP-β-CD complex with the best antifreeze activity were obtained. Then EWP-β-CD complex with different concentrations (2%, 4% and 6%) was applied to the four freeze-thaw cycle system of shrimp to study the antifreeze protection of EWP-β-CD complex on shrimp. The results showed that the optimum conditions for the preparation of EWP-β-CD composite system were pH7.0, the composite ratio of β-CD and EWP 1:10, the heat treatment temperature 75 ℃. The antifreeze activity of EWP-β-CD composite system was 84.09%±1.06% under the optimal conditions. The EWP-β-CD complex under this condition was applied to the freeze-thaw cycle of shrimp. After adding EWP-β-CD complex, the water retention, hardness and chewability of shrimps were significantly improved, and the chromaticity of shrimps was not significantly affected. When the addition of EWP-β-CD complex was 4% and 6%, the effect of EWP-β-CD complex on protein degradation and fat oxidation of shrimp was significantly better than that of commercial antifreeze. The preparation conditions of EWP-β-CD complex are optimized by response surface method, and it was preliminarily showed that it had a certain protective effect on the quality of shrimp. This result would provide a theoretical basis for the subsequent development of low sweetness and low calorie antifreeze.

Abstract Gluten and gums are usually used in veggie sausage for textural purposes; however, they are not label‐friendly for consumers with gluten sensitivity or consumers looking for clean‐label foods. Therefore, two commercial egg white proteins (P110 and M200) were studied at different levels (0%–10%) to substitute gluten or xanthan gum. The veggie sausages were subjected to color, texture, length, and weight loss evaluations. M200 significantly improved the texture of sausages and exhibited the most similar texture profile as a commercial meat sausage. The overall texture‐enhanced capability of gel materials was ranked in the order of 5% M200 > 5% P110 ≥ 3% Gluten ≥ 1.3% Xanthan Gum. Egg white proteins did not significantly affect the color, length, and weight loss of sausages. Raman spectra revealed that M200 gel had a higher α‐helix structure than P110 gel, which indicated that M200 formed an ordered gel by reforming tyrosine at Raman shift 833 and 860 cm−1 inside while P110 formed a disordered gel by exposing tyrosine. This study demonstrated that M200 would substitute both the gluten and xanthan gum for improving the texture of veggie sausages. The findings may also be applied to other meat analogs targeting gluten‐free and label‐friendly purposes.

In this study, whey protein concentrate (WPC) and egg white protein (EWP) were used as film forming substrates and 5 U/g protein transglutaminase (TG) was added to prepare WPC/EWP composite film. The effects of the mass ratio of WPC and EWP, pH of film-forming solutions and glycerin content on the properties of WPC/EWP composite film were investigated. Result showed that, when the mass ratio of WPC/EWP was 1:3, the pH of the film-forming solutions was 8, and the glycerol content was 35%. The results of electron microscope showed that the structure of composite film was compact without porosity. The infrared results showed that WPC and EWP had good compatibility. The water vapor permeability of WPC/EWP composite film was 2.08×10−10 g·s−1m−1Pa−1, the transmittance was 73.90%, the tensile strength was 1.60 MPa, and the elongation at break was 151.96%. WPC, EWP and glycerol had good fusion at pH8, which could significantly (P

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Frozen storage can greatly improve the shelf life of fresh egg white protein (EWP), but it will also lead to the reduction of protein foaming and can not meet the application needs. Herein, high-intensity ultrasound (HIUS) was used to improve the foam characteristics of EWP in different frozen storage periods. The results showed that compared with fresh egg white, the foaming ability of EWP with different freezing times (0, 3, 7, 14, 21 days) after HIUS treatment (20 kHz, 60% amplitude, 5 min) was significantly improved, especially the EWP after 21 days of frozen storage was doubled by HIUS induction. Furthermore, it was found that the improvement of EWP foamability was mainly due to the enhancement of surface hydrophobicity (H0, the value from 263 to 456) and the decrease of apparent viscosity (from 0.506 Pa.s to 0.007 Pa.s), which increased the diffusion rate of protein to the interface (from 0.19 mNm− 1s− 0.5 to 0.26 mNm− 1s− 0.5) and its adsorption amount (from 35.8 to 43.3%) at the interface. These results showed that HIUS was a simple, efficient and residue free way to improve the foam characteristics of frozen EWP, which has strong promotion and application value. [ABSTRACT FROM AUTHOR]

In this study, oleogels were prepared by the emulsion-template method using egg-white protein microgel as a gelator and xanthan gum (XG) as thickener. The physicochemical properties of the emulsion and oleogels were investigated. The adsorption of protein on the surface of the oil droplet reached saturation when the protein microgel concentration reached 2%. The excess protein combined with XG and accumulated on the outer layer of the oleogel, which prevented the emulsion from flocculation, enhanced the oil-holding capacity of the oleogel, and had a positive effect on preventing the oxidation of oil. When the concentration of XG was less than 0.4%, the EWP microgel, combined with the XG, stabilized the emulsion. As the concentration of XG was greater than 0.4%, excessive XG in the emulsion improved the viscosity and mechanical properties of the emulsion to prevent the aggregation of oil droplets. However, the change in XG concentration had no significant effect on the oxidation of the oil. [ABSTRACT FROM AUTHOR]

The study investigated the effects of different microwave vacuum freeze-drying powers (100–500 W) on the emulsifying properties and structural characteristics of egg white protein, which is of great significance in enhancing the added value of EWP and promoting its application. Emulsification analysis revealed that the emulsification performance was significantly influenced by microwave power and reached its maximum at 300 W. Fourier-transform infrared spectroscopy (FT-IR) and sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS-PAGE) analyses showed that microwave vacuum freeze-drying treatment altered the secondary structure of EWP without changing its peptide structure. Fluorescence measurements indicated that the maximum fluorescence emission intensity decreased, and the maximum emission wavelength shifted towards blue as the power increased. Particle size, zeta potential, scanning electron microscopy (SEM), and differential scanning calorimetry (DSC) analyses showed that the average particle size of EWP reached the minimum value of 1203.66 nm, the absolute value of zeta potential reached the maximum value of 41.35 mV, and the thermal stability was strongest, with a more uniform and loose structure observed at 300 W. Texture profile analysis (TPA) showed that appropriate power treatment significantly enhanced the chewiness and viscoelasticity of egg white protein. Therefore, appropriate power treatment could effectively improve the emulsifying properties and stability. [ABSTRACT FROM AUTHOR]

The study aimed to investigate the effect of high intensity ultrasonic (HIU) treatment at different times (0, 10, 20, and 30 min) on the structure and gel properties of water‐soluble potato protein isolate (WPPI) and to further investigate the improvement of gel properties of ultrasonicated WPPI (UWPPI) by the addition of egg white protein (EWP). HIU reduced the particle size of WPPI, whose structure became loose and disordered, which improved gelling properties of UWPPI. Fourier transform infrared results indicated that α‐helix content decreased, whereas the proportion of irregular curl increased with the increase in ultrasonication time (0–20 min), indicating that the initially ordered structure of UWPPI became disordered. After HIU treatment, the free sulfhydryl groups of UWPPI and surface hydrophobicity decreased and fluorescence intensity increased. These results demonstrated that the HIU loosened the structure of UWPPI, exposing more chromogenic groups while embedding more hydrophilic groups. After thermal induction, UWPPI gel hardness increased and exhibited excellent water holding capacity. After the addition of EWP, rheological properties stabilized, and the hardness of UWPPI‐EWP gels increased significantly, forming internally structured protein gels with a tightly ordered structure and increased brightness. Thus, HIU changed the structure and gelling properties of WPPI, and the addition of EWP further enhanced the performance of hybrid protein gels. Practical Application: High intensity ultrasonic changed the structure of water‐soluble potato protein isolate (WPPI) and improved the properties of WPPI gels. The addition of egg white protein significantly improved the quality of mixed protein gels which showed great potential industrial value. [ABSTRACT FROM AUTHOR]

Copyright of Food & Machinery is the property of Food & Machinery Editorial Office and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Abnormal skin pigmentation commonly occurs during the wound healing process due to the overproduction of melanin. Chicken egg white (CEW) has long been used to improve skin health. Previous published works had found CEW proteins house bioactive peptides that inhibit tyrosinase, the key enzyme of melanogenesis. The current study aimed to evaluate the anti-pigmentation potential and mechanism of the CEW-derived peptide (GYSLGNWVCAAK) and hydrolysates (CEWHmono and CEWHdi), using a cell-based model. All of these peptide and hydrolysates inhibited intracellular tyrosinase activity and melanin level up to 45.39 ± 1.31 and 70.01 ± 1.00%, respectively. GYSLGNWVCAAK and CEWHdi reduced intracellular cAMP levels by 13.38 ± 3.65 and 14.55 ± 2.82%, respectively; however, CEWHmono did not affect cAMP level. Moreover, the hydrolysates downregulated the mRNA expression of melanogenesis-related genes, such as Mitf, Tyr, Trp-1 and Trp-2, but GYSLGNWVCAAK only suppressed Tyr gene expression. Downregulation of the genes may lower the catalytic activities and/or affect the structural stability of TYR, TRP-1 and TRP-2; thus, impeding melanogenesis to cause an anti-pigmentation effect in the cell. Outcomes from the current study could serve as the starting point to understand the underlying complex, multifaceted melanogenesis regulatory mechanism at the cellular level. [ABSTRACT FROM AUTHOR]

As a natural emulsifier, egg white protein (EWP) has great interfacial characteristics and high security, and has broad development prospects. This study explored the impact of ultrasound synergized citral (CI) treatment on the microstructure, molecular flexibility and emulsifying property of EWP, and predicted the interaction between CI and ovalbumin (the main protein in EWP) through molecular docking. The decrease in free amino content and the growth in molecular weight of EWP suggested that CI and proteins were successfully grafted. The results of physicochemical properties revealed that UCEWP (ultrasound synergized citral-treated EWP) had smaller particle size and larger ζ-potential absolute value, which meant that the stability of UCEWP system was enhanced. From the perspective of interfacial characteristics, UCEWP had lower interfacial tension, which remarkably improved its emulsifying property. The emulsifying activity index (EAI) and emulsifying stability index (ESI) of UCEWP were 1.99 times and 3.19 times higher than that of natural EWP (NEWP). Analysis of Fourier transform infrared spectroscopy (FT-IR) and fluorescence spectroscopy illustrated that the secondary and tertiary structures of UCEWP were more disordered and stretched than those of EWPs. Protein microstructure demonstrated that UCEWP presented loose small particle distribution, and correlation analysis reflected that the improvement of molecular flexibility was positively correlated with the enhancement of emulsifying property. These results elucidated that ultrasound synergized CI treatment is an effective mean to improve the molecular flexibility and emulsifying property of EWP, which provides a valuable reference for further application of EWP. [ABSTRACT FROM AUTHOR]

Tailoring food-grade high-internal-phase Pickering emulsions (HIPPEs) with desired applicability has been extremely hindered due to the limited stabilization mechanism deciphering. This study illustrated the specific role of egg white protein (EWP) particlesꞌ structure and interface distribution to the stabilization of HIPPEs. Herein, gelation induced EWP aggregation into its microgel particles (EWPG) with apparent conformation transition (α-helix to β-sheet) and surface activity improvement (e.g., hydrophobicity, interface tension, and wettability). Besides, larger EWPG tended to sparsely absorb on the HIPPEsꞌ interface and achieve admirable long-term stability (6-month storage and 18-days lipid oxidation), owing to higher particle rigidity and steric repulsion. Comparably, EWP (small, soft, and rough) was superior in ready-to-use HIPPEs with centrifugation, freeze-thawing, and nutraceutical delivery demands, accompanied by a stronger rattan-like interfacial network with higher viscoelasticity. Overall, this research would facilitate the facile design of food matrices (e.g., EWP)-based HIPPEs via the gelation-tailored balance of particle structure and interface distribution. • EWPG with larger protein aggregates tended to form a sparse interfacial film. • EWPG (large, rigid, and smooth) could stabilize HIPPEs with long-storage demands. • Rattan-like EWP network improved viscoelasticity and bioaccessibility of HIPPEs. • EWP (small, soft, and rough) was more suitable in forming ready-to-use HIPPEs. • Complex processing could be a double-edged sword for EWP in forming HIPPEs. [ABSTRACT FROM AUTHOR]

Schematic diagram of the effects of different ultrasonic intensities on alkali-induced EWP gel. [Display omitted] • Moderate ultrasonic improved gel strength, while excessive ultrasonic did not achieved. • Ultrasonics affected the molecular properties and aggregation of alkali-induced egg white protein. • Ionic bond facilitate aggregation of egg white protein molecules for initial gelling. • Disulfide bond stabilized cross-linking among proteins molecular during gel maturation. • The formation of ionic bonds in gel was slightly inhibited by ultrasonic treatment. Egg white protein can be cross-linked to form a gel under alkali induction, which is typically represented by the preserved eggs from Chinese traditional food. The effects of ultrasonic at different intensities (50 W, 100 W, 200 W, and 300 W) on alkali-induced egg white protein (EWP) gel were investigated. The gel strength rose significantly by 26.08 % upon treatment with 50 W, but it gradually declined as the intensity increased. Meanwhile, the structure unfolding and molecular aggregation of EWP were affected by ultrasonic. Compared with 300 W, 50 W could enhance surface hydrophobicity and decrease total free sulfhydryl group content more during gel formation. Selective solubility experiment confirmed that ultrasonic reduced the formation of ionic bonds, which slightly slowed down the initial gelation. Simultaneously, 50 W promoted the formation of more disulfide bonds, which helped to improve the strength of the final gel, while the same effect was not observed at 300 W. In general, moderate ultrasonic can effectively improve the alkali-induced EWP gel properties, which provides theoretical support for developing high quality preserved eggs and protein gel foods. [ABSTRACT FROM AUTHOR]

[Display omitted] • Sodium alginate (SA) and egg white protein (EWP) were combined added to myofibrillar protein (MP). • The combined utilization of SA and EWP significantly improved the MP gel quality. • The SA/EWP/MP composite gel possessed excellent rheological properties. • The addition of SA and EWP reduced the α-helix while increasing the β-sheet. • An SA:EWP of 2:1 promoted more uniform and denser microstructure. This research explored the influence of varying sodium alginate (SA) and egg white protein (EWP) ratios (1:2, 2:3, 1:1, 3:2, 2:1, v/v) on the structural and gel characteristics of chicken myofibrillar protein (MP) gels. The findings showed that containing SA and EWP significantly improved (P < 0.05) the water-holding capacity (up to 95.02 %) and whiteness of MP gels. With a 2:1 ratio of SA to EWP, the absolute value of zeta potential reached 17.3 mV, and the lowest cooking loss (16.98 %) was achieved, accompanied by a reduction in turbidity. The MP formulation incorporating a 2:1 ratio of SA to EWP demonstrated the highest hardness, chewiness, cohesiveness, and springiness (P < 0.05), as confirmed by the rheological analysis conducted under temperature sweep mode. As the SA content increased, there was a notable enhancement in both the storage modulus (G′) and loss modulus (G″) of MP gel, indicating a strengthened cross-linking effect within the MP protein gel. FTIR and SEM analyses revealed a transformation from α-helix to β-sheet and the formation of a more uniform and dense gel structure due to non-covalent interactions. Overall, MP incorporating SA/EWP at a 2:1 ratio (v/v) has preferable gel properties. This study could provide a theoretical reference to enhance the gel attributes of chicken meat products in the industry through the utilization of SA and EWP. [ABSTRACT FROM AUTHOR]

Edible films are effective alternatives to plastic packaging, however, the hydrophilicity of edible films based on protein and polysaccharide limits the application. Therefore, we fabricated a water-stable hybrid film with a linear-spherical interpenetrating molecular topology network using egg white (EW), chitosan (CS), and pectin. Meanwhile, the nisin-tannin acid self-assembly complex nanoparticles were employed as a multifunctional cross-linker, antibacterial and antioxidant agent to improve the performance of films. The FTIR, XRD, and SEM analysis revealed that the conformation and crystalline structure rearrangement of chitosan induced by the alkaline environment provided by egg white enhanced the network structure of films, effectively avoided the addition of modifying reagents. The proposed hybrid films exhibited excellent properties, with EW/TNPCS3 showing the best overall performance. The water contact angle (WCA) increased to 105.27 ± 1.62°, and its dissolution and swelling rates were significantly lower than pure egg white and pure chitosan films. Moreover, tannin-nisin (TN) nanoparticles endowed the films with excellent antimicrobial activity against the common Gram-positive (Staphylococcus aureus) and Gram-negative (Escherichia coli) bacteria. Thus, the prepared blending films have great application potential in food preservation, especially to maintain stable performance in high humidity environment. • Egg white/chitosan/pectin blending film holds a markedly increased water resistance. • Alkaline environment of egg white induced conformational rearrangement of chitosan. • Antibacterial-antioxidant nanoparticles endowed the blending film great bioactive. • Multifunctional nanoparticles cross-linked the interpenetrating polymer network. [ABSTRACT FROM AUTHOR]

With the increasing number of children allergic to egg worldwide, there is an urgent need to develop strategies for effectively utilizing egg protein. As a novel food processing that can effectively reduce allergenicity and enhance protein quality and functional properties, cold plasma (CP) is gaining attention. The study investigated the impacts of the dielectric barrier discharge CP on the immunoreactivity, in vitro digestibility, functional properties, and structural changes of egg white protein (EWP). The results showed that the EWP treated with CP for 30 min had a significant decrease in immunoglobulin (IgG)-binding capacity by approximately 20% and improved in vitro digestibility. Further studies demonstrated that the decrease in the IgG-binding capacity of EWP correlated well with the alterations in the secondary and tertiary structures. The content of α-helix was decreased by 6.5% and the surface hydrophobicity increased by 2.5 folds after the 30-min treatment, compared with the untreated samples. The oxidation of peptide amino groups induces structural changes, accompanied by the oxidation of amino acid residues. This phenomenon has been validated through surface hydrophobicity and multispectral analysis. Additionally, CP also improved the foaming and emulsifying capacity of EWP by 140% and 8.03%, respectively. These findings suggest that CP treatment could be served as a potential technology to reduce the immunoreactivity, and improve the in vitro digestibility and functionality of EWP. • The effect of CP on immunoreactivity, digestibility, structure, and function of EWP was studied. • IgG binding capacity of EWP after CP treatment was decreased by 20%. • Immunoreactivity reduction in EWP was attributed to protein structural changes. • The plasma oxidation improved in vitro digestibility of EWP. • CP treatment significantly improved the foaming and emulsifying capacity of EWP. [ABSTRACT FROM AUTHOR]

The effects of lysozyme on egg white gel properties and their underlying causes were investigated under comparison between lysozyme removed with ion exchange resin and three levels of commercial lysozyme powder (1/2, 2/2, 3/2 the natural concentration in egg white) re-added in the lysozyme-removed system. Results showed that a lysozyme-removed gel obtained the best water holding capacity (61.61 %), lowest cooking loss (11.85 %), and enhanced textural properties (hardness, 638.04 g; resilience, 0.57; and gumminess), which was attributed to lysozyme promoting protein aggregation and weakening electrostatic repulsion by charge neutralization and competition for water, and this could be eliminated by removing lysozyme. Besides, the stronger intermolecular interactions (enhanced ionic bonds, hydrogen bonds and inhibited hydrophobic interactions), the shorter transverse relaxation time (T 21 and T 22), as well as more uniform microstructure formed in the lysozyme-removed gel, allowing the gels to bind more water molecules. With return of lysozyme, the gel properties were weakened to varying degrees, which was also ascribed to the filling of lysozyme in gel matrix narrowed interspace for binding and storage of water. In sum, adjustment on the content of lysozyme can regulate the gel properties of egg white, so as to obtain gels with regulable gel quality and processing characteristics. [Display omitted] • Egg white gel obtained the best water holding capacity(WHC) with lysozyme removed. • Lysozyme deteriorated egg white gel properties by promoting protein aggregation. • Excess lysozyme decreased the WHC by filling in its matrix, reducing water storage. • Egg whites can obtain better gel properties by adjusting lysozyme. [ABSTRACT FROM AUTHOR]

The interactions of chicken trachea collagen hydrolysate (CTH) obtained from the enzymatic hydrolysis of by-products from a chicken slaughterhouse, with two common proteins (egg white (E) and whey (W) proteins) was studied with and without sodium chloride (NaCl). The treatments with two protein types (E and W at 10% w/w) and different CTH concentrations (0, 0.25, and 0.5% w/w) and NaCl concentrations (0 and 1.5% w/w) were conducted. The addition of CTH reduced the emulsifying and foaming properties of those proteins due to their fibrillar structure, while the addition of NaCl promoted the foaming capacity. Moreover, CTH and NaCl promoted the gelling properties of those proteins, as revealed by the shift-up of the storage modulus (G′) value. The rapid shifting at 60–70 °C indicated that the heat-set gelation was observed. The strong gel strength was exhibited with the mixture containing W. The addition of 1.5% w/w NaCl improved the antioxidant and antihypertensive activities of the mixture of 0.5% w/w CTH and 10% w/w W. The best DPPH, ABTS, and FRAP radical-scavenging activities (40.00, 180.95, and 46.00 TEAC µM/mL, respectively) and the lowest IC50 value of the ACE inhibitor (30.05 mg/mL) was revealed. This mixture exhibits the highest inhibitory activity and is suited for improving the functionalities of high-protein products. [ABSTRACT FROM AUTHOR]