Implications of intracrystalline OC17 on the protection of lattice incorporated proteins.

Biogenic CaCO3 formation is regulated by crystallization proteins during crystal growth. Interactions of proteins with nascent mineral surfaces trigger proteins to be incorporated into the crystal lattice. As a result of incorporation, these intracrystalline proteins are protected in the lattice, an example of which is ancient eggshell proteins that have persisted in CaCO3 for thousands of years even under harsh environmental conditions. OC17 is an eggshell protein known to interact with CaCO3 during eggshell formation during which OC17 becomes incorporated into the lattice. Understanding protein incorporation into CaCO3 could offer insights into protein stability inside crystals. Here, we study the protection of OC17 in the CaCO3 lattice. Using thermogravimetric analysis we show that the effect of temperature on intracrystalline proteins of eggshells is negligible below 250 °C. Next, we show that lattice incorporation protects the OC17 structure despite a heat-treatment step that is shown to denature the protein. Because incorporated proteins need to be released from crystals, we verify metal chelation as a safe crystal dissolution method to avoid protein denaturation during reconstitution. Finally, we optimize the recombinant expression of OC17 which could allow engineering OC17 for engineered intracrystalline entrapment studies.

Oral Synergism of Egg-White-Derived Peptides (EWDP) and Curcumin for Colitis Mitigation via Polysaccharide/Cyclodextrin Metal-Organic Framework-Based Assemblies.

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.

Traditional cooking methods decreased the allergenicity of egg proteins.

Egg allergy is one of the most common food allergies globally. This study aimed to assess the impact of four traditional cooking methods on the allergenicity of egg proteins using a comprehensive strategy, including simulated gastrointestinal digestion in vitro, serology experiments, a rat basophilic leukemia (RBL)-2H3 cell degranulation model, and a passive cutaneous anaphylaxis (PCA) mice model, and the structure changes were detected by circular dichroism (CD) spectra and ultraviolet (UV) spectra. The results showed that the processed egg proteins were more readily digested compared to raw egg proteins. The serological experiments revealed a significant reduction in immunoglobulin E binding of egg proteins after thermal treatments (p < 0.05), particularly after frying. Subsequently, the RBL-2H3 cell degranulation experiment demonstrated a marked decrease in the level of egg allergens-induced ß-hexosaminidase release after cooking (p < 0.05). Moreover, the results from the PCA mice model indicated that the increase in vascular permeability was effectively relieved in the treated groups, especially in frying group (p < 0.05). Additionally, the α-helix and ß-turn contents of processed egg proteins were significantly decreased (p < 0.05) compared with native egg proteins. The UV spectra findings showed that all cooking treatments caused significant alterations in the tertiary structure, and fluorescence analysis indicated that cooking decreased the surface hydrophobicity of egg proteins. In conclusion, four traditional cooking methods reduced the allergenicity of egg proteins, particularly frying, and this reduction was associated with structural changes that could contribute to the destruction or masking of epitopes of egg allergens. PRACTICAL APPLICATION: Egg allergy has a serious impact on public health, and there is no ideal treatment method at present. This study demonstrated that four traditional cooking methods (boiling, steaming, baking, and frying) reduced the allergenicity of egg proteins, especially frying, and the results will provide a basis for the development of hypoallergenic egg products.

Integrating Computational and Experimental Methods to Identify Novel Sweet Peptides from Egg and Soy Proteins.

Sweetness in food delivers a delightful sensory experience, underscoring the crucial role of sweeteners in the food industry. However, the widespread use of sweeteners has sparked health concerns. This underscores the importance of developing and screening natural, health-conscious sweeteners. Our study represents a groundbreaking venture into the discovery of such sweeteners derived from egg and soy proteins. Employing virtual hydrolysis as a novel technique, our research entailed a comprehensive screening process that evaluated biological activity, solubility, and toxicity of the derived compounds. We harnessed cutting-edge machine learning methodologies, specifically the latest graph neural network models, for predicting the sweetness of molecules. Subsequent refinements were made through molecular docking screenings and molecular dynamics simulations. This meticulous research approach culminated in the identification of three promising sweet peptides: DCY(Asp-Cys-Tyr), GGR(Gly-Gly-Arg), and IGR(Ile-Gly-Arg). Their binding affinity with T1R2/T1R3 was lower than -15 kcal/mol. Using an electronic tongue, we verified the taste profiles of these peptides, with IGR emerging as the most favorable in terms of taste with a sweetness value of 19.29 and bitterness value of 1.71. This study not only reveals the potential of these natural peptides as healthier alternatives to traditional sweeteners in food applications but also demonstrates the successful synergy of computational predictions and experimental validations in the realm of flavor science.

Assessing the structural and foaming property changes in egg yolk proteins due to malondialdehyde: Experimental and molecular docking studies.

This study evaluated the effects of varying levels of malondialdehyde (MDA) on the structural and foaming properties of the egg yolk proteins (EYPs), and the interaction between them was explored by molecular docking. The results showed that oxidative modification due to MDA increased the carbonyl content of EYPs by 4.49 times. Simultaneously, the total sulfhydryl content was reduced by 21.47%, and the solubility of EYPs was significantly decreased (p < 0.05). Continuous oxidation disorders the previously ordered structure of EYPs. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis indicated that some proteins underwent crosslinking and aggregation with increased MDA oxidation, aligning with changes in particle size and zeta-potential. Moderate oxidation (<1 mmol/L) enhanced the foaming capacity and foam stability of EYPs. Additionally, molecular docking results uncovered favorable interactions between MDA and specific EYPs, primarily through hydrogen bonding. This research offers valuable insights into managing the functional and quality changes of yolk products during processing.

A promising food-grade protector for Retinyl acetate emulsions with fibrillated egg white.

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.

Endogenous reactive oxygen species (ROS)-driven protein oxidation regulates emulsifying and foaming properties of liquid egg white.

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.

Mechanism of ultrasound-induced soybean/egg white composite gelation: Gel properties, morphological structure and co-aggregation kinetics.

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 (Amax) because EWP could aggregate with SPI at a higher rate (Kapp), 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.

Integrated landscape of chicken egg chalaza proteomics.

Chicken egg chalaza (CLZ) is a natural colloidal structure in eggs that exists as an egg yolk stabilizer and is similar in composition to egg white. In this study, the proteome, phosphoproteome, and N-glycoproteome of CLZ were characterized in depth. We hydrolyzed the CLZ proteins and enriched the phosphopeptides and glycopeptides. We identified 45 phosphoproteins and 80 N-glycoproteins, containing 59 phosphosites and 203 N-glycosylation sites, respectively. Typically, the ovalbumin in CLZ was both phosphorylated and N-glycosylated, with 4 phosphosites and 4 N-glycosylation sites. Moreover, we identified 2 N-glycosylated subunits of ovomucin, mucin-5B and mucin-6, with 32 and nine N- glycosylation sites, respectively. Analysis of the phosphorylation and N-glycosylation status of CLZ proteins could provide novel insights into the structural and functional characteristics of CLZ.

Advances in Understanding the Antioxidant and Antigenic Properties of Egg-Derived Peptides.

Pepsin, trypsin and proteinase K were used in the present study to hydrolyse the proteins from whole eggs, yolks or whites, and the resulting hydrolysates were characterised in terms of antioxidant and IgE-binding properties, using a combination of in vitro and in silico methods. Based on the degree of hydrolysis (DH) results, the egg yolk proteins are better substrates for all the tested enzymes (DH of 6.2-20.1%) compared to those from egg whites (DH of 2.0-4.4%). The SDS-PAGE analysis indicated that pepsin and proteinase K were more efficient compared to trypsin in breaking the intramolecular peptide bonds of the high molecular weight egg proteins. For all the tested substrates, enzyme-assisted hydrolysis resulted in a significant increase in antioxidant activity, suggesting that many bioactive peptides are encrypted in inactive forms in the parent proteins. The hydrolysates obtained with proteinase K exhibited the highest DPPH radical scavenging activity (124-311 µM Trolox/g protein) and the lowest residual IgE-binding capacity. The bioinformatics tools revealed that proteinase K is able to break the integrity of the main linear IgE-binding epitopes from ovalbumin and ovomucoid. It can be concluded that proteinase K is a promising tool for modulating the intrinsic properties of egg proteins.

Proteomic Analysis of Egg Yolk Proteins During Embryonic Development in Wanxi White Goose.

To investigate the alterations of yolk protein during embryonic development in Wanxi white goose, the egg yolk protein composition at days 0, 4, 7, 14, 18, and 25 of incubation (D0, D4, D7, D14, D18, and D25) was analyzed by two-dimensional gel electrophoresis combined with mass spectrometry. A total of 65 spots representing 11 proteins with significant abundance changes were detected. Apolipoprotein B-100, vitellogenin-1, vitellogenin-2-like, riboflavin-binding protein, and serotransferrin mainly participated in nutrient (lipid, riboflavin, and iron ion) transport, and vitellogenin-2-like showed a lower abundance after D14. Ovomucoid-like were involved in endopeptidase inhibitory activity and immunoglobulin binding and exhibited a higher expression after D18, suggesting a potential role in promoting the absorption of immunoglobulin and providing passive immune protection for goose embryos after D18. Furthermore, myosin-9 and actin (ACTB) were involved in the tight junction pathway, potentially contributing to barrier integrity. Serum albumin mainly participated in cytolysis and toxic substance binding. Therefore, the high expression of serum albumin, myosin-9, and ACTB throughout the incubation might protect the developing embryo. Apolipoprotein B-100, vitellogenin-1, vitellogenin-2-like, riboflavin-binding protein, and serotransferrin might play a crucial role in providing nutrition for embryonic development, and VTG-2-like was preferentially degraded/absorbed.

Effects of freezing on the gelation behaviors of liquid egg yolks affected by saccharides: thermal behaviors and rheological and structural changes.

Monitoring and controlling the freezing process and thermal properties of foods is an important means to understand and maintain product quality. Saccharides were used in this study to regulate the gelation of liquid egg yolks induced by freeze‒thawing; the selected saccharides included sucrose, L-arabinose, xylitol, trehalose, D-cellobiose, and xylooligosaccharides. The regulatory effects of saccharides on frozen egg yolks were investigated by characterizing their thermal and rheological properties and structural changes. The results showed that L-arabinose and xylitol were effective gelation regulators. After freeze‒thawing, the sugared egg yolks exhibited a lower consistency index and fewer rheological units than those without saccharides, indicating controlled gelation. Weaker aggregation of egg yolk proteins was confirmed by smaller aggregates observed by confocal laser scanning microscopy and smaller particle sizes. Saccharides alleviated the freeze-induced conversion of α-helices to ß-sheets in egg yolk proteins, exposing fewer Trp residues. Overall, L-arabinose showed the greatest improvement in regulating the gelation of egg yolks, followed by xylitol, which is correlated with its low molecular weight.

Effect of salting and dehydration treatments on the physicochemical and gel properties of hen and duck egg yolks, plasma and granules.

BACKGROUND: Salted hen egg yolks are less oily and less flavorful than salted duck egg yolks. However, hen eggs have a more adequate market supply and have a broader application prospect than duck eggs. In the present study, egg yolks, plasma, and granules were dehydrated by adding 1% NaCl to simulate traditional curing process of salted egg yolk. The changes in the pickling process of hen egg yolks (HEY) and duck egg yolks (DEY) plasma and granules were compared to reveal the gelation mechanism and the underlying causes of quality differences in salted HEY and DEY. Salted HEY can be compared with the changes in DEY during the pickling process to provide a theoretical basis for the quality improvement of salted HEY to salted DEY. RESULTS: The results showed that both plasma and granules were involved in gel formation, but exhibited different aggregation behaviors. Based on the intermolecular forces, the HEY proteins achieved aggregation mainly through hydrophobic interactions and DEY proteins mainly through covalent binding. According to spin-spin relaxation time, HEY gels immobilized a large amount of lipid and interacted strongly with lipids. DEY gels showed much free lipid and had weak interaction with lipid. The microstructure showed that HEY proteins were easily unfolded to form a homogeneous three-dimensional gel network structure after salting, whereas heterogeneous aggregates were formed to hinder the gel development in DEY. Changes in protein secondary structure content showed that pickling can promote the transformation of the α-helices to ß-sheets structure in HEY gels, whereas more α-helices structure was formed in DEY gels. CONCLUSION: The present study has demonstrated that different gelation behaviors of hen and duck egg yolk proteins (especially in plasma) through salting treatment led to the difference in the quality of salted HEY and DEY. © 2024 Society of Chemical Industry.

The effects of sucrose/NaCl combined pickling on the textural characteristics, moisture distribution, and protein aggregation behavior of egg yolk.

Salted egg yolks have a tender, loose, gritty, and oily texture and are commonly employed as fillings in baked goods. This study investigated the formation mechanism of egg yolk gels using three different pickling methods: NaCl, sucrose, and mixed groups. The results revealed that of these pickling methods, egg yolks pickled with the mixture had the lowest moisture content (11.59% at 25°C and 10.21% at 45°C), almost no free water content, and the highest hardness (19.11 N at 25°C and 31.01 N at 45°C). Intermolecular force measurements indicated that pickling with the mixture mitigated the surface hardening effect of sucrose and facilitated protein cross-linking. Moreover, confocal laser scanning microscopy of the egg yolk gels pickled with the mixture displayed macromolecular aggregates and oil exudation, suggesting that this method partially disrupted the lipoprotein structure and notably promoted yolk protein aggregation and lipid release. Overall, egg yolks formed a dense gel via the mixed pickling method owing to the ionic concentration and dehydration effects. These findings show the impact of NaCl and sucrose in pickling egg yolks, providing a crucial foundation for developing innovative and desirable egg yolk products. PRACTICAL APPLICATION: This study introduces a novel pickling strategy that combines sucrose and NaCl for egg yolk processing. The egg yolk pickled using this method exhibited improved quality according to the evaluated textural characteristics, moisture distribution, and protein aggregation behavior. The findings may broaden the use of sucrose as a pickling agent for egg yolk processing and provide new ideas for developing and producing pickled eggs and other food products.

Effect of high-hydrostatic pressure on the digestibility of egg yolk and granule.

The impact of high hydrostatic pressure (HHP) on protein digestibility of egg yolk and egg yolk granule was evaluated by static in vitro digestion using the standardized INFOGEST 2.0 method. The degree of hydrolysis (DH) and the phospholipid content were determined during digestion, and the protein and peptide profiles were characterized by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and reverse phase-high pressure liquid chromatography (RP-HPLC). The results showed that HHP induced protein aggregation in egg yolk and granule, mainly by disulfide bridges, which were not disrupted in the oral phase. Proteolysis during the gastric phase improved egg yolk and granule protein solubility, regardless of whether HHP was applied. However, the extent of the samples' digestibility was not affected, with DH values ranging from 15% to 20%. During the intestinal phase, the DH of egg yolk protein (∼40%) was higher than that of the granule (∼25%), probably due to the denser structure of the granule reducing the accessibility of intestinal enzymes. The DH, peptide, and protein profiles of control and HHP-treated egg yolk showed similar protein digestion behaviors for both gastric and intestinal phases. Among the different proteins, only the digestibility of ß-phosvitin in HHP-treated granule was enhanced. Consequently, applying HHP to granules represents an interesting process that improves the digestibility of phosvitin with the potential to generate bioactive phosvitin-derived phosphopeptides. PRACTICAL APPLICATION: High hydrostatic pressure, mainly used as a preservation process, did not impair the nutritional quality of the egg yolk and granule proteins but improved the susceptibility of phosvitin (protein contained in egg yolk) proteolysis to produce bioactive phosphopeptides. Consequently, applying HHP to granules represents an interesting process that improves the digestibility of phosvitin.

Positive selection in gamete interaction proteins in Carnivora.

The absence of robust interspecific isolation barriers among pantherines, including the iconic South American jaguar (Panthera onca), led us to study molecular evolution of typically rapidly evolving reproductive proteins within this subfamily and related groups. In this study, we delved into the evolutionary forces acting on the zona pellucida (ZP) gamete interaction protein family and the sperm-oocyte fusion protein pair IZUMO1-JUNO across the Carnivora order, distinguishing between Caniformia and Feliformia suborders and anticipating few significant diversifying changes in the Pantherinae subfamily. A chromosome-resolved jaguar genome assembly facilitated coding sequences, enabling the reconstruction of protein evolutionary histories. Examining sequence variability across more than 30 Carnivora species revealed that Feliformia exhibited significantly lower diversity compared to its sister taxa, Caniformia. Molecular evolution analyses of ZP2 and ZP3, subunits directly involved in sperm-recognition, unveiled diversifying positive selection in Feliformia, Caniformia and Pantherinae, although no significant changes were linked to sperm binding. Structural cross-linking ZP subunits, ZP4 and ZP1 exhibited lower levels or complete absence of positive selection. Notably, the fusion protein IZUMO1 displayed prominent positive selection signatures and sites in basal lineages of both Caniformia and Feliformia, extending along the Caniformia subtree but absent in Pantherinae. Conversely, JUNO did not exhibit any positive selection signatures across tested lineages and clades. Eight Caniformia-specific positive selected sites in IZUMO1 were detected within two JUNO-interaction clusters. Our findings provide for the first time insights into the evolutionary trajectories of ZP proteins and the IZUMO1-JUNO gamete interaction pair within the Carnivora order.

Heat-induced gelation of egg white proteins depending on heating temperature: Insights into protein structure and digestive behaviors in the elderly in vitro digestion model.

This study investigated the effects of heating temperature of egg white gels (EWGs) on the digestive characteristics by heating egg white (EW) to reach 75 °C (EWG-75) and 95 °C (EWG-95). The gel protein structure showed a decrease in the maximum tryptophan fluorescence intensity and a significant increase in the surface hydrophobicity of EWGs compared to EW (P < 0.05). The total and reactive free sulfhydryl groups were higher in the EWGs than in the EW (P < 0.05). While the proportions of α-helical and ß-sheet structures remained similar in EW and EWG-75 (P > 0.05), EWG-95 exhibited a notable decrease in α-helix content (P < 0.05) and an increase in ß-sheet content (P < 0.05). Furthermore, EWG-95 displayed higher hardness and cohesiveness than EWG-75 (P < 0.05). In the adult and elderly in vitro digestion models, EWG-95 exhibited the highest protein digestibility (50.44 % and 54.65 % in the models of elderly and adult subjects, respectively) after GI digestion (P < 0.05), followed by EWG-75 and EW. The electrophoretogram of the digesta revealed more intense protein bands in the elderly digestion model, particularly in the gastric digesta of EW, indicating slower digestion compared to the adult model. Therefore, EW should be appropriately heated before consumption, especially for elderly individuals, to facilitate efficient protein digestion and absorption.

Inhibition of water-diluted precipitate formation from egg whites by ultrasonic pretreatment: Insights from quantitative proteomics analysis.

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 ß-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.

High-temperature glycosylation of saccharides to modify molecular conformation of egg white protein and its effect on the stability of high internal phase emulsions.

This paper investigates the freeze-thaw stability of oil-in-water emulsions stabilized by high-temperature wet heating glycosylation products. Glucose (Glu), D-fructose (Fru), xylose (Xyl), maltodextrin (MD), oligofructose (FO), and oligomeric isomaltulose (IMO) were chosen as sugar sources for the glycosylation reaction with egg white proteins (EWPs) at 120 °C to prepare the GEWPs. The study reveals that the type of sugar significantly influences the Maillard reactions with EWPs. The degree of glycosylation was highest in the Xyl group with the greatest reducing capacity and lowest in the MD, FO, and IMO groups. High-temperature wet glycosylation treatment induced changes in the secondary and tertiary structures of EWP. Elevated temperature exposed hydrophobic groups within the protein, while covalent binding of hydrophilic carbohydrates via the Maillard reaction decreased the protein's H0 value. Improved foaming and emulsifying properties were attributed to the increase in α-helix content, disulfide bond formation, and reduced surface tension. Emulsions prepared from GEWPs exhibited higher apparent viscosity and G' compared to those from natural EWPs, with the GEWP/Xyl group showing the highest values. After freeze-thaw treatment, the GEWP/Fru and GEWP/FO groups demonstrated superior stability and reduced freezing point, along with minimal microstructural alterations. These findings underscore the importance of sugar type in the stability of high internal phase emulsions (HIPEs) stabilized by GEWPs, indicating that a tailored Maillard reaction can yield stabilizers with exceptional freeze-thaw stability for emulsions.

The influence of unique interfacial networks based on egg white proteins for the stabilization of high internal phase Pickering emulsions: Physical stability and free fatty acid release kinetics.

This study was oriented towards the impacts of unique interfacial networks, formed by glycosylated and non-glycosylated egg white proteins, on the characteristics of high internal phase Pickering emulsions (HIPPEs). Glycosylated egg white protein particles (EWPG) manifested a more compact protein tertiary structure and amplified surface hydrophobicity, forming durable coral-like networks at the oil-water interface. The non-glycosylated egg white protein particles (EWP) could form spherical cluster interfacial networks. Raman spectroscopy analysis illuminated that EWPG could exhibit better interactions with aliphatic amino acids via hydrogen bonds and hydrophobic interactions. The release of free fatty acid (FFA) from both HIPPEs followed the first-order kinetic model with a combination of diffusion. EWPG-stabilized HIPPEs demonstrated superior physical stability and cellular antioxidant activity. This research shed light on the promising prospects of HIPPEs as promising amphiphilic delivery systems with capabilities to co-deliver hydrophilic and hydrophobic nutraceuticals and amplify their intracellular biological potency.