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Chicken egg whites contain hundreds of proteins, and are widely used in the food, biological and pharmaceutical industries. It is highly significant to study the separation and purification of egg white proteins. This review first describes the structures and functional properties of several major active proteins in egg whites, including ovalbumin, ovotransferrin, ovomucoid, lysozyme, ovomucin, ovomacroglobulin and avidin. Then, the common techniques (including precipitation, chromatography and membrane separation) and some novel approaches (including electrophoresis, membrane chromatography, aqueous two-phase system and molecular imprinting technology) for the separation and purification of egg white proteins broadly reported in the current research are introduced. In addition, several co-purification methods for simultaneous separation of multiple proteins from egg whites have been developed to improve raw material utilization and reduce costs. In this paper, the reported techniques in the last decade for the separation and purification of chicken egg white proteins are reviewed, discussed and prospected, aiming to provide a reference for further research on egg proteins in the future. [ABSTRACT FROM AUTHOR]

Abstract: The present study is aimed to investigate the effect of hydroxyl radical‐induced oxidation on the structure and gel properties of chicken ovalbumin. With the increase in oxidation time and H2O2 dose, the carbonyl content in ovalbumin increased, while the free sulfhydryl content decreased. The effect of oxidation on the structure of ovalbumin was examined, and the results indicated that the disorder level increased. Oxidation of ovalbumin lowered the solubility, and the viscosity of the solution decreased significantly. Oxidation weakened the water holding capacity and gel hardness, as well as resulting in significant changes in the microstructure of ovalbumin gels. Hydroxyl radical‐induced oxidation caused destabilization of the ovalbumin structure, thereby affecting the heat‐induced gel properties. Practical applications: The present study demonstrated the effect of hydroxyl radical‐induced oxidation on chicken OVA, concluding that the oxidation might be one of the primary reasons for the degradation of its gel properties. Consequently, avoiding protein oxidation during storage and processing would help maintain the functional properties of the chicken egg white. Therefore, this study provides important information for the research and application of ovalbumin. [ABSTRACT FROM AUTHOR]

An efficient one-step grafting approach was developed to modify ovalbumin (OVA) by phosphorylation through selective reaction with the hydroxyl group of Ser and Thr residues present in OVA. The site-specific phosphorylated conjugates were characterized by Matrix-Assisted Laser Desorption Ionization-Time-of-Flight Mass Spectrometry (MALDI-TOF/MS) and the results indicated that the Ser residue could be more readily phosphorylated, and the typical phosphopeptides 264 LTEWTSSNVMEER 276 and 340 EVVGSAEAGVDAASVSEEFR 359 demonstrated the formation of monophosphoester. Moreover, 13 C NMR analysis showed that the βCH 2 of Ser acted as a hydroxyl donor to react with sodium tripolyphosphate (STPP), and the conjugates with variable phosphorylation sites could improve the weak network and the resulting poor mechanical properties of ovalbumin-based hydrogels. Furthermore, small-amplitude oscillatory measurements, creep recovery tests and texture profile analysis of hardness and stickiness indicated that phosphorylation can strengthen the intermolecular cross-linking of protein molecules and produce significant influence on the rheological behavior and texture properties, suggesting that a suitable conjugation site is essential for the best gelation properties at a different pH. The integrated results indicate that phosphorylation change significantly modify the viscoelastic and mechanical properties of OVA-based hydrogels by changing molecular dynamics upon heating. [ABSTRACT FROM AUTHOR]

BACKGROUND Physical changes such as chicken egg white thinning and egg yolk flattening occur during storage, implying a decline in egg quality. To reveal the deteriorative process related to chicken egg internal quality, a comparative proteomic method was used in this study to analyze the alterations in egg yolk plasma proteins at different storage times (0, 20 and 40 days) under an ambient temperature of 22 ± 2 °C. RESULTS Using two-dimensional electrophoresis followed by matrix-assisted laser desorption/ionization time-of-flight tandem mass spectrometry, 33 protein spots representing 12 proteins were identified with significant ( P < 0.05) alterations in abundance at different storage times. The proteins that showed significant changes in abundance included serum albumin, vitellogenin fragments, IgY chains, ovalbumin, ovoinhibitor, α2-macroglobulin-like protein 1-like, hemopexin, transthyretin, apolipoprotein A-I and β2-glycoprotein I precursor. Accelerating degradation for most egg yolk plasma proteins was observed after prolonged storage (from day 20 to day 40). CONCLUSION It is likely that the increased degradation of protease inhibitors such as ovoinhibitor and α2-macroglobulin-like protein 1-like during prolonged storage lead to an imbalance of protease and antiprotease in egg yolk, which may play a key role in the degradation of egg yolk proteins. These findings will provide an insight into the effects of storage on egg yolk protein changes and give a deeper understanding of the deteriorative process of chicken egg yolk. © 2016 Society of Chemical Industry [ABSTRACT FROM AUTHOR]

Abstract: Avian egg albumen participates in embryonic development by providing essential nutrients as well as antimicrobial protection. Although various biological functions of egg white proteins were suggested during embryogenesis, global changes of these proteins under incubation conditions remained uninvestigated. This study presents a proteomic analysis on the change of egg white proteins during the first week of embryonic development. By using 2-DE, together with MALDI-TOF MS/MS, thirty protein spots representing eight proteins were identified showing significant changes in abundance during incubation. An accelerating degradation of ovalbumin was observed in a wide range of molecular weight. In addition, four protein complexes were predicted according to the detected molecular weight increase. Among these speculated protein complexes, an ovalbumin spot coupled with RNA-binding protein was detected. The absence of these protein complexes before incubation, followed by the constant increase in abundance during incubation indicates conceivable pivotal roles in embryonic development. To better understand the function of the proteins identified in this study, discrepancies of egg white protein changes between fertilized and unfertilized chicken eggs were additionally demonstrated. These findings will provide insight into the embryogenesis process to improve our knowledge of egg white proteins in regulating and supporting early embryonic development. [Copyright &y& Elsevier]

In this work, ovalbumin (OVA) was phosphorylated by dry-heating at three different pH values (5.0, 7.0 and 9.0) and 45 °C for 12 h in the presence of sodium tripolyphosphate (STP). The results indicated that, when compared with native OVA (N-OVA), the zeta potential absolute value of phosphorylated OVA (PP-OVA) increased from 2.13 mv (N-OVA) to 13.57(PP-OVA-pH5.0), 16.00(PP-OVA-pH 7.0) and 11.20 mv (PP-OVA-pH 9.0); the volume-weighted mean diameter (D [4,3])of emulsions stabilized by the N- and PP-OVA decreased from 70.22 μm (N-OVA) to 37.16(PP-OVA-pH 5.0), 16.21(PP-OVA-pH 7.0) and 43.52 μm (PP-OVA-pH 9.0); and PP-OVA emulsions exhibited a more narrow monomodal size distribution and a smaller particle size than those of N-OVA, with the corresponding emulsifying activities index (EAI) increased from 92.71(N-OVA) to 142.51(PP-OVA-pH5.0), 224.88(PP-OVA-pH 7.0), and 150.97(PP-OVA-pH 9.0), respectively. The microscopic observation showed that the emulsion droplets of PP-OVA were more densely and uniformly distributed than those of N-OVA. Furthermore, characterization of PP-OVA by Fourier transform infrared spectroscopy (FTIR), X-ray photoelectron spectroscopy (XPS), and 31 P nuclear magnetic resonance ( 31 P NMR) revealed that phosphate groups were bound to the -OH on serine and threonine and the -NH 2 on lysine and arginine, with covalent interactions (C–O–P and C-N-P bounds) formed between OVA and STP. This study demonstrated that the introduction of phosphate groups could increase the amount of negative charge and intermolecular repulsion, decrease the particle size of droplets and improve the emulsifying ability of PP-OVA. [ABSTRACT FROM AUTHOR]

This study prepared emulsion gels by modifying ovalbumin (OVA)-flaxseed oil (FSO) emulsions with transglutaminase (TGase) and investigated their properties, structure and oxidative stability under different enzyme reaction times. Here, we found prolonged reaction times led to the transformation of α-helix and β-turn into β-sheet and random coil. The elasticity, hardness and water retention of the emulsion gels increased significantly, but the water-holding capacity decreased when the reaction time exceeded 4 h. Confocal laser scanning microscope (CLSM) indicated extended enzyme reaction time fostered oil droplet aggregation with proteins. Emulsion gel reduced FSO oxidation, especially after 4 h of the enzyme reaction, the peroxide value (PV) of the emulsion gel was reduced by 29.16% compared to the control. In summary, the enzyme reaction time of 4 h resulted in the formation of a dense gel structure and enhanced oxidative stability. This study provides the potential applications in functional foods and biomedical fields. [Display omitted] • A novel FSO - encapsulated emulsion gel was constructed by inducing OVA with TGase. • Extended enzymatic reaction time improved emulsion gel properties and structure. • TGase - treated OVA aggregated more on the surface of the oil droplets. • Emulsion gel enhanced the oxidative stability of FSO during storage. [ABSTRACT FROM AUTHOR]

Hydrogels could be used as wound dressings, but most protein-based hydrogels lack anti-bacterial effects. Here, we successfully prepared a silver ion cross-linked thiolated protein hydrogel (thiolated Ovalbumin and Gelatin, O3G7). The wound photographs showed that the healing rate (96.23 %) of hydrogel-treated mice was higher than the control group. Meanwhile, the hydrogel increased the granulation tissue's total protein content. Furthermore, it significantly increased the collagen content, consistent with the results of Masson's trichrome (MT) staining and immunohistochemical analysis of type I collagen (Col I). The results of hematoxylin and eosin (H&E) staining showed the growth and proliferation of inflammatory cells, granulation tissue, fibroblasts, blood vessels and hair follicles in acute wounds. O3G7 hydrogel had fewer inflammatory cells and more neovascularization, and hair follicle tissue and intact epidermis could be observed. The results of immunofluorescence and immunohistochemistry showed that the O3G7 group reduced the expression of tumor necrosis factor (TNF)-α (56.87 % of the control group) and upregulated the expression of transforming growth factor (TGF)-β (1.29 times of the control group). These results suggest that O3G7 hydrogel significantly affects the healing of acute wounds. This study demonstrates that hydrogels prepared from food-derived proteins will be promising and bio-safe candidates in bioengineering. [Display omitted] • Silver icon brought the general protein-based hydrogel with antibacterial activity. • The thiolated protein hydrogel has both a dense structure and excellent biocompatibility. • The tOVA/tGel@Ag hydrogels accelerate the healing of acute wounds in mice observably. [ABSTRACT FROM AUTHOR]

Abstract In this study, ovalbumin (OVA) was phosphorylated under wet-heating in the presence of sodium tripolyphosphate at pH 6.0 and 60 °C for 1, 2, 3, 4 and 5 h, and the structural and physical properties of phosphorylated OVA (P-OVA) were investigated. The FT-IR spectrum confirmed the covalent attachment of the phosphate group to OVA. New possible phosphate sites (Ser-221, Ser-269, Tyr-281 and Ser-324) were detected by using liquid chromatography in tandem with mass spectrometry. Circular dichroism (CD) spectra demonstrated that P-OVA molecular became more flexible and disordered. The decreased fluorescence intensity indicated that the chromophore microenvironment became more exposed and polar because of conformational changes. The surface hydrophobicity (H 0) and the absolute value of zeta potential of P-OVA obtained at 5 h was 1.8 and 1.5 times higher than that of N-OVA. Foaming ability (FA) and foaming stability (FS) were enhanced by 1.7 and 4.4 times after wet-heating phosphorylation for 4 h, which were up to 87.0% and 28.5%, respectively. Furthermore, the correlation analysis suggested that FA was significantly correlated to random structure (P < 0.01) and H 0 (P < 0.01), and zeta potential was related with FS (P < 0.05). Graphical abstract Image 102 Highlights • Ovalbumin was phosphorylated by sodium tripolyphosphate under wet-heating. • Possible phosphate sites were detected by LC-MS/MS. • Structural changes were confirmed by fluorescence and CD spectrum. • H 0 and the absolute value of zeta potential increased after the phosphorylation. • Foaming ability and stability were promoted by phosphorylation. [ABSTRACT FROM AUTHOR]

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. [ABSTRACT FROM AUTHOR]

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. [ABSTRACT FROM AUTHOR]

Fluorescence resonance energy transfer (FRET), a near-field energy transfer from a fluorescent donor to a fluorescent acceptor within close proximity, has been widely used in biosensing. In this study, a rapid and universal sensor for the detection of ovalbumin (OVA) using nitrogen, oxygen, phosphoric co-doped CDs (NOP-CDs) and graphene oxide (GO) was established based on the FRET technology. First, novel NOP-CDs peak at 443 nm were synthesized by a one-pot hydrothermal method using egg powder and phosphorus acid. Then, in the absence of OVA, the fluorescence of OVA-antibody modified NOP-CDs was quenched by GO via electrostatic attraction and π-π stacking interaction due to the FRET effect. The introduced OVA competed to displace the GO by special binding with the anti-OVA, resulting in the recovery of the fluorescence. This sensor displayed a linear response to OVA from 0.5 to 15 μg/mL with a detection limit of 153 ng/mL and was successfully applied to the detection of the OVA sample with recoveries ranging from 99.25 to 118.90%. In summary, the green and easy-to-synthesize nano-material was used in this method, the accurate detection results, and the simple process exhibited the great potential of this method for practical applications. [ABSTRACT FROM AUTHOR]

During the egg storage, the change in structure of ovalbumin (OVA) was determined by spectroscopy of Fluorescence, Circular Dichroism and Fourier-Transform Raman. The relationships between the OVA properties and structure were also investigated in this study. Comparing with the consequence of Circular Dichroism and Fourier-Transform Raman spectra, it was obvious that the percentage of α-helix and β-sheet showed downward trends after storage. In contrast, the percentage of β-turn and random coil clearly presented raising trend. Furthermore, tryptophan residues were buried in a more hydrophobic environment. The emulsifying and foaming properties of OVA all decreased during the storage. Moreover, the correlation analysis indicated that β-sheet related to the emulsifying stability of OVA ( p < 0.01), α-helix related to the foaming stability ( p < 0.05) at the same time. This study provided new interesting idea for the study on the relationships between the structure and functional properties of protein during food storage. [ABSTRACT FROM AUTHOR]

[Display omitted] • Enhanced unfolding of ovalbumin was induced by succinylation combined with pH-shifting method. • Succinylation combined with pH-shifting pretreatment induced a highly strong and transparent ovalbumin hydrogel. • Uniform network structures with macroporous and thin connecting walls were formed in strong and transparent ovalbumin hydrogel. • Hydrophobic interactions and hydrogen bonds play important role in strong and transparent ovalbumin hydrogel. Ovalbumin (OVA) is a model protein with extensive research on structure and function, however, the application of OVA in food processing is limited due to its low gelation properties. In this study, thermally-induced highly transparent and elastic hydrogels from OVA pretreated by succinylation combined with pH-shifting method were reported. Transmission electron microscope (TEM) and free sulfhydryl groups determination revealed that the pretreatment induced the stretching of the protein structure and promoted the formation of preliminary aggregates. Further heating the pretreated OVA suspension resulted in a homogeneous and macroporous gel network with thin connecting walls. Such homogeneous gel network structures may be related to the effective modulation of the thermal aggregation efficiency of proteins by succinylation and the high level of protein unfolding by pH-shifting treatments, which synergistically allowed for more active sites to be created during heating to facilitate intermolecular interactions, including hydrogen bonding and hydrophobic interactions. Notably, the method resulted in a 507.14% increase in elasticity, a 60.74% increase in water holding capacity of the OVA hydrogels compared to the native OVA hydrogels without pretreatment. Also, the hydrogels were transparent with 73.11% light transmittance. In conclusion, succinylation and pH-shifting combined treatment could be an effective method for the preparation of OVA hydrogels with superior gelation properties. [ABSTRACT FROM AUTHOR]