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Food packaging plays a crucial role in the food supply chain by aiding in food preservation and reducing food losses throughout the distribution process. The extensive, unregulated utilization, and waste mismanagement of food packaging materials made up of conventional petroleum-based plastics has led to a significant environmental crisis. Egg components-based food packaging has attracted considerable attention from the global packaging industry as a viable alternative to synthetic polymers due to its biodegradability, sustainability, and health-related benefits. This comprehensive review explores the composition and properties of egg components (eggshell, eggshell membrane, egg white, and egg yolk), and recent advancements in biodegradable packaging films derived from them. Additionally, it introduces the characteristics of these films and their applications in food, highlighting their biodegradability, sustainability, and suitable mechanical, barrier, thermal, optical, antioxidant, and antimicrobial properties as substitutes for traditional synthetic polymers. The utilization of various egg components in the packaging industry is a safe, non-toxic, cost-effective, and economical approach. However, it was found that incorporating active compounds from natural sources into packaging films, as well as composite films composed of egg components combined with other biopolymers, resulted in superior properties, compared to single component films. Moreover, the application of novel technologies in film development has proven to be more effective than conventional methods. These innovative egg components-based packaging films can be optimized and commercialized for use as packaging materials for food products., (© 2024 The Author(s). Comprehensive Reviews in Food Science and Food Safety published by Wiley Periodicals LLC on behalf of Institute of Food Technologists.)

Embryonic mortality is a significant problem in the commercial duck industry worldwide. Therefore, identification of new biomarkers for duck embryo development is necessary. In the chicken (order Galliformes), we previously showed that chemerin is a hormone locally produced by the reproductive tract in hens, particularly in the magnum area, leading to its accumulation in the egg white and within the embryo annexes during embryonic development. We therefore hypothesized that the chemerin concentration in egg white could be a biomarker of egg performance and reproductive parameters in Pekin ducks (order Anseriformes). Thus, we collected eggs from Pekin ducks over a 5-d period at three stages of the laying period (before the laying peak, after the laying peak, and at the end of the laying period) to measure the chemerin concentrations in egg white by enzyme-linked immunosorbent assay. The chemerin concentration in egg white decreased during the laying period and was not associated with reproductive parameters. We found negative correlations between the chemerin level in egg white and the albumen weight. Reverse-transcriptase quantitative polymerase chain reaction showed that chemerin and its three receptors CMKLR1, GPR1, and CCRL2 were expressed in the reproductive tract and within allantoic and amniotic annexes during embryo development. Chemerin concentrations strongly increased in amniotic fluid on embryonic day 16 (ED16) when the egg white was transferred into the amniotic sac. Finally, chemerin inhibition in egg white by in ovo injections of anti-chemerin antibodies (0.01, 0.1, and 1 µg) increased the embryo mortality rate. These data demonstrate the important role of the chemerin system during egg formation and embryo development in Pekin ducks, suggesting their potential use as biomarkers for determining the quality of poultry eggs and embryo development., Competing Interests: DISCLOSURES The authors declare no conflicts of interest., (Copyright © 2024 The Authors. Published by Elsevier Inc. All rights reserved.)

Pasteurization is an effective sterilization technique for the treatment of liquid egg white (LEW), but the pasteurization temperature is generally limited because increased temperature can lead to aggregation of the proteins and affect their processing properties. In this study, phosphorylation modification was used to increase the thermal stability and pasteurization temperature of LEW, aiming to enhance the pasteurization sterilizing effect. The FT-IR results showed that the phosphate groups were successfully grafted into protein molecules, improving the order degree of protein molecules. In this case, the pasteurization temperature of LEW increased from 58 °C to 61 °C, without accompanying thermal aggregation. The molecular structural results suggested that the enhanced thermal stability was attributed to the decreased average particle size and the increased electrostatic repulsion between protein molecules, which largely reduced the turbidity of LEW during pasteurization treatment. Meanwhile, this process was dominated by noncovalent interactions (hydrophobic interactions and hydrogen bonding). Furthermore, the phosphorylation modification can synchronously improve emulsifying and foaming properties of LEW. Therefore, this work suggested that phosphorylation has great potential to improve thermal stability and pasteurization temperature of LEW, which can be utilized to extend its sterilizing effect and shelf life., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 Elsevier B.V. All rights reserved.)

This work presents a novel use of fibrous egg white protein (FEWP) in food preservation and nutraceutical applications. In this study, food-grade FEWP was used as an encapsulating material, along with chitosan (CS), to stabilize emulsions. The emulsion system was then used as a delivery system to improve the stability of retinyl acetate (RA). The structural and functional properties, as well as the stability and rheological behavior of the FEWP/CS copolymer, was investigated. The stability of RA-enriched emulsions was also evaluated. FEWP and CS stabilized emulsions exhibited smaller particle size and enhanced stability against different ionic strengths and storage periods. Additionally, RA-encapsulated emulsions stabilized by FEWP:CS (25:1 w/w) effectively inhibited apple browning. This study provides a promising strategy for delivering antioxidant components, highlighting its potential in food preservation and nutraceutical applications., Competing Interests: Declaration of competing interest The authors declare that they have no conflict of interest., (Copyright © 2024 Elsevier Ltd. All rights reserved.)

Background: In the quest for sustainable food ingredients, the present study delves into the potential of a tri-component hydrocolloid blend, comprising gellan gum (GG), soy protein isolate (SPI) and maltodextrin (MD), as a replacement for egg white in meringue production. The research aims to elucidate the intricate physical properties of meringue containing this tri-component structure, focusing on foaming dynamics, rheological behavior and the textural properties of the resulting meringue cookies., Results: Experiments were conducted with various hydrocolloids (k-carrageenan, GG, and locust bean gum) and GG was identified as optimal for improving foaming capacity and foaming stability. Rheological evaluations showed a positive correlation between increased GG concentration within the tri-component matrix and an increase in both storage modulus (G') and loss modulus (G"), indicating improved structural integrity. Furthermore, a comparative analysis of the texture profiles of cookies prepared with this blend highlighted the ability of higher GG concentrations to satisfactorily replicate the tactile and visual qualities of traditional egg white-based meringues. This result was particularly evident compared to formulations utilizing solely SPI or the combined SPI-MD configuration., Conclusion: Conclusively, the results of the present study highlight the significant potential of the GG-SPI-MD tri-component structure to closely mimic the critical properties of egg white, thus offering a promising plant-based alternative for meringue production. © 2024 Society of Chemical Industry., (© 2024 Society of Chemical Industry.)

There is currently a growing interest in health-promoting foods. The beneficial effects of food on human health are actively promoted by health professionals and nutritionists. This growing awareness is influencing the increasing range of functional foods and the pursuit of more innovative solutions. Recent research indicates that spherical nanoparticles have the potential to be used as functional biomaterials in the food industry, particularly for encapsulating hydrophobic natural phytochemicals. Techniques and systems based on micro- and nano-encapsulation are of great importance in the food and pharmaceutical industries. It is of paramount importance that encapsulation materials are safe for use in food. The aim of this study was to obtain micelles containing extracts from chokeberry fruit pomace using egg yolk powder (EYP) for emulsification (as a source of lecithin) and egg white powder (EWP) for stabilisation. The structural properties of the micelles in the resulting powders were characterised using Fourier transform infrared spectroscopy (FTIR). Scanning electron microscopy (SEM) analysis confirmed the presence of spherical micellar structures between 500 and 1000 nm in size. The water activity and water content of the obtained powders were determined, and the thermal (DSC) and antioxidant properties were investigated. The results indicated that the powder with the micellar structures had a higher stability compared to the powder obtained by simple mixing without the use of encapsulation techniques.

The substantial waste of perishable foods during transportation significantly contributes to greenhouse gas emissions, intensifying the climate crisis. To mitigate the rapid spoilage of fruits, an eco-friendly bilayer film was developed using natural egg white (EW), amylose (Am), and tannic acid (TA). The EW/Am-TA bilayer film features a primary layer of amphiphilic EW, ensuring a uniform coating on hydrophobic fruit surfaces, and a secondary layer composed of Am and TA, imparting notable tensile strength (5.3 ± 0.5 MPa) and elongation at break (28.5 ± 4.1 %). This bilayer film effectively shields fruits from UV-B and UV-C radiation (~0 % transmittance at 280 and 330 nm) and exhibits antioxidant and antibacterial properties due to the presence of TA. Fruits such as bananas, avocados, and cherry tomatoes, when dip-coated with the optimized EW/Am-TA bilayer, maintained their freshness, color, weight, and texture for up to seven days, demonstrating the effectiveness of this bilayer coating in food preservation. The natural materials in the coated film are edible and can be safely removed with tap water at room temperature in <10 s, posing no food safety risks. Thus, the proposed bilayer coating presents a significant solution to the global problem of food waste., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that may have influenced the work reported in this study., (Copyright © 2024 Elsevier B.V. All rights reserved.)

Ultrasound-induced egg white fluidic gels (UEFG) were prepared through ultrasonic pretreatment followed by subsequent heating. The optimal preparation parameters for UEFG were: ultrasonic power density between 0.2 to 0.8 W/mL, ultrasonic treatment time surpassing 150 s, heating temperature within 70 to 76°C, and heating time under 16 min. The prepared UEFG is a milky white solution with a viscosity lower than that of fresh egg white, and displayed a particle size distribution primarily between 100 and 1,200 nm. Stability assessments conducted over 28 d at 4°C revealed that UEFG remained stable at pH 6-10, with exceptional stability from pH 8 to 10, while it is less stable in highly acidic (pH 2-4) or basic environments (pH 12). The UEFG also showed commendable stability in the presence of salt and sucrose solutions. We report a simple and novel method for preparing UEFG with good flowability after heating treatment. The UEFG has broad applications in the food industry, such as precooked egg white powder, high protein beverages, composite dairy products, etc., Competing Interests: DISCLOURES The authors declare no conflicts of interest., (Copyright © 2024 The Authors. Published by Elsevier Inc. All rights reserved.)

The aim of this study was to elucidate the different effects and difference mechanism of gelling properties among egg white (EW) treated with different heating intensities and the composite addition of rhamnolipid and soybean lecithin. Particle size analyzer, potentiometric analyzer, surface hydrophobicity method, and Fourier transform infrared spectroscopy techniques were used to determine the physicochemical properties and molecular structure, respectively. Low-field nuclear magnetic resonance, magnetic resonance imaging, texture profile analysis, and scanning electron microscopy techniques were used to analyze the gelling properties and gel structure, respectively. And we illuminate the different mechanisms in the gelling properties of the EW with various treatments and key internal factors that play important roles in improving gelling properties by establishing the link between the gelling properties and relevant characteristics by mixed effects model and visual network analysis. The results indicate raising the content of rhamnolipid decreased the migration of immobilized water in the EW gel and the free water content. At the heating intensities of 55 °C/3.5, 65 °C/2.5, and 67 °C/1.5 min, with an increase in rhamnolipid, the gel's cohesiveness, gumminess, and chewiness gradually increased. The mixed effects model indicated that heating intensities and composite ratios have a 2-way interaction on zeta potential, the relaxation time of bound water (T 21 ), the content of bound water (P 21 ), the content of immobilized water (P 22 ), and fractal dimension (d f ) attributes (P < 0.05). The visual network analysis showed that the protein solubility, the relaxation time of immobilized water (T 22 ), surface hydrophobicity, zeta potential, average particle size (d 43 ) and the relaxation time of free water (T 23 ) are critical contributors to the different gelling properties of EW subjected to various treatments and the improvement of gelling properties. This study will provide theoretical guidance for the development of egg white products and the expansion of egg white's application scope in the egg product processing industry., Competing Interests: DISCLOSURES The authors declare no conflicts of interest., (Copyright © 2024 The Authors. Published by Elsevier Inc. All rights reserved.)

Pasteurization is necessary during the production of liquid egg whites (LEW), but the thermal effects in pasteurization could cause an unavoidable loss of foaming properties of LEW. This study intended to investigate the mechanism of pasteurization processing affects the foam performance of LEW. The foaming capacity (FC) of LEW deteriorated significantly (ΔFCmax = 72.33 %) and foaming stability (FS) increased slightly (ΔFSmax = 3.64 %) under different temperature-time combinations of pasteurization conditions (P < 0.05). The increased turbidity and the decreased solubility together with the decreased absolute value of Zeta potential indicated the generation of thermally induced aggregates and the instability of the protein particles, Rheological characterization demonstrated improved viscoelasticity in pasteurization liquid egg whites (PLEW), explaining enhanced FS. The study revealed that loss in foaming properties of PLEW resulted from thermal-induced protein structural changes and aggregation, particularly affecting FC. This provided a theoretical reference for the production and processing of LEW products., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 Elsevier Ltd. All rights reserved.)

Food proteins are considered an ideal source for the identification of bioactive peptides with the potential to intervene in nutrition-related chronic diseases such as cardiovascular disease, obesity, and diabetes. Egg white-derived peptides (EWPs) have been shown to improve glucose tolerance in insulin-resistant rats. However, underlying mechanisms are to be elucidated. Therefore, we hypothesized that EWP exerts a hypoglycemic effect by regulating hepatic glucose homeostasis. Our results showed that 7 weeks of EWP treatment reduced the fasting blood glucose in T2DM mice and the inhibition of the liver gluconeogenic pathway was involved in the mechanisms of actions. Using the untargeted metabolomics technique, we found that EWP treatment also altered the hepatic metabolic profile in T2DM mice, in which, the role of fatty acid esters of hydroxy fatty acids in mediating the hypoglycemic effect of EWPs might be pivotal.

The study constructed fingerprints and analyzed adsorption rules of volatile compounds (VOCs) in egg powder (EP) under different production processes, including egg white powder (EWP), egg yolk powder (EYP) and whole egg powder (WEP) by HS-GC-IMS. The 29 VOCs identified were primarily ketones and aldehydes. Characteristic VOCs responsible for flavor differences were clarified by difference comparison, clustering and PCA analysis. Additionally, variations in lipid and protein were the primary causes of the VOCs differences in EP through microscopy imaging, infrared and fluorescence spectroscopy. EWP's stretched structure favored fishy-smelling VOCs adsorption but limited total aldehyde binding due to strong hydrophobic interaction. EYP's higher β-sheet ratio and fewer hydrogen bond sites weakened its alcohol VOCs binding capacity. The abundance of ketone VOCs in EP was linked to their low steric hindrance. Therefore, this study elucidated the flavor differences reasons among EWP, EYP and WEP, laying foundation for EP applications in food industry., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024. Published by Elsevier Ltd.)

Egg white protein is widely used in food, chemical, medical and other fields due to its excellent thermal gel properties. However, the regularity of egg white thermal gel (EWTG) by temperature influence is still unknown. In this study, we investigated the potential mechanism of temperature (75-95 °C, 15 min) gradient changes inducing thermal aggregation and gel formation of EWTG. The results showed that changes in textural characteristics and water holding capacity (WHC) of EWTGs depended on switching in protein aggregation morphology (spherical shape - chain shape - regiment shape) and gel network structure differences ("irregular bead-like" - "regular lamellar structure"). In addition, proteomics indicated that the generation of amorphous protein aggregates at 95 °C might be related to Mucin 5B as the aggregation core. The research revealed the EWTG formation from "whole egg white protein" to "single molecules", aiming to provide a reference for quality control in gel food processing., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 Elsevier Ltd. All rights reserved.)

This study aimed to investigate the mechanism of NaCl perturbed preheat-treated egg white proteins' (EWPs) physicochemical and structural properties to modulate the foaming property (FP). The results revealed that NaCl regulated the salinolysis (5 mM) - salt precipitation (50 mM) - gradual or complete coverage with hydrated Na + of the hydration layer (100-300 mM) - enhanced Cl - hydration repulsion (500 mM) of EWP, showing a gradual decrease in aggregates particle size, and reversibility of structural freedom, including moleculer flexibility and surface hydrophobicity. Whereas preheating temperature affected the secondary structure rearrangement and tertiary conformation exposure, and excessive temperature reduced foaming capacity while enhanced foam stability, with a tight correlation between NaCl-mediated EWPs' FP and the extent of Na + covering the hydration layer. The findings provide a theoretical basis for processing factors to modulate the protein hydration layer to influence the functional properties., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 Elsevier Ltd. All rights reserved.)

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., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 Elsevier B.V. All rights reserved.)

Steamed bread has long been an important part of Chinese cuisine. This study investigated the effects of salted egg white (SEW) (5, 10, 15, and 20% w/w) on the quality of steamed breads. Findings revealed that SEW notably enhanced the bread's volume and texture, with a 20% inclusion significantly boosting water retention and rheological properties, albeit reducing bread's lightness. In addition, the H-bond absorption band intensity in the Fourier transform infrared spectroscopy (FTIR) analysis showed increased peak intensities with higher SEW levels, indicative of protein structure alterations. X-ray diffraction confirmed the presence of an amylose-lipid complex. Scanning electron microscope (SEM) and Confocal laser scanning microscope (CLSM) imaging depicted a smooth, consistent protein network with SEW addition. Consumer sensory evaluation responded favourably to the SEW15 steamed bread, suggesting its potential for food industry application. Overall, the study considers SEW an effective ingredient for improving steamed bread quality., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 Elsevier Ltd. All rights reserved.)

Alkali-induced preserved egg gel formation is a dynamic process that involves complex protein changes. Ovomucin (OVM) is closely associated with the gel properties of egg white. In this study, the effect of OVM in alkali-induced egg white gel (AEWG) formation was investigated. The results suggested that OVM reduced the gel formation time by 15 %. The mechanical properties of the fully formed gel were also improved by OVM. Specifically, OVM increased the storage modulus (G') of the gel by 1.5-fold, while the hardness significantly increased from 78.90 ± 4.24 g to 99.80 ± 9.23 g. Low-field nuclear magnetic resonance (LF-NMR) demonstrated that OVM significantly shortened T 23 relaxation time and reduced the water mobility, thus increasing the water holding capacity (WHC). Meanwhile, the presence of OVM resulted in a more homogeneous and denser microscopic morphology of the gel. Selective solubility experiments revealed that disulfide bonds are the primary force in gel formation. OVM promoted the formation of more disulfide bonds, which increased the strength and stability of the gel network. Overall, this research proved OVM plays a critical role in the performance improvement of AEWG, which provides a new insight into the quality control of preserved egg and protein gel foods., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 Elsevier B.V. All rights reserved.)

The purpose of this study was to investigate the effect of an egg white hydrolysate (EWH) to protect white adipose tissue damage from cardiometabolic changes induced by severe hypertension. Male Wistar rats were uninephrectomised and divided: SHAM (weekly subcutaneous vehicle (mineral oil + propylene glycol, 1:1)), SHAM + EWH (subcutaneous vehicle plus EWH via gavage, 1 g/kg per day), DOCA (deoxycorticosterone acetate diluted in vehicle subcutaneously weekly in subsequent doses of 20 mg/kg -1st week, 12 mg/kg - 2–3th week, and 6 mg/kg -4–8th week, respectively, plus 1 % NaCl and 0·2 % KCl in drinking water), and DOCA + EWH. Body weight gain, food and water intake, glucose and lipid metabolism were evaluated. Oxidative stress was assessed by biochemical assay and immunofluorescence for NOX-1, nuclear factor kappa B (NFκB), and caspase-3 in retroperitoneal white adipose tissue (rtWAT). Proinflammatory cytokines (IL-6 and 1β), CD163 + macrophage infiltration, and immunohistochemistry for TNFα and uncoupling protein-1 were evaluated, as well as histological analysis on rtWAT. Glutathione peroxidase and reductase were also determined in plasma. EWH showed hypocholesterolemic, antioxidant, anti-inflammatory, and anti-apoptotic properties in the arterial hypertension DOCA-salt model. The results demonstrated the presence of functional changes in adipose tissue function by a decrease in macrophage infiltration and in the fluorescence intensity of NFκB, NOX-1, and caspase-3. A reduction of proinflammatory cytokines and restoration of antioxidant enzymatic activity and mitochondrial oxidative damage by reducing uncoupling protein-1 fluorescence intensity were also observed. EWH could be used as a potential alternative therapeutic strategy in the treatment of cardiometabolic complications associated with malignant secondary arterial hypertension.

We aimed to investigate whether the consumption of Egg White Hydrolysate (EWH) acts on nervous system disorders induced by exposure to Cadmium (Cd) in rats. Male Wistar rats were divided into (a) Control (Ct): H 2 O by gavage for 28 days + H 2 O (i.p. - 15th - 28th day); (b) Cadmium (Cd): H 2 O by gavage + CdCl 2 - 1 mg/kg/day (i.p. - 15th - 28th day); (c) EWH 14d: EWH 1 g/kg/day by gavage for 14 days + H 2 O (i.p.- 15th - 28th day); (d) Cd + EWH cotreatment (Cd + EWHco): CdCl 2  + EWH for 14 days; (e) EWH 28d: EWH for 28 days; (f) EWHpre + Cd: EWH (1st - 28th day) + CdCl 2 (15th - 28th day). At the beginning and the end of treatment, neuromotor performance (Neurological Deficit Scale); motor function (Rota-Rod test); ability to move and explore (Open Field test); thermal sensitivity (Hot Plate test); and state of anxiety (Elevated Maze test) were tested. The antioxidant status in the cerebral cortex and the striatum were biochemically analyzed. Cd induces anxiety, and neuromotor, and thermal sensitivity deficits. EWH consumption prevented anxiety, neuromotor deficits, and alterations in thermal sensitivity, avoiding neuromotor deficits both when the administration was performed before or during Cd exposure. Both modes of administration reduced the levels of reactive species, and the lipid peroxidation increased by Cd and improved the striatum's antioxidant capacity. Pretreatment proved to be beneficial in preventing the reduction of SOD activity in the cortex. EWH could be used as a functional food with antioxidant properties capable of preventing neurological damage induced by Cd., (© 2024. The Author(s).)

Soft assembly of peptide and curcumin (Cur) molecules enables functional integration by finding dynamic equilibrium states through non-covalent interactions. Herein, we developed two soft assembly systems, curcumin-egg white peptides (Cur-EWP) aggregations (AGs) and Cur-EWP-casein-quaternary chitosan (Cur-EWP-CA-QC) nanoparticles (NPs) to comparatively investigate their therapeutic effects on ulcerative colitis in mice and elucidate their underlying mechanism. Results revealed that Cur-EWP AGs, despite gastrointestinal tract instability, exhibited a propensity for swift accumulation within the colorectal region, enriching mucus-associated and short-chain fatty acid (SCAF)-producing bacteria, restoring the intestinal barrier damage. Whereas, Cur-EWP-CA-QC NPs, benefiting from their remarkable stability and exceptional mucosal adsorption properties, not only enhanced permeability of Cur and EWP in the small intestine to activate the immune response and boost tight junction protein expression but also, in their unabsorbed state, regulated the intestinal flora, exerting potent anti-inflammatory activity. Soft assembly of peptides and hydrophobic nutraceuticals could synergize biological activities to modulate chronic diseases., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 Elsevier B.V. All rights reserved.)

Recently, oral deliverable strategies of multiple nutraceuticals for ulcerative colitis (UC) mitigation have attracted increasing attention. This study aimed to fabricate facile oral assemblies loaded with egg-white-derived peptides (EWDP) and curcumin based on carboxymethyl chitosan (CMCS) and an γ-cyclodextrin metal-organic framework (MOF). Herein, outer CMCS could coassemble with EWDP (both nutraceuticals and building blocks) into cobweb-like fibrils to promote bridging with inner MOF via coordinative noncovalent interactions (hydrogen bonding, hydrophobic interaction, and electrostatic interaction). Compared with conventional γ-cyclodextrin/MOF-based composites, the above coassembly could also endow the biocompatible assemblies with superior nanoscale colloidal properties, processing applicability (curcumin storage stability, bioaccessibility, and aqueous solubility), and bioactivity. Moreover, the oral synergism of EWDP and curcumin (initially nonsynergistic) for UC mitigation was achieved by alleviating inflammatory damage and gut microbiota imbalance. Overall, the novel assemblies could be a promising amplifier and platform to facilitate oral formulations of various nutraceuticals for food processing and UC relief.

Highly oxidative reactive oxygen species (ROS) attack protein structure and regulate its functional properties. The molecular structures and functional characteristics of egg white (EW) protein (EWP) during 28 d of aerobic or anaerobic storage were explored to investigate the "self-driven" oxidation mechanism of liquid EW mediated by endogenous ROS signaling. Results revealed a significant increase in turbidity during the storage process, accompanied by protein crosslinking aggregation. The ROS yield initially increased and then decreased, leading to a substantial increase in carbonyl groups and tyrosine content. The free sulfhydryl groups and molecular flexibility in EWP exhibited synchronicity with ROS production, reflecting the self-repairing ability of cysteine residues in EWP. Fourier-transform infrared spectroscopy indicated stable crosslinking between EWP molecules in the early oxidation stage. However, continuous ROS attacks accelerated EWP degradation. Compared with the control group, the aerobic-stimulated EWP showed a significant decrease in foaming capacity from 30.5 % to 9.6 %, whereas the anaerobic-stimulated EWP maintained normal levels. The emulsification performance exhibited an increasing-then-decreasing trend. In conclusion, ROS acted as the predominant factor causing deterioration of liquid EW, triggering moderate oxidation that enhanced the superior foaming and emulsifying properties of EWP, and excessive oxidation diminished the functional characteristics by affecting the molecular structure., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 Elsevier B.V. All rights reserved.)

This study aims to develop ultrasound-assisted acid-induced egg white protein (EWP)-soy protein isolate (SPI) composite gels and to investigate the mechanistic relationship between the co-aggregation behavior of composite proteins and gel properties through aggregation kinetics monitored continuously by turbidity. The results showed that the inclusion of EWP caused the attenuation of gel properties and maximum aggregation (A max ) because EWP could aggregate with SPI at a higher rate (K app ), which impeded the interaction between SPI and the formation of a continuous gelling network. In the EWP-dominated system, SPI with higher molecular weights also increased the fractal dimension of gels. Ultrasound improved properties of composite gels, especially the SPI-dominated system. After ultrasound treatment, the small, uniform size of co-aggregates and the decrease in potential led to an increase in the aggregation rate and formation of dense particles, consistent with an increase in gelation rate and texture properties. Excessively fast aggregation generated coarse chains and more pores. Still, the exposure of free sulfhydryl groups assisted the gel structure units to form a compact network through disulfide bonding. On the whole, the study could provide theoretical support for a deeper understanding on the interaction mechanism and gelation of composite proteins., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 Elsevier B.V. All rights reserved.)

Avian leukemia is an infectious tumorous disease of chickens caused by subgroup A of the avian leukemia virus (ALV-A), which mainly causes long-term viremia, slow growth, immune suppression, decreased production performance, multi-tissue tumors, and even death. The infection rate of this disease is very high in chicken herds in China, causing huge economic losses to the poultry industry every year. We successfully expressed the specific antigen protein of ALV (P27) through recombinant protein technology and screened a pair of highly sensitive monoclonal antibodies (mAbs) through mouse immunity, cell fusion, and antibody pairing. Based on this pair of antibodies, we established a dual antibody sandwich ELISA and gold nanoparticle immunochromatographic strip (AuNP-ICS) detection method. In addition, the parameters of the dual antibody sandwich ELISA and AuNP-ICS were optimized under different reaction conditions, which resulted in the minimum detection limits of 0.2 ng mL -1 and 1.53 ng ml -1 , respectively. Commonly available ELISA and AuNP-ICS products on the market were compared, and we found that our established immune rapid chromatography had higher sensitivity. This established AuNP-ICS had no cross-reactivity with Influenza A (H1N1), Influenza A (H9N2), respiratory syncytial virus (RSV), varicella-zoster virus (VZV), Listeria monocytogenes listeriolysin (LLO), and Staphylococcal enterotoxin SED or SEC. Finally, the established AuNP-ICS was used to analyze 35 egg samples, and the results showed 5 positive samples and 30 negative samples. The AuNP-ICS rapid detection method established by our group had good specificity, high sensitivity, and convenience, and could be applied to the clinical sample detection of ALV-A.

The chicken egg, an excellent natural source of proteins, has been an overlooked native biomaterial with remarkable physicochemical, structural, and biological properties. Recently, with significant advances in biomedical engineering, particularly in the development of 3D in vitro platforms, chicken egg materials have increasingly been investigated as biomaterials due to their distinct advantages such as their low cost, availability, easy handling, gelling ability, bioactivity, and provision of a developmentally stimulating environment for cells. In addition, the chicken egg and its by-products can improve tissue engraftment and stimulate angiogenesis, making it particularly attractive for wound healing and tissue engineering applications. Evidence suggests that the egg white (EW), egg yolk (EY), and eggshell membrane (ESM) are great biomaterial candidates for tissue engineering, as their protein composition resembles mammalian extracellular matrix proteins, ideal for cellular attachment, cellular differentiation, proliferation, and survivability. Moreover, eggshell (ES) is considered an excellent calcium resource for generating hydroxyapatite (HA), making it a promising biomaterial for bone regeneration. This review will provide researchers with a concise yet comprehensive understanding of the chicken egg structure, composition, and associated bioactive molecules in each component and introduce up-to-date tissue engineering applications of chicken eggs as biomaterials.

Background: The uses of egg white powder (EWP) are restricted because of its odor. It is necessary to find a method to improve its flavor. In this paper, three different antioxidants - green tea extract (GTE), sodium ascorbate (SA), and glutathione (GSH) - were selected to modify the flavor. The physicochemical and structural properties of EWP were investigated to study the mechanism of the formation and release of volatile compounds., Results: Antioxidants can modify the overall flavor of EWP significantly, inhibiting the generation or release of nonanal, 3-methylbutanal, heptanal, decanal, geranyl acetone, and 2-pemtylfuran. A SA-EWP combination showed the lowest concentration of 'off' flavor compounds; GTE-EWP and GSH-EWP could reduce several 'off' flavor compounds but increased the formation of geranyl acetone and furans. The changes in the carbonyl content and the amino acid composition confirmed the inhibition of antioxidants with the oxidative degradation of proteins or characteristic amino acids. The results of fluorescence spectroscopy and Fourier transform infrared (FTIR) spectroscopy provided structural information regarding EWP, which showed the release of volatile compounds decreased due to structural changes. For example, the surface hydrophobicity increased and the protein aggregation state changed., Conclusions: Antioxidants reduce the 'off' flavor of EWP in two ways: they inhibit protein oxidation and Maillard reactions (they inhibit formation of 3-methylbutanal and 2-pemtylfuran) and they enhance the binding ability of heat-denatured proteins (reducing the release of nonanal, decanal, and similar compounds). © 2023 Society of Chemical Industry., (© 2023 Society of Chemical Industry.)

The formation of the egg white precipitate (EWP) during dilution poses challenges in food processing. In this paper, the effects of 90 W and 360 W ultrasonic intensities on the inhibition of EWP formation were investigated. The findings revealed that 360 W sonication effectively disrupted protein aggregates, decreasing the dry matter of EWP by 5.24 %, particle size by 57.86 %, and viscosity by 82.28 %. Furthermore, the ultrasonic pretreatment unfolded protein structures and increased the content of β-sheet structures. Combined with quantitative proteomics and intermolecular forces analysis, the mechanism by which ultrasonic pretreatment inhibited water-diluted EWP formation by altering protein interactions was proposed: ultrasonic pretreatment disrupted electrostatic interactions centered on lysozyme, as well as hydrogen-bonding interactions between ovomucin and water. In conclusion, our research provides valuable insights into the application of ultrasonic pretreatment as a means to control and improve the quality of egg white-based products., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 Elsevier B.V. All rights reserved.)

The effects of different copper salts (CuSO 4 , CuCl 2 , Cu(CH 3 COO) 2 ) on the physicochemical characteristics, microstructure and protein conformation of alkali-induced egg white (EW) gels were investigated. With increasing concentration, three copper salts promoted the aggregation of EW proteins while decreasing the β-sheet content. The three-dimensional gel network was promoted to form, and the water-holding capacity (WHC), texture and solubility of gels were improved by three copper salts at low concentrations. While at high concentrations, the gel deteriorated. The main forces maintaining the alkali-induced EW gels added with copper salts were mainly ionic and disulfide bonds. And the protein component was not affected by ion concentration. Due to the difference in charge density, the three anions had different effects on the stability of proteins, and finally showed different gel characteristics (gel strength, WHC, solubility): CuSO 4  > CuCl 2  > Cu(CH 3 COO) 2 . Therefore, copper salts (especially CuSO 4 ) can be used to improve EW protein aggregation., Competing Interests: Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2023. Published by Elsevier Ltd.)

In the research presented in this manuscript, an intricate study has been carried out on the interaction of zinc ions with the hen egg white lysozyme (HEWL) protein. Utilizing a spectroscopic technique, the alterations that arise due to the binding of Zn 2+ to the HEWL were scrutinized, underscoring the paramount significance of deprotonated carboxyl and thiol groups in the process of binding. The binding phenomena were substantiated using capillary electrophoresis integrated with inductively coupled plasma mass spectrometry (CE-ICP-MS). Further spectrometric assessments (MALDI-TOF MS and FT-ICR-MS) shed light on the direct interaction of zinc ions with the functional groups of the protein. Importantly, high-resolution FT-ICR-MS techniques elucidated the capability of a single protein molecule to bind to multiple zinc ions. The empirically derived spectroscopic data received additional confirmation via a molecular docking study of the Zn 2+ binding process, which highlighted a substantial affinity between the predicted 3D model of zinc-lysozyme complexes. Predominantly, the interaction between the bound entities was observed at the cysteine residues. Lastly, the conducted antimicrobial tests revealed that the zinc-lysozyme complexes manifest an inhibitory effect against bacterial (E. coli and S. aureus) and yeast (C. albicans) strains., Competing Interests: Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2023. Published by Elsevier B.V.)

Our study aimed to investigate the effects of ultrasound on the fibrillation kinetics of HEWL (hen egg white lysozyme) and its physicochemical properties. Ultrasound, a mechanical wave, can induce conformational changes in proteins. To achieve this, we developed an ultrasound exposure system and used various biophysical techniques, including ThT fluorescence spectroscopy, ATR-FTIR, Far-UV CD spectrophotometry, Fluorescence microscopy, UV-spectroscopy, and seeding experiments. Our results revealed that higher frequencies significantly accelerated the fibrillation of lysozyme by unfolding the native protein and promoting the fibrillation process, thereby reducing the lag time. We observed a change in the secondary structure of the sonicated protein change to the β-structure, but there was no difference in the T m of native and sonicated proteins. Furthermore, we found that higher ultrasound frequencies had a greater seeding effect. We propose that the effect of frequency can be explained by the impact of the Reynolds number, and for the Megahertz frequency range, we are almost at the transition regime of turbulence. Our results suggest that laminar flows may not induce any significant change in the fibrillation kinetics, while turbulent flows may affect the process., Competing Interests: Declaration of competing interest The authors report that they have no conflict of interest., (Copyright © 2023. Published by Elsevier B.V.)

In this study, the properties of pigeon egg white (PEW) and chicken egg white (CEW) thermal gels were compared, with the aim of revealing the mechanisms involved in the high transparency of PEW thermal gels. Results demonstrated that PEW gels exhibited higher transparency than CEW gels. Scanning electron microscope (SEM) and transmission electron microscope (TEM) analysis revealed that PEW gels formed a fine chain gel network structure with an average diameter of thermal aggregates (89.84 ± 7.13 nm). The molecular properties of PEW proteins, such as higher content of β-sheet structures (32.73 %), reactive groups (free sulfhydryl groups, hydrophobic groups), and absolute zeta potential (-3.563 mV), were found to contribute to the formation of smaller thermal aggregates during thermal denaturation. The microrheology measurements showed that these features allowed PEW proteins to interact less with each other and form smaller thermal aggregates during thermal denaturation, which facilitated the formation of fine chain gel networks and thus improved the transparency of the gels. The present study initially reveals the molecular basis of the high transparency of PEW thermal gels and provides a theoretical reference for the development of new highly transparent protein materials., Competing Interests: Declaration of competing interest We declare that the work described was original research that has not been published previously, and not under consideration for publication elsewhere. No conflict of interest exits in the submission of this manuscript, and manuscript is approved by all authors to be published., (Copyright © 2023 Elsevier B.V. All rights reserved.)

This research investigated the effects of spray drying (SD, set at 180 °C), freeze-drying (FD, set at -35 °C), and electrohydrodynamic drying (EHD) with and without the foam-mat method on egg white. The configuration used in EHD was a wire-to-plate type at room temperature. The results showed no significant difference in gel hardness and WHC% (P ≥ 0.05). Also, the foam-mat EHD powders resembled the FD powders in microstructure, appearance, flowability, and absorption intensity of the Amide I and II bands. Furthermore, the foam-mat EHD (DC-) powder had the highest protein content (66.1%), enthalpy (-183.06 J/g), and foaming capacity (725%) (P < 0.05). This finding was proved by FTIR, Raman, and SDS-PAGE tests, which revealed the minor structural changes in proteins (peptide chain structure, Amide I, Amide II, α-helix, and β-sheet). FD powder demonstrated good protein stability in zeta potential and foam stability tests., Competing Interests: Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2023. Published by Elsevier Ltd.)

This paper aimed to investigate the in vivo absorption of egg white hydrolysate (EWH) in rats and the transport route across the intestinal epithelium. Results showed that the level of plasma peptide-bound amino acid (PAA) of the EWH-supplemented rats (EWH-R) was determined to be 2012.18 ± 300.98 μmol/L, 10.72% higher than that of the control group, and was significantly positively correlated to that of EWH. Thirty-three egg white-derived peptides were successfully identified from the plasma of EWH-R, and 20 of them were found in both EWH-R plasma and EWH, indicating that these peptides tend to be absorbed through the intestinal epithelium in intact forms into the blood circulation. In addition, 637 up-regulated and 577 down-regulated genes in Caco-2 cells incubated with EWH were detected by RNA-sequencing and the clathrin-dependent endocytosis was the most enriched pathway in KEGG analysis. EWH significantly increased the mRNA levels of the key genes involved in the clathrin-dependent endocytosis but these changes would be inhibited by the clathrin-dependent endocytosis inhibitor of chlorpromazine. Moreover, the transepithelial transport of EWH across Caco-2 cell monolayers was significantly reduced by chlorpromazine. This study provided molecular-level evidence for the first time that clathrin-dependent endocytosis might be the main transport route of EWH in the intestinal epithelium., Competing Interests: Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2023. Published by Elsevier Ltd.)

Background: Ovalbumin (OVA), accounting for 50% of proteins in egg white, is a kind of high-quality protein with excellent nutritional and processing functions. Acid heat treatment will induce the deformation and filtration of OVA, endowing it with improved functionality. However, the molecular kinetic process during the fibrillation of OVA and the application of the fabricated OVA fibrils (OVAFs) have not been thoroughly studied and revealed., Results: In this study, the fabrication mechanism and the application OVAFs as an interfacial stabilizer and polyphenol protector were investigated. Acidic (pH 3.0) heat treatment was used to induce the fibrillation of OVA, and thioflavin T fluorescence intensity, molecular weight distribution, and the tertiary and secondary structures of OVAF samples were recorded to determine the fibrillation efficiency and the molecular mechanism. The results showed that, in the initial stage of fibrillation, OVA first hydrolyzed to oligopeptides, accompanied by the exposure of hydrophobic domains. Then, oligopeptides were connected by disulfide bonds to form primary fibril monomers. Hydrophobic interaction and hydrogen bonding may participate in the further polymerization of the fibrils. The fabricated OVAFs were characterized by a β-sheet-rich structure and possessed improved emulsifying, foaming, and polyphenol protection ability., Conclusion: The research work was meaningful for exploring the application of globular water-soluble OVA in an emerging nutritious food with novel texture and sensory properties. © 2023 Society of Chemical Industry., (© 2023 Society of Chemical Industry.)

Background: Changes in storage temperature and time alter the functional properties of egg white powder (EWP) and determine its quality and shelf-life, finally affecting the consumer acceptance of the products made from EWP. In the present study, the EWP samples were stored at four different temperatures (-20, 4, 25 and 37 °C) for 60 days, and then the protein structural, physical and functional properties of EWP were measured and assessed further for correlation with storage conditions using heatmap., Results: The viscosity of the EWP solution increased after 30 days. Foaming ability and rheological properties increased first and then decreased compared to untreated samples with the prolonged storage time. Correlation analysis results indicated that the gel hardness, water holding capacity, foaming ability, emulsifying ability, particle size, dispersibility and viscosity of EWP were significantly related to storage time (P < 0.05). Only the gelation properties of EWP stored at 37 °C for 60 days changed significantly and were negatively related to its moisture content (P < 0.05). Additionally, the random coil content of EWP was positively correlated with particle size, moisture content, solubility and gel properties, whereas β-sheet was negatively correlated with them., Conclusion: Compared to other temperatures, the functional properties of EWP were relatively stable under 4 °C. Therefore, the low temperature (4 °C) was selected as the most suitable storage temperature for EWP. The results of the present study could provide a theoretical basis for the shelf-life extension of EWP. © 2022 Society of Chemical Industry., (© 2022 Society of Chemical Industry.)

In this study, the thermal gelation and digestion properties of hen egg white (hen EW) proteins with different salts were investigated. Results show that the addition of neutral salt - sodium chloride (NaCl) decreased the gel hardness/resilience, increased gel lightness, aggregated particle size and digestibility of hen EW proteins significantly. In contrast, alkaline salts - phosphate and carbonate addition increased the gel resilience and strain tolerance as well as reduced the aggregated particle size and gel lightness of hen EW proteins due to the increase of solution pH and negative charge. Correlation analysis shows that the digestibility of hen EW gels was affected by gel viscoelasticity, molecule forces and texture. In conclusion, thermal gelation properties of hen EW proteins could be modulated by salts with different pH/ionic strength, and thus affected the protein digestion and peptide released., Competing Interests: Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2022 Elsevier Ltd. All rights reserved.)

The performance of lysozyme adsorption by the aminated nanofiber membrane immobilized with Reactive Green 19 (RG19) dyes was evaluated in batch and flow systems. The physicochemical properties of the dye-immobilized nanofiber membrane were characterized. The parameters of batch-mode adsorption of lysozyme (e.g., pH, initial dye concentration, and lysozyme concentration) were optimized using the Taguchi method. In a flow process, the factors influencing the dynamic binding performance for lysozyme adsorption in the chicken egg white (CEW) solution include immobilized dye concentration, adsorption pH value, feed flow rate, and feed CEW concentration. The impact of these operating conditions on the lysozyme purification process was investigated. Under optimal conditions, the recovery yield and purification factor of lysozyme achieved from the one-step adsorption process were 98.52% and 143 folds, respectively. The dye-affinity nanofiber membrane also did not exhibit any significant loss in its binding capacity and purification performance after five consecutive uses., Competing Interests: Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2022 Elsevier Ltd. All rights reserved.)

This study was conducted to investigate the effects of different copper salts on the physicochemical properties, microstructure and intermolecular interactions of preserved egg white (PEW) during pickling. With increased pickling time, the alkalinity of the pickling solution and the moisture of PEW pickled by three copper salts (CuSO 4 , CuCl 2 and Cu(CH 3 COO) 2 ) gradually decreased, while the pH showed dynamic trends. During the early stage of pickling, the viscosity of PEW changed dynamically. With the progress of pickling, the hardness and springiness of PEW increased gradually and the α-helix structure gradually transformed into a more stable β-structure. The main forces that maintained PEW gel were ionic and disulfide bonds. In the early stage of pickling, the alkali penetration rate of CuCl 2 pickled preserved eggs was faster, and better gel strength and network structure were observed, followed by CuSO 4 and Cu(CH 3 COO) 2 , while there were no significant differences in the later stage of pickling., Competing Interests: Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2022 Elsevier Ltd. All rights reserved.)

Egg proteins, as one of the most abundant animal protein sources, have received considerable attention for developing delivery systems. Among all egg proteins, egg white (ovalbumin) is the most promising encapsulant due to its excellent properties such as gelling, digestibility, self-assembly, amphiphilic nature. In this review paper, we focused particularly on egg protein-based delivery systems with superior encapsulation and delivery functions, including polymeric nanoparticles, emulsions, hydrogels and aerogels. Egg protein-based delivery systems across a wide range of geometry and dimensions have been applied to protect or control-release bioactive small molecules and macromolecules, probiotics and metal nanostructures. However, there are challenges that must be carefully addressed for advancing the practical applications of egg protein-based delivery system in foods, including allergenicity from ovalbumin and ovotransferrin, intolerance to environmental conditions, limited processing technologies. More efforts are warranted to fill knowledge gaps related to fabrication, utilization and digestive mechanisms of egg protein-derived delivery systems., Competing Interests: Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2022 Elsevier Ltd. All rights reserved.)

Background: Glycosylation is an effective method to modify protein. However, there is a lack of research on the property changes of glycosylated protein during storage. In the present study, the changes in the physicochemical, functional, and structural properties of xylo-oligosaccharide (XOS) glycosylated egg white powder (EWP) (XOS-EWP conjugates) prepared with different glycosylation conditions (XOS/EWP ratio and reaction time) were investigated when stored at 25 °C and 60% relative humidity., Results: In the 12 weeks of storage, the degree of grafting, browning, and the formation of Maillard reaction products of XOS-EWP conjugates increased. The increase in XOS/EWP ratio and reaction time led to an increase in protein aggregation, though a decrease in solubility, due to increased degree of glycosylation and structural changes. Furthermore, improved gel hardness of XOS-EWP conjugates deteriorated, while improved emulsification ability was kept stable during storage. For the sample with a lower XOS/EWP ratio and reaction time, the gel hardness and emulsifying properties underwent little or no deterioration even improving during storage. The results could be attributed to the limited degree of glycosylation, further unfolding of the protein structure, increased surface hydrophobicity of protein, and improved thermal characteristics., Conclusion: During storage, the Maillard reaction would continue to occur in the glycosylated EWP, further affecting the performance of modified EWP. Modified EWP prepared under different glycosylation conditions performed differently during storage. Modified EWP with a larger XOS/EWP ratio and reaction time meant it was harder to maintain good performance. Modified EWP with a smaller XOS/EWP ratio and reaction time changed significantly to better performances. © 2022 Society of Chemical Industry., (© 2022 Society of Chemical Industry.)

Sterile homogeneous egg white (EW) is obtained through a three-step process, high-speed homogenization, centrifugation, and ultraviolet radiation. After incorporating 1.056 × 10 10  CFU/g of Escherichia coli, the EW mixture was dehydrated by slow drying to form a brittle, water-soluble, and transparent bacteria-embedded egg white glass (BE-EWG). The BE-EWG stored at -20 °C for 4 months maintains almost all the cell growth functions and proliferation activities of the labeled E. coli, and most of the cell functions and 60 % of the proliferation activities are maintained for up to one year. The BE-EWG exhibits a porous hydrogel membrane structure after heat treatment, and many E. coli cells are accommodated in a grid with a pore size of 2-10 mm. The loss of bacteria-carrying viability after storage at room temperature may be related to the Maillard reaction between protein and glucose in EW, which results in the structural changes caused by protein cross-linking, darkened color and water insolubility of the BE-EWG. Therefore, the method of embedding E. coli cells in EWG as solid form at room temperature to avoid ice crystal formation during cryopreservation is more beneficial for storage, packaging and shipping at -20 °C., Competing Interests: Declaration of competing interest The authors declare that they have no conflict of interest., (Copyright © 2022 Elsevier B.V. All rights reserved.)

Background: Approximately 9.9% of young children in China suffer from egg allergies. Ovalbumin (OVA) and ovomucoid (OVM) are both the main allergens with higher allergenicity in egg white. The previous studies mainly focused on the effects of pasteurization on the structure and allergenicity of the isolated protein itself. The effects of the interaction between OVA and OVM on their spatial structure and allergenicity under pasteurization are still unclear. Therefore, in this study, the spectroscopic, immunological, and cytological methods were used to investigate the effects on OVA and OVM by their interactions which were induced by the following pasteurization, heating for 10 min at 60, 65, and 70 °C, respectively., Results: Results indicated that OVA and OVM could form macromolecular aggregates by their interaction at 70 °C, and their solubility was decreased while turbidity was increased. The spatial structures of OVA and OVM were both changed by their interaction, when pasteurization temperature was at 70 °C the exposure of their hydrophobic groups and α-helix content were decreased while their β-sheet was increased. The potential allergenicity of OVA and OVM was also changed, which showed that the immunoglobulin G (IgG)-binding ability of OVA and OVM could be increased, and their IgE-binding ability was decreased a bit. The releases of interleukin 4 (IL-4), IL-6, β-HEX, histamine and tumor necrosis factor alpha (TNF-α) from OVA-OVM-induced KU812 cells were all decreased at 70 °C., Conclusion: Therefore, according to the results, if the liquid egg products were pasteurized for 10 min, the temperature of 70 °C should be carefully considered. © 2022 Society of Chemical Industry., (© 2022 Society of Chemical Industry.)

Heat-induced gel-assisted desalination could efficiently and inexpensively remove salt from salted egg whites. However, it was at the expense of the excellent foaming properties of egg whites, caused by the denaturation and aggregation of proteins during heating treatment. Hence, in this current work, the enzymatic treatment was used to re-endow duck egg white nanogels (DEWN) with outstanding foaming properties. We found that low levels of hydrolysis (DH = 2.27 %) could dramatically improve the foaming capability (FC), reaching >200 %, which also enhanced the foaming stability (FS). As the hydrolysis time extended, the adsorption and diffusion rate of the supernatant on the interface increased and performed high elasticity. The dilatational rheology and Lissajous plots were explored to investigate the nonlinear dilatational rheological behaviors of the air/water interface stabilized by the hydrolysed samples. Finally, we evaluated the effect of pH on foaming properties and found that the FC could exceed 250 %, and the FS was close to 80 % at pH = 5. These encouraging results showed that simple enzymatic treatment could revive nanogels from their dissatisfied foaming properties. In this work, gel-assisted desalination combined with enzyme treatment significantly promotes the high-quality and high-value utilization of salted egg white., Competing Interests: Declaration of competing interest The authors declare no conflicts of interest., (Copyright © 2022 Elsevier B.V. All rights reserved.)

This study aimed to evaluate the combined effect of κ-carrageenan and salted duck egg white powder (SDEWP) in improving the gel quality of threadfin bream surimi. Effects of κ-carrageenan at different levels (0-2 %) on gel properties of threadfin bream surimi without and with salted duck egg white powder at 3 % (protein equivalent) were investigated. A combination of 0.5 % κ-carrageenan and SDEWP increased breaking force of surimi gel by 139.7 % and deformation by 55.1 %, compared to the control (P < 0.05). The expressible moisture content (EMC) was decreased by 50.0 % in the surimi gel added with 0.5 % κ-carrageenan and SDEWP. Hardness, cohesiveness, gumminess, and chewiness of surimi gel were also improved (P < 0.05). However, springiness of surimi gel was not affected. SDEWP reduced proteolytic degradation in surimi gel. Surimi gel with augmented whiteness was attained when κ-carrageenan was added at higher levels. Microstructure of surimi gel shown that the gel became denser and more uniform when added with 0.5 % κ-carrageenan and SDEWP. Therefore, κ-carrageenan can be used to enhance the effectiveness of SDEWP and further improve the gel quality of threadfin bream surimi added with SDEWP., Competing Interests: Declaration of competing interest None., (Copyright © 2022 Elsevier B.V. All rights reserved.)

Several food dyes are known to induce amyloid fibrillation when interacting with proteins. Here, we studied the role of sunset yellow (SY) in the amyloid fibrillation of hen egg white lysozyme (HEWL) and characterized the changes using spectroscopy techniques. Turbidity results showed that SY dye induces aggregation in HEWL in concentrations dependent manner. The aggregation induced by SY dye is kinetically very fast, no lag phase was detected, and the kinetics process follows an isodesmic kinetics pathway. The SY-dye induce aggregates have cross-β secondary structure confirmed by far-UV CD measurements. The effect of salts and solvents was also seen on SY-induced aggregates. Turbidity, far-UV CD, and kinetics results suggest that certain concentrations of NaCl and (NH 4 ) 2 SO 4 solubilize the SY-induce amyloid fibrils, but (NH 4 ) 2 SO 4 is more effective. Similarly, solvents are also solubilized the SY-induces HEWL amyloid fibrillation but the order of defibrillation is as follows: Isopropanol> ethanol > methanol which signified that isopropanol is more effective than other solvents. The salts and solvents data suggest that the electrostatic, as well as hydrophobic interaction, is responsible for SY-induced amyloid fibrillation. These conformational changes should be examined, more seriously for the purpose of food safety., Competing Interests: Declaration of competing interest None., (Copyright © 2022 Elsevier B.V. All rights reserved.)

As a typical colloidal solution system, egg white (EW) will naturally thin during storage. This paper discussed mechanism of EW thinning and protein depolymerization from the perspective of "protein composition and molecular structure". The results of rheology showed that viscoelasticity of EW declined substantially. Analysis of EW protein in gel system demonstrated that arrangement of EW thermal gel gradually tightened with dissociation of skeleton protein during storage. Molecular characteristics of EW protein in solution showed that particle size and free sulfhydryl content decreased. The increase of disulfide bonds enhanced intermolecular electrostatic force and hindered molecular aggregation, which improved solubility of molecules and reduced surface hydrophobicity. Quantitative proteomic analysis indicated the reduced abundance of β-ovomucin (OVO) might be the direct cause of EW thinning. Notably, some proteins extensively involved in the aggregation of proteins during later storage. The results can provide scientific basis for depolymerization and aggregation of EW during storage., (Copyright © 2022 Elsevier Ltd. All rights reserved.)

Selenium-enriched egg white peptides (Se-EWP) were prepared by pre-heat treatment and enzymatic hydrolysis in this study. In addition, their selenopeptide sequence identification and immunomodulatory effect were investigated. Results showed that the yield of Se-EWP obtained from alkaline-neutral protease treatment reached 76.90%, and peptides with a molecular weight of 200-1000 Da accounted for 98.33%. Four characteristic selenopeptides, including SeCys-Trp-Leu-Glu, Trp-Ser-SeCys, SeMet-Ala-Pro, and SeMet-Leu, were identified by HPLC-ESI-MS/MS, which were rich in hydrophobic and branched-chain amino acids. Se-EWP (750 mg/kg/d) could effectively retard the decrease of immune organ index in immunosuppressed mice induced by cyclophosphamide. Moreover, supplementation of Se-EWP could promote a higher content of Se in liver, the number of white blood cells, and the levels of serum cytokines (IL-6, IL-2, and TNF-α) as compared with EWP groups, indicating that Se-EWP could effectively alleviate immunosuppression induced by cyclophosphamide. These findings suggested that Se-EWP exhibited great potential as functional foods for immunomodulatory effect.

Background: Isolation of lysozyme from egg white (EW) using ion exchange resin adsorption method generates large quantities of lysozyme-free egg white (LFEW) with poor gelling property. To maximize the applications of LFEW, the effect of Lactiplantibacillus plantarum fermentation on the gel properties of LFEW was investigated in this study., Results: The fermentation efficiency of LFEW with lysozyme removed was significantly improved, and the sugar removal rate (2 g kg -1 Lactiplantibacillus plantarum, 37 °C, 7 h) was more than 90%. Removal of lysozyme resulted in increased stability and surface hydrophobicity of EW. After Lactiplantibacillus plantarum fermentation, the stability of EW decreased, and the average particle size and surface hydrophobicity increased. In addition, by comparing the gel properties of EW and LFEW before and after fermentation at different pH, it was found that the hardness, elasticity, and water holding capacity (WHC) of EW gel increased significantly. The removal of lysozyme effectively improved the WHC and springiness of the EW gel and promoted the formation of a denser network structure with smaller pores. After Lactiplantibacillus plantarum fermentation treatment, LFEW gel hardness decreased, with loose and porous network structure, no browning occurred after autoclaving., Conclusion: This study provided the direction and theoretical basis for producing a fermented LFEW gel with pleasing texture and appearance. © 2022 Society of Chemical Industry., (© 2022 Society of Chemical Industry.)

"Fenghuang Egg" is a special egg product incubated for 12 days by fertilized hen eggs. Its egg white contains high-viscosity and excellent thermal gel strength. A comparative study on the differences in gel properties, structure, and substance composition between fresh egg white (FEW) and "Fenghuang egg" gelatinous egg white (GEW) was carried out. Experimental results showed GEW had better apparent viscosity, as well as the hardness, cohesiveness and water holding capacity (WHC) of thermal gel; the content and size of aggregate structure increased significantly in GEW, and a fibrous dense network composed of numerous spherical nanoparticles connected in series was formed after heating. In addition, it also discovered that more water molecules in GEW existed in the form of bound water. A total of 41 proteins changed significantly in FEW and GEW, Mucin 6 might be the main reason for the enhanced viscosity of GEW, and OVA might be the dominant protein differentiating the thermal gel properties between FEW and GEW. This study revealed that the differences in gel properties and structures between FEW and GEW were closely related to the content of highly glycosylated globular proteins, laying a theoretical foundation for the application of high-viscosity egg whites., (Copyright © 2022 Elsevier B.V. All rights reserved.)