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Astaxanthin (AST) is a natural hydrophobic nutrient with various biological activities, but its low solubility limits its application. In this study, self‐assembly nanoparticles were prepared by ovomucin (OVM) and Ca2+ with the enhancement of glycerol to deliver AST. Glycerol compressed the particle size of nanoparticles from 175.7 ± 1.8 to 142.9 ± 0.6 nm, and the nanoparticles had a strong negative charge (−28.9 ± 0.6 mV). Ultraviolet–visible spectroscopy and X‐ray diffraction (XRD) confirmed the successful encapsulation of AST in an amorphous form with a high encapsulation efficiency (82.9% ± 2.1%). Fourier transform infrared and circular dichroism analyses demonstrated that nanoparticles formation mainly involved electrostatic interactions and hydrophobic interactions. AST in nanoparticles presented excellent gastric juice resistance and sustained release ability, whereas free radical scavenging efficiency reached up to 75%. In addition, the nanoparticles had no apparent toxicity to cell viability. This study is expected to provide a new insight into the safe and efficient delivery of AST, while demonstrating the potential of OVM as a delivery carrier in the food and health industries. [ABSTRACT FROM AUTHOR]

To compare the physical and chemical changes in egg whites during storage, assisting in the evaluation of differences in egg freshness between various chicken breeds, we chose 240 blue-shelled eggs (Blue group) and 240 commercial brown-shelled eggs (Brown group) that 28-week-old hens had laid. In this study, all eggs were stored at 25 °C. The egg weight, egg components' weight and proportion, Haugh Unit value and the contents of S-ovalbumin, ovomucin and lysozyme in the thick albumen (KA) and thin albumen (NA) were measured at eight time points every 3 days until the 21st day of storage. The eggshell, yolk and KA proportions in the Brown group were significantly lower, whereas the NA proportion was significantly higher than that in the Blue group (p < 0.001). The Haugh Unit value and S-ovalbumin in the Brown group were significantly higher, whereas KA ovomucin and NA lysozyme were significantly lower than those in the Blue group (p < 0.001). There existed significant negative correlations between the KA and NA, irrespective of weight or proportion. The Haugh Unit value was significantly positively correlated with lysozyme and ovomucin, but significantly negatively correlated with S-ovalbumin. During storage, the KA weight (proportion), Haugh Unit value, lysozyme and ovomucin decreased, whereas the NA weight (proportion) and S-ovalbumin increased. At each time point, the NA lysozyme in the Brown group was lower than that in the Blue group (p < 0.05). After storage for 6 days, the KA ovomucin in the Brown group began to be lower than that in the Blue group (p < 0.05). The study showed that the weight (proportion) differences in egg components between blue-shelled eggs and commercial brown-shelled eggs are mainly due to the NA. The Haugh Unit value and albumin protein indexes of blue-shelled eggs were better than those of brown-shelled eggs, and showed mild changes during storage, indicating the better storage performance of blue-shelled eggs. [ABSTRACT FROM AUTHOR]

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. [Display omitted] • Temperature-induced changes in the morphology of egg white aggregates followed the "spherical - chain - regiment" shape rule. • The EWTG network structure followed the changing rule from "irregular bead-like" to "regular lamellar structure". • Amorphous aggregates of EWTGs disrupted the ordering and continuity of gel networks. • Amorphous aggregates based on Mucin 5B as an "aggregation core" were the main reason for the impaired texture of EWTG at 95 °C. [ABSTRACT FROM AUTHOR]

To compare the physical and chemical changes in egg whites during storage, assisting in the evaluation of differences in egg freshness between various chicken breeds, we chose 240 blue-shelled eggs (Blue group) and 240 commercial brown-shelled eggs (Brown group) that 28-week-old hens had laid. In this study, all eggs were stored at 25 °C. The egg weight, egg components’ weight and proportion, Haugh Unit value and the contents of S-ovalbumin, ovomucin and lysozyme in the thick albumen (KA) and thin albumen (NA) were measured at eight time points every 3 days until the 21st day of storage. The eggshell, yolk and KA proportions in the Brown group were significantly lower, whereas the NA proportion was significantly higher than that in the Blue group (p < 0.001). The Haugh Unit value and S-ovalbumin in the Brown group were significantly higher, whereas KA ovomucin and NA lysozyme were significantly lower than those in the Blue group (p < 0.001). There existed significant negative correlations between the KA and NA, irrespective of weight or proportion. The Haugh Unit value was significantly positively correlated with lysozyme and ovomucin, but significantly negatively correlated with S-ovalbumin. During storage, the KA weight (proportion), Haugh Unit value, lysozyme and ovomucin decreased, whereas the NA weight (proportion) and S-ovalbumin increased. At each time point, the NA lysozyme in the Brown group was lower than that in the Blue group (p < 0.05). After storage for 6 days, the KA ovomucin in the Brown group began to be lower than that in the Blue group (p < 0.05). The study showed that the weight (proportion) differences in egg components between blue-shelled eggs and commercial brown-shelled eggs are mainly due to the NA. The Haugh Unit value and albumin protein indexes of blue-shelled eggs were better than those of brown-shelled eggs, and showed mild changes during storage, indicating the better storage performance of blue-shelled eggs.

Ovomucin (OVM) is a natural glycoprotein with various biological activities but poor solubility. This study aimed to enhance the solubility of OVM by using an ultrasonic-assisted method. The effect of ultrasound (US) on the structure, thermal stability and biological functions of OVM aggregates was evaluated. It was found that insoluble OVM aggregates were dissociated and the solubility increased significantly to 90.0 % after US under 400 W for 45 min. US also improved the onset temperature (To) and denaturation temperature (Td) of OVM. More importantly, the cholesterol binding capacity of both OVM and its digestion products were significantly improved after US (p < 0.05). The gastrointestinal digestion products of US-OVM also showed higher α-amylase and α-glucosidase inhibition than native OVM aggregates. US-induced dissociation of OVM aggregates and the conversion of β-sheet and β-turn to random coil, resulting in the exposure of hydrophobic binding sites may be an important reason for the enhanced stability and adsorption capacity. These findings suggested that US was an effective method for preparing soluble OVM and improved its adsorption capacity, which can further facilitate the application of OVM in the food industry. [Display omitted] • US promoted the depolymerisation of OVM insoluble aggregates and the formation of soluble aggregates. • US improved the flow and thermal stability of OVM. • US improved the cholesterol adsorption capacity of OVM and its gastrointestinal digestion products. • The gastric and intestinal digestion products of US-OVM had the potential to control blood glucose. [ABSTRACT FROM AUTHOR]

The effects of ultrasonic treatment on the structure, functional properties and bioactivity of Ovomucin (OVM) were investigated in this study. Ultrasonic treatment could significantly enhance OVM solubility without destroying protein molecules. The secondary structure changes, including β-sheet reduction and random coil increase, indicate more disorder in OVM structure. After ultrasonic treatment, the OVM molecule was unfolded partially, resulting in the exposure of hydrophobic regions. The changes in OVM molecules led to an increase in intrinsic fluorescence and surface hydrophobicity. By detecting the particle size of protein solution, it was confirmed that ultrasonic treatment disassembled the OVM aggregations causing a smaller particle size. Field emission scanning electron microscopy (FE-SEM) images showed that ultrasonic cavitation significantly reduced the tendency of OVM to form stacked lamellar structure. Those changes in structure resulted in the improvement of foaming, emulsification and antioxidant capacity of OVM. Meanwhile, the detection results of ELISA showed that ultrasonic treatment did not change the biological activity of OVM. These results suggested that the relatively gentle ultrasound treatment could be utilized as a potential approach to modify OVM for property improvement.

Ovomucin is a key component in maintaining the viscous nature of egg white and has vast potential in the utilization of food industry. The objectives of the study were to determine the effect of different pH on the extractability and gel properties of ovomucin. After removing lysozyme through ion exchange, the diluted duck egg white was acidified to a narrow pH range (4.50, 4.75, 5.00, 5.25, 5.50, 5.75 and 6.00) to precipitate ovomucin. By comprehensive study of purity, yield, and convenience of large-scale preparation, 4.75 was chosen as the optimal pH to extract ovomucin with the highest purity of 85.17 ± 2.31% and a compromised yield of 4.60 ± 0.06 mg/g duck egg white. A series of self-supporting gels were prepared with freeze-dried ovomucin powder at room temperature upon rehydration and centrifugation, and the gels properties were highly associated with pH. Gel formed around pH 5 was the aggregate of natural globular proteins with lowest hydrophobicity and electrostatic interaction, relatively dense structure and high water-holding capacity (WHC). Stronger acidic conditions disrupted the disulfide bonds and formed a rougher spherical aggregate. Under alkaline conditions, however, the protein gradually unfolded and broke into linear basic polypeptides, thus a porous three-dimensional network was formed. Overall, this study provided insights into the formation mechanism of the "acid-tight/alkali-loose" ovomucin gels, and introduced a potential candidate for the development of bioactive substance delivery materials. [Display omitted] • The yield of ovomucin from duck white was a litter higher than that from hen. • Ratio of subunits and amino acids of ovomucin vary slightly among different species. • A self-supporting gel can easily be prepared at room temperature upon rehydration. • The extractability and gel formation of ovomucin is highly associated with pH. • Ovomucin has unique "Acid-Tight/Alkali-loose"pH-responding properties. [ABSTRACT FROM AUTHOR]

In order to explore the effects of spray freeze drying (SFD) on the structure and functional properties of ovalbumin (OVA) and ovomucin (OVM), the spray drying (SD) and vacuum freeze drying (FD)were used as the control. The structure was analyzed by low field nuclear magnetic resonance, Fourier transform infrared spectroscopy, fluorescence spectroscopy, differential scanning calorimetry and scanning electron microscope. The results show that the free water of spray freeze-dried samples is decreased, and the binding water increases and water retention increases. SFD interacting proteins α-helix and β-folding structure is large and the degree of protein aggregation is small. The fluorescence peak intensity at wavelength 340 nm is SFD>FD>SD. The denaturation temperature of SFD interacting proteins is 51.37 °C, which is lower than that of SD, and close to FD protein. SFD interacting proteins have a spherical structure and internal space is network structure. The emulsifying property, solubility, foaming ability and foam stability of the SFD interacting proteins are close to those of FD Protein, and are significantly better than those of spray dried samples (P<0.05). The apparent viscosity of the SD protein is larger than that of the SFD protein. The storage modulus is higher than the loss modulus. SFD is suitable for processing because of the high cost of FD. [ABSTRACT FROM AUTHOR]

Despite modern advances in food hygiene, food poisoning due to microbial contamination remains a global problem, and poses a great threat to human health. Especially, Listeria monocytogenes and Staphylococcus aureus are gram-positive bacteria found on food-contact surfaces with biofilms. These foodborne pathogens cause a considerable number of food poisoning and infections annually. Ovomucin (OM) is a water-insoluble gel-type glycoprotein in egg whites. Enzymatic hydrolysis can be used to improve the bioactive properties of OM. This study aimed to investigate whether ovomucin hydrolysates (OMHs) produced using five commercial enzymes (Alcalase®, Bromelain, α-Chymotrypsin, Papain, and Pancreatin) can inhibit the biofilm formation of L. monocytogenes ATCC 15313, L. monocytogenes H7962, S. aureus KCCM 11593, and S. aureus 7. Particularly, OMH prepared with papain (OMPP; 500 μg/mL) significantly inhibited biofilm formation in L. monocytogenes ATCC 15313, L. monocytogenes H7962, S. aureus KCCM 11593, and S. aureus 7 by 85.56 %, 80.28 %, 91.70 %, and 79.00 %, respectively. In addition, OMPP reduced the metabolic activity, exopolysaccharide production (EPS), adhesion ability, and gene expression associated with the biofilm formation of these bacterial strains. These results suggest that OMH, especially OMPP, exerts anti -biofilm effects against L. monocytogenes and S. aureus. Therefore, OMPP can be used as a natural anti -biofilm agent to control food poisoning in the food industry. • Papain-hydrolysates of ovomucin reduce biofilm formation of L. monocytogenes and S. aureus • Papain-hydrolysates of ovomucin downregulate the expression of biofilm-related genes in L. monocytogenes and S. aureus. • Papain-hydrolysates of ovomucin can be used as a natural anti -biofilm agent against pathogens in the food industry. [ABSTRACT FROM AUTHOR]

BACKGROUND: Cucumber plants suffer from a serious threatening disease, downy mildew, throughout the growing seasons irrespective of the weather temperature. The causal agent, Pseudoperonospora cubensis, tends to evolve rapidly upon sequential applications of chemical fungicides and generate new progeny possessing tolerance to such fungicides. Glycoproteins represent an environmentally safe alternative for chemically synthetized fungicides and do not trigger fungicide resistance. We studied the antifungal activity of four glycoproteins namely soybean β‐conglycinin, chickpea vicilin, duck egg ovomucin and catfish p22 against P. cubensis. Ten commercial fungicides of different chemical groups were used as positive controls of glycoprotein treatments. RESULTS: The results revealed that soybean β‐conglycinin and catfish p22 glycoproteins possess significant antifungal activity against P. cubensis. The amount of disease suppression caused by β‐conglycinin and p22 was comparable to the highly efficient chemical fungicides containing copper oxychloride, cymoxanil and fosetyl Al as active ingredients. Vicilin and ovomucin were less efficient biocides as they gave moderate suppression of disease severity. However, all tested glycoproteins provided full protection for the newly emerged cucumber leaves. Microscopic examination of glycoprotein‐treated leaves inferred the ability of catfish p22 and soybean β‐conglycinin to disrupt the integrity of sporangial cell walls of P. cubensis rendering them non‐viable compared to untreated ones. Expression levels of total phenolic compounds and the antioxidant enzymes catalase, superoxide dismutase and peroxidase were elevated upon glycoproteins application, which infers their involvement in disease suppression. CONCLUSION: This report emphasizes the direct and indirect roles of glycoproteins in safe management of cucumber downy mildew disease. © 2021 Society of Chemical Industry. [ABSTRACT FROM AUTHOR]

Egg white protein ovomucin and its hydrolysates were previously reported to exhibit anti-inflammatory and anti-adhesive activities. However, their potential to regulate pathogen colonization and disease severity has not been fully characterized. To investigate the effects of ovomucin (OVM) and its hydrolysates including ovomucin-Protex 26L (OP) and -pepsin/pancreatin (OPP) on host resistance to pathogen infection, a well-documented colitis model in mice for attaching and effacing E. coli pathogens, Citrobacter rodentium , was used in the current study. C57Bl/6J female mice were fed on a basal diet supplemented with OVM or its hydrolysates for 3 weeks prior to the C. rodentium challenge, with the dietary treatments continued for seven days. Body weight was not affected throughout the experimental period. OP supplementation resulted in lower ( P < 0.05) pathogen loads at 7 dpi. Attenuated colitis severity was observed in mice that received OVM and OP, as indicated by reduced colonic pathological scores and pro-inflammatory responses compared with the infected control group. In contrast, OPP consumption resulted in enhanced C. rodentium colonization and disease severity. Notably, reduced microbial diversity indices of the gut microbiota were observed in the OPP-supplemented mice compared with the OVM- and OP-supplemented groups. This study showed the potential of OVM and OP to alleviate the severity of colitis induced by infection while also suggesting the opposite outcome of OPP in mitigating enteric infection.

Ovomucin (OM), which has insoluble fractions is a viscous glycoprotein, found in egg albumin. Enzymatic hydrolysates of OM have water solubility and bioactive properties. This study investigated that the immunostimulatory effects of OM hydrolysates (OMHs) obtained by using various proteolytic enzymes (Alcalase ® , bromelain, α-chymotrypsin, Neutrase ® , pancreatin, papain, Protamax ® , and trypsin) in RAW 264.7 cells. The results showed that OMH prepared with pancreatin (OMPA) produced the highest levels of nitrite oxide in RAW 264.7 cells, through upregulation of inducible nitric oxide synthase mRNA expression. The production of pro-inflammatory cytokines such as tumor necrosis factor-α and interleukin-6 were increased with the cytokines mRNA expression. The effect of OMPA on mitogen-activated protein kinase signaling pathway was increased the phosphorylation of p38, c-Jun NH2-terminal kinase, and extracellular signal-regulated kinase in a concentration-dependent manner. Therefore, OMPA could be used as a potential immune-stimulating agent in the functional food industry., Competing Interests: The authors declare no potential conflicts of interest., (© Korean Society for Food Science of Animal Resources.)

Intestinal dysfunction, which may cause a series of metabolic diseases, has become a worldwide health problem. In the past few years, studies have shown that consumption of poultry eggs has the potential to prevent a variety of metabolic diseases, and increasing attention has been directed to the bioactive proteins and their peptides in poultry eggs. This review mainly focused on the biological activities of an important egg-derived protein named ovomucin. Ovomucin and its derivatives have good anti-inflammatory, antioxidant, immunity-regulating and other biological functions. These activities may affect the physical, biological and immune barriers associated with intestinal health. This paper reviewed the structure and the structure-activity relationship of ovomucin，the potential role of ovomucin and its derivatives in modulation of intestinal health are also summarized. Finally, the potential applications of ovomucin and its peptides as functional food components to prevent and assist in the pretreatment of intestinal health problems are prospected. Unlabelled Image [ABSTRACT FROM AUTHOR]

Enterotoxigenic Escherichia coli (ETEC) K88 is the most common cause of diarrhea in neonatal and postweaning pigs. After adhering to small intestinal epithelial cells via glycoprotein receptor recognition, the pathogen can produce enterotoxins, impair intestinal integrity, trigger watery diarrhea, and induce inflammation via nuclear factor κB (NF-κB) and mitogen-activated protein kinase phosphatase (MAPK) pathways. Inhibiting ETEC K88 adhesion to cell surfaces by interfering with the receptor-fimbriae recognition provides a promising strategy to prevent the initiation and progression of infection. Ovomucin is a highly glycosylated protein in chicken egg white with diverse bioactivities. Ovomucin hydrolysates prepared by the enzymes Protex 26L (OP) and pepsin/pancreatin (OPP) were previously revealed to prevent adhesion of ETEC K88 to IPEC-J2 cells. Herein, we investigated the protective effects of ovomucin hydrolysates on ETEC K88-induced barrier integrity damage and inflammation in IPEC-J2 and Caco-2 cells. Both hydrolysates inhibited ETEC K88 adhesion to cells and protected epithelial cell integrity by restoring transepithelial electronic resistance (TEER) values. Removing sialic acids in the hydrolysates reduced their antiadhesive capacities. Ovomucin hydrolysates suppressed ETEC-induced activation of NF-κB and MAPK signaling pathways in both cell lines. The ability of ETEC K88 in activating calcium/calmodulin-dependent protein kinase 2 (CaMK II), elevating intracellular Ca 2+ concentration, and inducing oxidative stress was attenuated by both hydrolysates. In conclusion, this study demonstrated the potential of ovomucin hydrolysates to prevent ETEC K88 adhesion and alleviate inflammation and oxidative stress in intestinal epithelial cells.

Background: Many children are consuming some egg when they are diagnosed with egg allergy. We hypothesized that egg consumption could modify the diagnostic performance of allergy tests., Objective: To stratify diagnostic performance of tests according to egg consumption status., Methods: The BAT2 study (NCT03309488) participants underwent oral food challenge (OFC), food-frequency questionnaires, skin prick test (SPT), specific immunoglobulin E (sIgE) and specific immunoglobulin G4 (sIgG4) and basophil activation test (BAT)., Results: At study entry, 45% of participants reported partial egg consumption ("consumers") and 55% were avoiding egg strictly ("avoiders"). Avoiders had larger SPT (P < .001), higher BAT to egg (P < .001), sIgE to egg white (EW; P = .001) and to ovalbumin (OVA; P = .001), but not to ovomucoid (P = .231). Consumers had higher levels of sIgG4 to all egg allergens (P < .001) than avoiders. In consumers, the test with the best diagnostic performance was BAT (area under the curve [AUC] = .912) followed by SPT to raw egg (AUC = 0.805), EW-sIgE (AUC = 0.738), and OVA-sIgE (AUC = 0.732). In avoiders, the best tests were BAT (AUC = 0.834) and EW-sIgE (AUC = 0.833) followed by OVA-sIgE (AUC = 0.793) and SPT to EW (AUC=0.789). Using 100% sensitivity and 100% specificity cut-offs, the proportion of patients requiring OFC were 33% for BAT, 53% for SPT to raw egg, 61% for OVA-sIgE, and 73% for EW-sIgE for consumers; and 73% for BAT, 79% for EW-sIgE, and 93% for SPT to EW for avoiders., Conclusions: The diagnostic performance of tests is influenced by the immunomodulatory effect of egg consumption. BAT is the most reliable test and reduced the need for OFC, particularly in partial egg consumers., (Copyright © 2024 The Authors. Published by Elsevier Inc. All rights reserved.)

Background: There are no indices to monitor desensitization by low-dose egg oral immunotherapy (eOIT)., Objective: We aimed to examine the relationship between desensitization by low-dose eOIT and the changes in allergen-specific immunoglobulin E (IgE) and IgG4 levels., Methods: We carried out low-dose eOIT in 31 patients with severe egg allergy in our previous two studies. After 4 months of treatment, the patients with no observed allergic symptoms in response to the open hard-boiled egg white challenge tests were classified as the negative group, and the remaining patients, the positive group. The fold-difference levels were calculated using 10 Log (Titer after eOIT/Titer before eOIT)., Results: The 28 patients who completed eOIT with sufficient serum collected before and after eOIT were analyzed. The median fold-difference levels of ovomucoid-specific IgE in the negative and positive groups were 0.819 and 0.953, respectively (P = 0.082). The median fold-difference levels of ovalbumin-specific IgG4 in the negative and positive groups were 2.01 and 1.29, respectively (P = 0.057). In the receiver-operating characteristic curves, the area under the curves of fold-difference ovomucoid-specific IgE and ovalbumin-specific IgG4 were 0.701 and 0.719, respectively. The challenge positive predictive values of fold-difference ovomucoid-specific IgE and ovalbumin-specific IgG4 were 83.8% (cut-off point: 0.934) and 77.8% (cut-off point: 1.87), respectively. Moreover, the challenge positive predictive value in patients with both 0.934 < ovomucoid-specific IgE and ovalbumin-specific IgG4 <1.87 was 100%., Conclusions: The fold-difference levels of allergen-specific IgE and IgG4 in serum are considered useful for monitoring desensitization by low-dose OIT.

Background: Identifying patients at risk of severe allergic reactions and/or low threshold of reactivity is very important, particularly for staple foods like egg., Methods: One hundred and fifty children underwent double-blind placebo-controlled food challenge (DBPCFC) to baked egg (BE), skin prick testing and blood collection for serology and basophil activation test (BAT). Patients who passed BE DBPCFC underwent loosely cooked egg (LCE) DBPCFC. Severity of allergic reactions was classified following Practall guidelines and threshold dose was determined during DBPCFC., Results: Sixty out of 150 (40%) children reacted to BE and 16 out of 77 (21%) to LCE on DBPCFC. Considering DBPCFC to BE, 23 children (38%) had severe reactions and 33 (55%) reacted to 0.13 g or less of egg protein (low threshold group). Two children (2 out of 16 = 12%) had severe reactions to LCE. Demographic, clinical and most immunological features were not significantly different between severe/non-severe BE reactors or low/high threshold groups. Severe BE reactors had higher ovomucoid-sIgE (p = .009) and higher BAT to BE (p = .001). Patients with lower threshold to BE had higher IgE-specific activity (p = .027) and BAT to egg (p = .007) but lower severity score (p = .008). Optimal cut-offs for ovomucoid-sIgE had 100% sensitivity, 35% specificity and 60% accuracy and for BAT 76% sensitivity, 74% specificity and 75% accuracy to identify BE severe reactors. Optimal cut-offs for specific activity had 70% sensitivity, 68% specificity and 69% accuracy and for BAT 70% sensitivity, 72% specificity and 71% accuracy to identify low threshold patients., Conclusions: BAT was the best biomarker to predict severity and threshold of allergic reactions to BE and can be useful when making decisions about management of egg allergy., (© 2023 The Authors. Allergy published by European Academy of Allergy and Clinical Immunology and John Wiley & Sons Ltd.)

Background: Streptococcus mutans, the main pathogen associated with tooth decay, forms cariogenic biofilms on tooth surfaces. Therefore, controlling oral biofilm helps prevent dental caries. Hen's egg is a nutrient-dense food, and egg white is a good source of protein. Ovomucoid is one of the major proteins in egg white, with a 28 kDa molecular weight. The present study aimed to investigate the inhibitory effects of ovomucoid on the biofilm formation of S. mutans by suppressing virulence factors, including bacterial adherence, cellular aggregation and exopolysaccharide (EPS) production., Results: Crystal violet staining showed that biofilm formation by S. mutans was inhibited by ovomucoid at 0.25-1 mg mL -1 levels. Field emission scanning electron microscopy also confirmed this inhibition. In addition, ovomucoid reduced mature biofilm, water-insoluble EPS synthesis and the metabolic activity of bacterial cells in the biofilm. The bacterial adhesion and aggregation abilities of S. mutans were also decreased in the presence of ovomucoid. Ovomucoid downregulated the expression of comDE and vicR genes involved in the two-component signal transduction system and gtfA and ftf genes involved in EPS production., Conclusion: Ovomucoid has the potential for use as an anti-biofilm agent for dental caries treatment because of its inhibitory effects on the virulence factors of S. mutans. © 2023 Society of Chemical Industry., (© 2023 Society of Chemical Industry.)

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.)

Objective: Evaluate biomarkers capable of safely guiding Yellow fever vaccine (YFV) vaccination among individuals suspicious of hen's egg allergy, and identify factors associated with a higher risk for adverse events after immunization (AEAI)., Methods: Patients underwent skin prick test (SPT) for standardized allergens: whole egg, egg white, egg yolk; YFV (1:10 dilution; Biomanguinhos-Fiocruz), and intradermal test (IDT; YFV 0.02 mL, 1:100 dilution) and positive and negative controls. Serum levels of specific IgE (sIgE) for a whole egg, egg white, egg yolk, egg albumin, ovomucoid, lysozyme, and conalbumin (ImmunoCap®; ThermoFisher®) were obtained. Patients sensitized to YFV were submitted to YFV desensitization, and those negatives received YFV (0.5mL) and remained under surveillance for at least one hour., Results: 103 patients were enrolled, 95% under 12 years old. 71% (81/103) of patients had reactions: 80% immediate, 11% mixed, and 9% delayed. There was an association between positive skin test results with YFV and the severity of the reaction (OR:7.64; 95%CI:1.61-36.32; p = 0,011). Only the presence of sIgE to ovomucoid was associated with clinical symptoms (p = 0,025). Thirty patients underwent the YFV desensitization protocol., Conclusion: There is a relationship between the positivity of the egg's components and the severity of the clinical reaction. Furthermore, the relationship between the positivity of the tests with the YFV and egg's components may show a tendency to look at ovomucoid and conalbumin, but it is not a certainty. Therefore, further studies are needed to confirm these associations, and for now, the authors still recommend using the vaccine for testing when necessary., Competing Interests: Conflicts of interest The authors declare no conflicts of interest., (Copyright © 2023 Sociedade Brasileira de Pediatria. Published by Elsevier Editora Ltda. All rights reserved.)

Ovomucin is known to be critical for keeping the high quality and freshness of thick albumen, but there is lack of understanding on the dynamics changes of this important protein during storage. This study aimed to investigate the relationship between ovomucin content and egg freshness during storage. Firstly, the viscoelasticity of albumen was shown to be much higher than that of ovomucin-depleted albumen from rheological analysis results, indicating that ovomucin is an important component in maintaining the natural viscoelasticity of albumen. Then, the ovomucin content determined by ELISA method was compared to albumen pH, Haugh unit (HU), and yolk index in terms of egg white quality and to the time of storage in terms of egg freshness at 4°C, 25°C, and 37°C, respectively. Results of the transformation kinetic showed a decrease in ovomucin content with prolonged storage time (P ≤ 0.01). Correlation analysis showed a high positive correlation between ovomucin content and HU (P ≤ 0.01) and a high negative correlation between ovomucin content and the albumen pH (P ≤ 0.01) at the test temperatures. We therefore conclude that ovomucin content in albumen can be used as an index for egg freshness. At last, predictive models of the equivalent egg age (4°C and 25°C) for evaluating the egg freshness were established by means of exponential regression model with ovomucin content as the variable. These results can provide a theoretical and technical basis for the storage and fresh evaluation of shell eggs. [ABSTRACT FROM AUTHOR]

Abstract Ovomucin (OVM) plays an important role in inhibiting infection of various pathogens. However, this bioactivity mechanism is not much known. Here, the role of sialic acid in OVM anti-virus activity has been studied by ELISA with lectin or ligand. Structural changes of OVM after removing sialic acid were analyzed by circular dichroism and fluorescence spectroscopy. OVM could be binding to the hemagglutinin (HA) of avian influenza viruses H 5 N 1 and H 1 N 1 , this binding was specific and required the involvement of sialic acid. When sialic acid was removed, the binding was significantly reduced 71.5% and 64.35%, respectively. Therefore, sialic acid was proved as a recognition site which avian influenza virus bound to. Meanwhile, the endogenous fluorescence and surface hydrophobicity of OVM removing sialic acid were increased and the secondary structure tended to shift to random coil. This indicated that OVM molecules were in an unfolded state and spatial conformation disorder raising weakly. Remarkably, free sialic acid strongly promoted OVM binding to HA and thereby enhanced the interaction. It may contribute to the inhibition of host cell infection, agglutinate viruses. This study can be extended to the deepening of passive immunization field. [ABSTRACT FROM AUTHOR]

Ovomucin has a great potential because of its numerous bioactivities, which makes it an attractive molecule for industrials. However, to isolate soluble ovomucin without degradation and contamination remains a challenge. In this study, ovomucin of high purity (99.13%) was obtained in good yield (3.02 g kg −1 fresh egg white) via an improved two-step precipitation followed by gel filtration chromatography. The IC50 of the preparation for three representative new disease virus strains named LaSota, Mukteswar and V-4 is 1.99, 4.95 and 5.78 × 10 −3  g L −1 , respectively. Produced ovomucin showed limited reduction in the hemagglutination inhibition activity against all of the virus strains during the purification. Infrared spectroscopy of the ovomucin preparation indicated extensive glycosylation and sulfation. Amino acid analysis found that it was rich in alanine, glutamic acid, threonine and valine residues, which is typical in mucins. The improved process developed in this study is an alternative approach to obtain pure ovomucin with elevated antiviral activity and purity, which may significantly push forward the further research on bioactivities of ovomucin. [ABSTRACT FROM AUTHOR]

Egg white thinning during ambient storage is a well-known phenomenon. The objective of the study was to characterize the formation of peptides <10 kDa in egg white during storage at room temperature. The results indicated that the content of peptides in the egg white fraction of <10 kDa increased gradually. Similar but a faster trend was observed for the fraction of <3 kDa. Gallin, also called ovodefensin (∼7 kDa), was the main component in 10–3 kDa egg white fraction, which rapidly degraded and disappeared at 28 d of storage. Mass spectrometry analysis of <3 kDa fraction identified 6 peptide fragments from ovotransferrin and 11 peptides from ovomucin. Ovodefensin, ovotransferrin and ovomucin are the major innate components of egg defense; thus the degradation of these proteins during storage contributes to egg white thinning and increased susceptibility to bacterial contamination. This study provides the insights on the molecular mechanism of egg deterioration during prolonged ambient storage. [ABSTRACT FROM AUTHOR]

In the current study, ovomucin was isolated from Egyptian duck and characterized by several methods including SDS-PAGE, Urea-PAGE, and amino acids composition. Furthermore, Antibacterial activity was estimated against some gram positive and gram negative bacteria. Based on SDS-PAGE, the ovomucin consists of 2 subunits β-ovomucin and a-ovomucin. The molecular masses of these subunits arc 400 and 210 KDa, respectively. The migration in Urea-PAGE from anode to cathode direction indicated that ovomucin w-as much faster than their respective duck egg white protein referring to bigger positive charges and basic amino acids. The content of the hydrophobic amino acids residues (Pro, Gly, Ala, Val, Ile, Leu, Phe) js 35.02% and this represents 35.78% of the total amino acids. The content of the acidic amino acids residues (asp + glu) is 22.5% and the case lower than that of the basic amino acids (arg + lys + his; 27.99%). The minimum inhibitory concentration (MIC) of ovomucin from duck egg white was 50 ug/ml against Bacillus subtilis and 100 ug/ml against Staphylococcus aureus, Pseudomonas aeruginosa and Escherichia coli. This study elucidated that the ovomucin isolated from duck egg white has potent antibacterial activity against selected pathogenic bacteria. [ABSTRACT FROM AUTHOR]

Studies have shown the technological and functional properties of ovomucin (OVN) in the food-agricultural industry. But research has yet to explore its potential as an implantable biomaterial for tissue engineering and regenerative medicine. In this study we isolated OVN from egg white by isoelectric precipitation and fabricated scaffolds with tunable porosity by utilizing its foaming property. Gelatin a known biocompatible material was introduced to stabilize the foams, wherein different ratios of OVN and gelatin had a significant effect on the degree of porosity, pore size and stability of the formed hydrogels. The porous scaffolds were crosslinked with EDC resulting in stable scaffolds with prolonged degradation. Improved cell proliferation and adhesion of rat bone marrow-derived mesenchymal stem cells were observed for OVN containing scaffolds. Although, scaffolds with 75% OVN showed decrease in cell proliferation for L929 fibroblast type of cells. Further biocompatibility assessment as implant material was determined by subcutaneous implantation in rats of selected scaffold. H&E staining showed reasonable vascularization over time and little evidence of severe fibrosis at the implant site. Persistent polarization of classically activated macrophage was not observed, potentially reducing inflammatory response, and showed increased expression of alternatively activated macrophage cells that is favorable for tissue repair. Analysis of IgE levels in rat serum after implantation indicated minimal and resolvable allergic response to the OVN implants. The results demonstrate OVN as an acceptable implant scaffold that could provide new opportunities as an alternative natural biocompatible and functional biomaterial in various biomedical applications. © 2016 Wiley Periodicals, Inc. J Biomed Mater Res Part B: Appl Biomater, 105B: 2107-2117, 2017. [ABSTRACT FROM AUTHOR]

Ovomucin, with a similar structure to mucin and gelation ability at room temperature, is a potential mucosal carrier. To evaluate this potential, the mucoadhesive property of ovomucin was studied by the tensile strength and rheology methods, and compared with three known mucoadhesive polymers, chitosan, polyacrylic acid (PAA), and alginate. Ovomucin particles were basically spherical in shape with an average size of ~572, 235 and 54 nm prepared at pH 5, 6.5, and 9, respectively. The absolute value of the zeta potential increased from ~ −51 mV at pH 5 to ~ −59 and −91 mV at pH 6.5 and 9, respectively. Drug loading efficiency of ovomucin particles for brilliant blue (negatively charged), riboflavin (non-ionic), and ciprofloxacin (positively charged) were ~87.7, 25.4, and 89.1%, respectively. The release of encapsulated ciprofloxacin was evaluated in phosphate-buffered saline (PBS), simulated intestinal fluid (SIF), and simulated gastric fluid (SGF). The mechanism of the releases was studied using different mathematical models: zero-order, first-order, Higuchi, Hixson-Crowell, and Korsmeyer-Peppas models. Approximately 61 and 67% of loaded ciprofloxacin were released from the particles over 7 h of incubation in PBS and SIF, respectively. The kinetics of drug releases in PBS and SIF followed the Fickian diffusion mechanism (Korsmeyer-Peppas model). Therefore, ovomucin could function as a mucoadhesive carrier to efficiently encapsulate drugs and sustainably release them in the non-digestive and intestinal mucosal tissues. [ABSTRACT FROM AUTHOR]

Ovomucin (OVM) is an ideal natural macromolecular glycoprotein extracted from eggs with good adhesion. Based on the defect that glycyrrhizin (GL) has good antiviral activity but fast metabolism, this study aimed to explore the binding effect and mechanism of GL to OVM, using multi-spectroscopic techniques, isothermal titration calorimetry (ITC), and molecular docking. The adhesion ability of OVM to the hydrophilic interface and GL was first demonstrated by dual polarization interferometry (DPI) analysis and binding capacity assay, and the OVM-GL complex exhibited a similar affinity for the spike protein of COVID-19. The spectroscopic results show that GL can quench the inherent fluorescence and change the glycosidic bond and secondary structure of OVM. The ITC measurements suggested that the binding was exothermic, the hydrogen bond was the dominant binding force for forming OVM-GL. Finally, molecular docking results indicated that GL has hydrogen bond interaction with several amino acid residues located in α-OVM and β-OVM while embedding into the hydrophobic pocket of OVM via hydrophobic interactions. In conclusion, OVM can adhere to the hydrophilic interface and bind to GL through hydrogen bonding and hydrophobic interactions to form a stable complex, that is expected to be helpful in virus prophylaxis. [Display omitted] • GL can form a stable complex with OVM on the hydrophilic surface. • Hydrophobic interactions and hydrogen are the dominant binding force for forming OVM-GL. • GL binding induces the glycosidic bond and secondary structure changes of OVM. • OVM-GL complex exhibited a similar affinity to OVM for the spike protein in COVID-19. [ABSTRACT FROM AUTHOR]

As a weakly gelling protein, hot spring egg white underwent thinning during storage. This study explored the mechanism of thinning in hot spring egg white from the perspective of "gel structure and protein composition" using quantitative proteomics, SEM, SDS-PAGE, and other techniques. Quantitative proteomics analysis showed that there were 81 (44 up-regulated and 21 down-regulated) key proteins related to thinning of hot spring egg white. The changes in the relative abundance of proteins such as ovalbumin-related Y, mucin-6, lysozyme, ovomucoid, and ovotransferrin might be important reasons for thinning in hot spring egg white. SEM results indicated that the gel network gradually became regular and uniform, with large pores appearing on the cross-section and being pierced. Along with the decrease in intermolecular electrostatic repulsion, protein molecules gradually aggregated. The particle size gradually increased from 139.1 nm to 422.5 nm. Meanwhile, the surface hydrophobicity, and disulfide bond content gradually increased. These changes might be the reasons for thinning in hot spring egg white during storage. It can provide a new perspective for studying the thinning mechanism of weakly gelling egg whites., 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.)

A process-simplified hard template approach was established to synthesize the monodisperse macroporous silica microspheres with homogeneous structures by twice alkali-thermal treatment and calcination routes. Porous vinyl-functionalized polysesquioxane microspheres (V-PMSQ) were synthesized through a hydrolyzation-polycondensation method and used as templates. The template particles with large aperture and high pore volume were obtained by adjusting the pH value and reaction time of the twice alkali-thermal reaction. After calcination, monodisperse silica microspheres with an average pore size of 30 nm, homogeneous pore structures, and narrow particle size distribution were fabricated, which can be directly used as chromatographic matrices without classification. After that, a new reversed-phase/strong anion-exchange (RP/SAX) mixed-mode stationary phase Sil-S-VOIM was prepared by bonding the 1-vinyl-3-octyl-imidazole ligands to the above silica microspheres through a "thiol-ene" click reaction. The performance of the Sil-S-VOIM column was evaluated by one acidic protein (transferrin) and two basic proteins (lysozyme, α-chymotrypsin) and compared to a single imidazole-modified Sil-S-VIM column and an octyl-modified Sil-C 8 column, respectively. Due to the synergistic effect of electrostatic repulsion and hydrophobic interactions, baseline separations of the above proteins were observed only on the Sil-S-VOIM column, with resolutions of 2.55 and 2.01 between lysozyme and transferrin, and between transferrin and α-chymotrypsin, respectively, indicating good selectivity and separation ability compared with single-mode stationary phases. It was applied to the isolation of egg white samples with peaks identified by SDS-PAGE and MALDI-TOF-MS. The results showed that the selective retention and isolation of ovomucoid and ovotransferrin were successfully achieved, with yields of 78.8% and 67.2%, respectively. The protocol described in this work is simpler, faster, and has higher protein recovery. Overall, this new mixed-mode stationary phase provided a promising potential for the separation and determination of intact proteins., (© 2023. The Author(s), under exclusive licence to Springer-Verlag GmbH Austria, part of Springer Nature.)

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.)