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The thermal sterilization process of protein beverages inevitably leads to the formation of insoluble thermal aggregates, greatly reducing the texture and taste of protein beverages. In this study, homogenized egg white (HEW) was obtained by ultrahigh-high-pressure (UHP) homogenization pretreatment of egg white (EW), and then a special egg white fluid gel (EWFG) was prepared by water bath heating. The results showed that the optimal conditions for preparing EWFG were three cycles at 20 MPa homogenizing pressure and heating in a water bath at 72℃ for 10 min. Under these conditions, the EWFG was a milky-white homogeneous liquid with an average particle size of about 560 nm. Measurements of the physicochemical properties of HEW and EWFG showed that the UHP homogenization treatment reduced the viscosity of HEW, decreased the particle size of protein aggregates, and increased the zeta potential, which altered the interactions of proteins during the subsequent heating process and facilitated the formation of homogeneous and dispersed EWFG. EWFG showed good stability at pH 6-10 and in low-concentration saline and medium-concentration sucrose solutions. The EWFG obtained by the present treatment is more suitable for factory-scale production and has great potential for protein beverage applications., 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.)

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 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.)

Chicken egg whites (whole egg white, EW; thick egg white, TKEW; thin egg white, TNEW) become turbid and are accompanied by the formation of precipitates after being diluted with an equal mass of deionized water. The precipitates of TKEW induced by water dilution (Thick Egg White Precipitates, TKEWP) account for 14.47 % of TKEW total dry matter, much higher than that of thin egg white precipitates (TNEWP) (1.51 %) and whole egg white precipitates (EWP) (5.53 %). Quantitative proteomic analysis identified 27 differentially abundant proteins (p < 0.05) among EW, EWP, TNEWP, and TKEWP. Lysozyme was found to be a key protein in the formation of EW precipitates induced by water dilution, as its abundance was significantly higher in TNEWP and TKEWP. Mucin-5B (α-ovomucin) had the highest abundance in TKEWP, suggesting that its insolubility is one of the important factors contributing to the large formation of TKEWP. This paper systematically studies the formation, characteristics, and composition of egg white precipitation caused by water dilution, and puts forward a new understanding of the processing characteristics of egg white liquid, thus laying a theoretical foundation for further research methods to reduce egg white precipitation by water dilution., Competing Interests: Declaration of competing interest The authors state no conflict of interest., (Copyright © 2023 Elsevier B.V. All rights reserved.)

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.)

The protein profiles and properties of chicken egg white and its three components (thick egg white, TKEW; thin egg white, TNEW; and chalaza, CLZ) were comprehensively compared. The proteomes of TNEW and TKEW are relatively similar, but the abundance of mucin-5B and mucin-6 (the two subunits of ovomucin) is significantly higher in TKEW than in TNEW (42.97% and 870.04%, respectively), while the lysozymes in TKEW are 32.57% higher (p < 0.05) than those in TNEW. Meanwhile, the properties (including the spectroscopy, viscosity, and turbidity) of TKEW and TNEW are significantly different. Comprehensively, it is speculated that the electrostatic interactions between lysozyme and ovomucin are the main reason for the high viscosity and turbidity of TKEW. Compared with egg white sample (EW), CLZ has a higher abundance of insoluble proteins (mucin-5B, 4.23-fold; mucin-6, 6.89-fold) and a lower abundance of soluble proteins (ovalbumin-related protein X, 89.35% lower than EW; ovalbumin-related protein Y, 78.51% lower; ovoinhibitor, 62.08% lower; riboflavin-binding protein, 93.67% lower). These compositional differences should explain the insolubility of CLZ. These findings are important references for deepening the research and development of egg white in the future, such as the thinning of egg white, the molecular basis of changes in egg white properties, and the differential application of TKEW and TNEW., 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 Elsevier Ltd. 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.)

This study systematically analyzed and compared thechanges of physicochemical, functional and molecular structural characteristics between thick egg white (KEW) and thin egg white (NEW) during storage. Analysis of physicochemical properties showed that moisture content decreased significantly with the increase of pH during storage. KEW was gradually thinning, while NEW was closer to Newtonian fluid. Functional properties indicated that KEW thermal gel was gradually hard and brittle with the properties of NEW. KEW had better emulsifying property than NEW, and NEW had superior foaming ability. The α-helix and β-sheet in the FT-IR spectrum showed a downward trend, revealing secondary structure changed from order to disorder. Enhancement of fluorescence intensity indicated the structural unfolding and exposure of tryptophan residues. SDS-PAGE proved that OVO might be related to the difference between KEW and NEW characteristics. This study provided new idea and reference value for egg storage and diversified utilization of egg white., (Copyright © 2021 Elsevier Ltd. All rights reserved.)

Theaflavin (TF), which is the key pigment in black tea, is a health-promoting food component with beneficial effects on humans. However, the interactions by which these effects are transferred and exerted into protein-rich foods are unclear. Here, egg ovalbumin (OVA) was selected as a representative dietary protein to ascertain their binding mechanism. Steady-state, time-resolved fluorescence and isothermal titration calorimetric results showed that TF can interact well with OVA with an affinity magnitude of 10 4 . The noncovalent binding was mainly driven by hydrophobic interaction and hydrogen bonds. Structural analysis displayed that the TF binding pocket significantly overlapped with one of the surrounding specific IgE-binding epitopes, thereby causing a subtle structural adjustment on the secondary conformation of OVA. The biological complexation model that was delineated here will help understand how black tea dyes egg white in tea egg products and for the development of protein-rich carriers in functional foods., (Copyright © 2019 Elsevier Ltd. All rights reserved.)

In addition to small amounts of minerals and carbohydrates, most of the dry matter of chicken egg white is protein, making egg white an ideal resource for obtaining food proteins. Ovalbumin (OVA), which accounts for more than 50% of the total egg white protein, is one of the most widely studied food proteins due to its multiple functional properties, and it has also been used as a model protein molecule in many research fields. The objective of this study was to develop a simple and rapid method for the purification of OVA from egg whites on large scale. First, OVA was separated from ovomucin, ovotransferrin, and ovomucoid by polyethylene glycol (PEG) concentration, using the following optimal parameters: the PEG concentration was 15%, the pH was 6.5, the salt concentration was 100 mmol/L, and the operating temperature was 10°C. The OVA-rich supernatant obtained from PEG precipitation was further purified by isoelectric precipitation at a pI of 4.5 and a temperature of 4°C, and the purified OVA was obtained with at a purity of 95.1% by HPLC, with a yield of 46.4%. After the extraction of OVA, the PEG solution was vacuum dried and then utilized cyclically in the PEG precipitation steps. The whole purification process could be finished within 2 to 3 h at a scale of several kilograms of egg white. This method has the advantages of rapidity, simplicity, low cost, and ease of scalability., (© 2018 Poultry Science Association Inc.)

As the most abundant protein in chicken eggs, ovalbumin plays an important role in the processing of high value-added poultry products. The present study investigated the effects of hydroxyl radical-induced early stage oxidation on the physicochemical and interfacial properties of chicken egg white ovalbumin. Protein carbonyl content of ovalbumin increased (from 0.78 to 1.13 nmol/mg) with the oxidation time (0-5 h), while free sulfhydryl content (from 0.43 to 0.09 nmol/mg) and free amino group content (from 0.49 to 0.43 nmol/mg) decreased. Sodium dodecyl sulfate polyacrylamide gel electrophoresis analysis showed that the exposure of ovalbumin to hydroxyl radicals caused self-cross-linking and resulted in the formation of dimers and trimers. Accompanied by these changes, the surface hydrophobicity of ovalbumin was enhanced about 1.5-fold with the deepening of oxidation, and the value of zeta potential became more negative (from -7.15 to -20.51 mv). About 2 h of moderate oxidation improved the foaming and emulsifying properties of ovalbumin (1.2-fold to 1.8-fold), while excessive oxidation (3 h) decreased these interface properties. Hydroxyl radical-induced oxidation changed the surface chemical groups and structures of ovalbumin, thereby affecting the surface properties. The foaming and emulsifying properties of ovalbumin could be improved by oxidation, increasing the application possibilities of ovalbumin in the food interface system., (© 2018 Poultry Science Association Inc.)

Glycosylation of proteins plays an important role in their biological functions, such as allergenicity. Ovomacroglobulin (OVMG) is a glycoprotein from hen egg white, but few studies have been done so far to delineate the glycosylated sites of OVMG. The present study characterized the glycosylation of OVMG using mass spectrometry and two-dimensional electrophoresis. MALDI-TOF-MS showed that the OVMG subunit [M + H](+) ion has a peak at m/z 183297; therefore, the carbohydrate moiety is calculated as 11.5% of the whole OVMG molecule. HPLC-ESI-MS/MS confirmed that of 13 potential N-glycosylation sites of OVMG, 11 sites were glycosylated; 1 site (N(1221)) was found in both glycosylated and nonglycosylated forms. On the two-dimensional electrophoresis gel, a series of OVMG spots horizontally distributed at 170 kDa, with an isoelectric point range of 5.03-6.03, indicating the heterogeneity of glycosylation of OVMG. These results provided important information for understanding of structure, function, and potential allergenic sites of OVMG.

Hen egg white (EW) are one of the most ideal sources of active proteins, and ovomacroglobulin, as a protease inhibitor, has been demonstrated to possess numerous biological properties including antibacterial and anti-inflammatory properties as well as activity for the treatment of keratitis. The objective of this study was to develop a simple and rapid method for the purification of ovomacroglobulin from hen EW on a laboratory scale. Hen EW was diluted with an equal volume of distilled water followed by a two-step PEG precipitation to remove ovomucin and to obtain ovomacroglobulin-rich precipitate. The precipitate was dissolved and further purified by gel filtration chromatography. Ovomacroglobulin was collected with a purity of 97.0 ± 0.3% by HPLC and a yield of 62.5%. The atomic force microscopy images showed that ovomacroglobulin molecules on a mica surface emerged as an "oval-shaped plate" with a molecular volume of 1536.9 ± 330.0 nm(3) , indicating that purified ovomacroglobulin has an integrated molecular structure. With the improvement of PEG precipitation and the simplification of the chromatography, the whole purification process could be finished well within one working day. This protocol has an advantage of rapidity, and would facilitate studies of ovomacroglobulin., (© 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.)