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Food Chemistry Dec 2016Ovomucin, accounting for ∼3.5% of egg white proteins, contains 2.6-7.4% of sialic acid; sialic acid is suggested to play important roles in host-recognition, cognition...
Ovomucin, accounting for ∼3.5% of egg white proteins, contains 2.6-7.4% of sialic acid; sialic acid is suggested to play important roles in host-recognition, cognition and memory development. However, ovomucin's limited water solubility might restrict its future applications. The objective of the study was to examine the effect of proteolysis of ovomucin on the sialic acid content and bifidogenic activity of ovomucin hydrolysates. Ovomucin extract was hydrolyzed by 14 proteases with yields and DHs ranging from 42.6% (flavourzyme) to 97.4% (protease N), and 2.4% (flavourzyme) to 46.3% (pronase), respectively. Ovomucin hydrolyzed by pronase and protex 26L showed molecular weight (Mw) distributions less than 40kDa while others larger than 200kDa. Allergenicity of ovomucin hydrolysates was significantly reduced (P<0.05) in comparison to ovomucin extract. The content of sialic acid in hydrolysates ranged from 0.1% (protex 26L) to 3.7% (pronase). Ovomucin hydrolysates did not generally support growth of Bifidobacterium spp. in vitro.
Topics: Endopeptidases; Hydrolysis; N-Acetylneuraminic Acid; Ovomucin; Peptide Hydrolases; Proteolysis
PubMed: 27374509
DOI: 10.1016/j.foodchem.2016.05.153 -
Poultry Science Apr 2014Ovalbumin, ovotransferrin, ovomucin, and lysozyme are a few of the egg white proteins that can be used as functional components. The objective of this study was to...
Ovalbumin, ovotransferrin, ovomucin, and lysozyme are a few of the egg white proteins that can be used as functional components. The objective of this study was to develop a simple, sequential separation method for multiple proteins from egg white. Separated proteins are targeted for human use, and thus any toxic compounds were excluded. The methods for individual components and the sequential separation were practiced in laboratory scale first, and then tested for scale-up. Lysozyme was separated first using FPC3500 cation exchange resin and then ovomucin using isoelectric precipitation. Ovalbumin and ovotransferrin were separated from the lysozyme- and ovomucin-free egg white by precipitating ovotransferrin first using 5.0% (wt/vol) (NH4)2SO4 and 2.5% (wt/vol) citric acid combination. After centrifugation, the supernatant (S1) was used for ovalbumin separation and the precipitant was dissolved in water, and reprecipitated using 2.0% ammonium sulfate (wt/vol) and 1.5% citric acid (wt/vol) combination. The precipitant was used as ovotransferrin fraction, and the supernatant (S2) was pooled with the first supernatant (S1), desalted using ultrafiltration, and then heat-treated to remove impurities. The yield of ovomucin and ovalbumen was >98% and that of ovotransferrin and lysozyme was >82% for both laboratory and scale-up preparations. The SDS-PAGE and western blotting of the separated proteins, except for ovomucin, showed >90% purity. The ELISA results indicated that the activities of separated ovalbumin, ovotransferrin, and lysozyme were >96%. The protocol separated 4 major proteins in sequence, and the method was simple and easily scaled up.
Topics: Animals; Blotting, Western; Chemical Precipitation; Chickens; Conalbumin; Egg Proteins; Egg White; Electrophoresis, Polyacrylamide Gel; Enzyme-Linked Immunosorbent Assay; Food Handling; Muramidase; Ovalbumin; Ovomucin
PubMed: 24706978
DOI: 10.3382/ps.2013-03403 -
Journal of Agricultural and Food... May 2002Ovomucin was fractionated from whole egg albumen, thick egg albumen, liquid egg albumen, and a liquid egg albumen filtration byproduct by using the isoelectric... (Comparative Study)
Comparative Study
Ovomucin was fractionated from whole egg albumen, thick egg albumen, liquid egg albumen, and a liquid egg albumen filtration byproduct by using the isoelectric precipitation method. The amounts of ovomucin measured in the above-mentioned fractions were 280, 340, 500, and 520 mg per 100 g of albumen, respectively. There was great variation between the beta-ovomucin contents of the different albumen fractions. Whole egg albumen contained about 25 mg of beta-ovomucin in 100 g of albumen, whereas thick egg albumen, liquid egg albumen, and the filtration byproduct contained about 1.5, 3, and 5 times more beta-ovomucin, respectively, as compared to whole egg albumen. The results indicate that both the liquid egg albumen fraction and especially the filtration byproduct fraction appear to be potential sources of ovomucin when it is used as an ingredient for functional foods.
Topics: Carbohydrates; Chemical Precipitation; Chromatography, Gel; Ovalbumin; Ovomucin
PubMed: 11982409
DOI: 10.1021/jf011333y -
British Journal of Experimental... Oct 1951
Topics: Humans; Influenza, Human; Microbial Viability; Orthomyxoviridae; Ovomucin; Virion
PubMed: 14886502
DOI: No ID Found -
International Journal of Biological... Aug 2023Ovomucin (OVM) is an ideal natural macromolecular glycoprotein extracted from eggs with good adhesion. Based on the defect that glycyrrhizin (GL) has good antiviral...
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.
Topics: Ovomucin; Glycyrrhizic Acid; Molecular Docking Simulation; Spectrum Analysis; Eggs; Binding Sites; Protein Binding
PubMed: 37356685
DOI: 10.1016/j.ijbiomac.2023.125535 -
Development (Cambridge, England) Mar 1996A mucin was discovered on the surface of migratory primordial germ cells (PGCs) from chick and rat embryos by means of two monoclonal antibodies. The protein was found...
A mucin was discovered on the surface of migratory primordial germ cells (PGCs) from chick and rat embryos by means of two monoclonal antibodies. The protein was found to be identical or closely related to ovomucin, a 600 X 10(3) relative molecular mass glycoprotein, and a major constituent of the vitelline membrane of the avian yolk. Based on its resemblance to ovomucin it is referred to as ovomucin-like protein (OLP). The OLP was expressed on PGCs from E3 to E7 female, and from E3 to E12 male chick embryos as the PGCs migrate and colonize the gonadal ridges. After the PGCs have settled in the gonads, they no longer express OLP. In tissue cultures of dissociated cells from E6 gonads, OLP was present only on cells that were positive for PAS staining, the standard histological method to identify PGCs in the chick embryo. Since unfixed PGCs were recognized by the antibodies, at least part of the OLP is localized on the cell surface. The anti-OLP antibodies also stained PGCs in the gonads of the rat embryo, showing that the expression of this antigen on PGCs is phylogenetically conserved. Ovomucin isolated from vitelline membrane prevented adhesion of fibroblasts but not PGCs when used a as a substratum in vitro. The anti-adhesive quality of the mucin resides in the sialic acid residues of the carbohydrate side chains. We propose that OLP has a similar anti-adhesive quality as the ovomucin from vitelline membrane, and that this anti-adhesive property is important to prevent precocious adhesion of migrating PGCs to blood vessel walls and to connective tissue in the mesentery as they migrate toward the gonadal ridges.
Topics: Animals; Antigens, Surface; Cell Adhesion; Cell Movement; Chick Embryo; Fibroblasts; Germ Cells; Immunologic Techniques; Ovomucin; Rats
PubMed: 8631269
DOI: 10.1242/dev.122.3.915 -
Lipids Mar 2002This experiment was designed to evaluate the effect of casein or ovomucin (OV) on the micellar solubility of cholesterol and the taurocholate binding capacity in vitro....
This experiment was designed to evaluate the effect of casein or ovomucin (OV) on the micellar solubility of cholesterol and the taurocholate binding capacity in vitro. We also evaluated the effects of casein or OV on cholesterol metabolism in rats and Caco-2 cells. OV had a significantly greater bile acid-binding capacity than that of casein in vitro. Micellar cholesterol solubility in vitro was significantly lower in the presence of OV compared to casein. The cholesterol micelles containing OV significantly suppressed cholesterol uptake by Caco-2 cells compared to the cholesterol micelles containing casein. Consistent with these in vitro findings, OV-feeding significantly increased the fecal excretion of bile acids or cholesterol compared with casein-feeding. Serum total cholesterol was significantly lower in rats fed OV than in those fed casein. The concentrations of total lipids in liver were significantly lower in the OV-fed group compared with the casein group. These results suggest that the suppression of cholesterol absorption by direct interaction between cholesterol mixed micelles and OV in the jejunal epithelia is part of the mechanism underlying the hypocholesterolemic action of OV. OV may also inhibit the reabsorption of bile acids in the ileum, thus lowering the serum cholesterol level.
Topics: Animals; Caco-2 Cells; Cholesterol; Eggs; Humans; Hypercholesterolemia; Intestinal Absorption; Micelles; Ovomucin; Rats
PubMed: 11942477
DOI: 10.1007/s11745-002-0890-6 -
Comparative Biochemistry and... 19911. Egg white proteins are the principal solutes present in egg white, making up approximately 10% of its weight. 2. They are globular proteins and most have acidic... (Review)
Review
1. Egg white proteins are the principal solutes present in egg white, making up approximately 10% of its weight. 2. They are globular proteins and most have acidic isoelectric points. 3. Many are glycoproteins with carbohydrate contents ranging from 2 to 58%. 4. Of the major egg white proteins, lysozyme is the only one having catalytic activity, but many have specific binding sites, e.g. for vitamins such as biotin, riboflavin and thiamin, or for metal ions such as FeIII. 5. A major group are those showing proteinase inhibitory activity, and they include ovomucoid, ovoinhibitor, cystatin and ovostatin. 6. The synthesis of egg white protein occurs in the oviduct, and is hormonally controlled either by oestrogens or progesterone. 7. Extensive studies have been carried out in the genes coding for egg white proteins.
Topics: Animals; Carrier Proteins; Chick Embryo; Conalbumin; Egg Proteins; Muramidase; Ovalbumin; Ovomucin; Protease Inhibitors; Vitamins
PubMed: 1756612
DOI: 10.1016/0305-0491(91)90076-p -
Journal of Biomedical Materials... Oct 2017Studies 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...
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.
Topics: Animals; Bone Marrow Cells; Cell Adhesion; Cell Line; Cell Proliferation; Chickens; Egg White; Implants, Experimental; Materials Testing; Mesenchymal Stem Cells; Mice; Ovomucin; Rats; Tissue Engineering; Tissue Scaffolds
PubMed: 27405539
DOI: 10.1002/jbm.b.33750 -
Food Research International (Ottawa,... Jun 2018Protein susceptibility to in vitro gastrointestinal digestion of ovomucin-depleted egg white (OdEW) adjusted to pH 4, 5, 7 and 9 and processed by heat (60 and 80 °C... (Comparative Study)
Comparative Study
Protein susceptibility to in vitro gastrointestinal digestion of ovomucin-depleted egg white (OdEW) adjusted to pH 4, 5, 7 and 9 and processed by heat (60 and 80 °C for 10 min) or pulsed electric fields (PEF) (1.4-1.8 kV/cm, 259-695 kJ/kg) was studied by assessing peptide production, proteolytic pattern, and the final peptide profile. Ovotransferrin was more susceptible to pepsin hydrolysis than lysozyme, with ovalbumin showing the highest proteolytic resistance. Ovalbumin was, however, hydrolyzed by pancreatin to produce a stable fragment. Heat treatment of OdEW solutions at 60 °C had little impact on protein susceptibility with the ovalbumin dimers formed having a comparable resistance to pepsinolysis as ovalbumin. Heating at 80 °C significantly enhanced protein susceptibility, as ovalbumin and protein aggregates formed were completely hydrolyzed within 30 min of pepsinolysis. Adjusting OdEW solution to pH 4 and treating with PEF at 695 kJ/kg enhanced protein susceptibility, similar to heat treatment at 80 °C, mainly owing to the enhanced enzymatic hydrolysis of ovalbumin. PEF processing can, therefore, increase protein digestion while minimizing protein aggregation, which will enhance protein functionality in egg whites.
Topics: Chromatography, Liquid; Conalbumin; Digestion; Egg Proteins, Dietary; Electricity; Electrophoresis, Polyacrylamide Gel; Food Handling; Hot Temperature; Hydrogen-Ion Concentration; Hydrolysis; Muramidase; Ovalbumin; Ovomucin; Peptide Hydrolases; Peptides; Protein Aggregates; Proteolysis; Spectrometry, Mass, Electrospray Ionization; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
PubMed: 29735080
DOI: 10.1016/j.foodres.2018.03.075