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Food Research International (Ottawa,... Jul 2023Currently, the biological consequences of advanced glycation end-products (AGEs) and their link to the antigenicity of food allergens are largely unknown due to the...
Effect of glycation derived from α-dicarbonyl compounds on the in vitro digestibility of ovalbumin: Tracing of advanced glycation end-products and immuno-active peptides.
Currently, the biological consequences of advanced glycation end-products (AGEs) and their link to the antigenicity of food allergens are largely unknown due to the uncertainty in their digestive fates within the body. In this study, the influence of glycation derived from α-dicarbonyl compounds (α-DCs), precursors of AGEs, on digestive behaviors of ovalbumin (OVA) was investigated in a two-step simulated gastrointestinal (GI) model. Methylglyoxal (MGO), glyoxal (GO), and 3-deoxyglucosone were selected as typical α-DCs to obtain glycated OVA with different AGE-modifications (AGE-Ms). It was unveiled that α-DC-glycation reduced the digestibility of OVA via blocking tryptic cleavage sites and inducing steric hindrance, especially seen in the GO- and MGO-OVA groups. The formed AGE-Ms, depending on the precursor type, showed masking effects on the epitopes of OVA, which counteracted the negative effects of reduced digestibility on its antigenicity. Substantial changes in the peptide release patterns were also noted in glycated OVA, including alterations in the sequences and structures of several known protease-resistant epitopes of OVA. This study provides new insights into the nutritional and healthy effects of MRPs in heat-processed foods, as well as their potential connection to the modulation of egg allergy.
Topics: Maillard Reaction; Ovalbumin; Glycation End Products, Advanced; Magnesium Oxide; Peptides; Glyoxal; Pyruvaldehyde
PubMed: 37254415
DOI: 10.1016/j.foodres.2023.112842 -
AAPS PharmSciTech Oct 2017The purpose of this study was to evaluate the use of different types of microneedles and doses of ovalbumin antigen for in vitro skin permeation and in vivo...
The purpose of this study was to evaluate the use of different types of microneedles and doses of ovalbumin antigen for in vitro skin permeation and in vivo immunization. In vitro skin permeation experiments and confocal laser scanning microscopy revealed that hollow microneedles had a superior enhancing effect on skin permeation compared with a solid microneedle patch and untreated skin by efficiently delivering ovalbumin-fluorescein conjugate into the deep skin layers. The flux and cumulative amount of ovalbumin-fluorescein conjugate at 8 h after administering with various conditions could be ranked as follows: hollow MN; high dose > medium dose > low dose > MN patch; high dose > medium dose > low dose > untreated skin; high dose > medium dose > low dose > without ovalbumin-fluorescein conjugate. As the dose of ovalbumin-fluorescein conjugate was increased to 500 μg, the antigen accumulated in the skin to a greater extent, as evidenced by the increasing green fluorescence intensity. When the hollow microneedle was used for the delivery of ovalbumin into the skin of mice, it was capable of inducing a stronger immunoglobulin G immune response than conventional subcutaneous injection at the same antigen dose. Immunoglobulin G levels in the hollow MN group were 5.7, 11.6, and 13.3 times higher than those of the subcutaneous injection group for low, medium, and high doses, respectively. Furthermore, the mice immunized using the hollow microneedle showed no signs of skin infection or pinpoint bleeding. The results suggest that the hollow MN is an efficient device for delivering the optimal dose of antigen via the skin for successful immunization.
Topics: Administration, Cutaneous; Animals; Antigens; Immunization; Immunoglobulin G; Mice; Needles; Ovalbumin; Skin
PubMed: 28160208
DOI: 10.1208/s12249-017-0730-4 -
International Journal of Biological... Jul 2019Ovalbumin peptides are food protein-derived fragments comprised of amino acid residues. The bioactive properties of the peptides are determined by the inherent amino...
Ovalbumin peptides are food protein-derived fragments comprised of amino acid residues. The bioactive properties of the peptides are determined by the inherent amino acid composition and sequence of the peptide. The objective of this study was to evaluate the proteomics characteristics in Tibetan chicken egg ovalbumin peptides, compared to ordinary eggs, using isobaric tags for the relative and absolute quantification labelling technique (iTRAQ). The results showed that 165 proteins were identified and 56 proteins were significantly changed including 34 significantly upregulated and 22 significantly downregulated proteins. The more abundant proteins of the Tibetan ovalbumin peptides included vitellogenin-2, vitellogenin-1, vitellogenin, apolipoprotein A-I, and serum albumin, which were upregulated. A Gene Ontology (GO) analysis showed that these proteins mostly participated in biological processes and the Kyoto Encyclopedia of Genes and Genomes (KEGG) pathway analysis showed that they may be associated with the peroxisome proliferator-activated receptor (PPAR) pathway, which is related to lipid metabolism. The Protein-Protein Interaction (PPI) analysis showed that these proteins significantly interacted.
Topics: Animals; Chick Embryo; Gene Ontology; Ovalbumin; Peptide Fragments; Protein Binding; Proteomics; Species Specificity; Staining and Labeling
PubMed: 30876899
DOI: 10.1016/j.ijbiomac.2019.03.075 -
Cellular and Molecular Biology... Jul 2015The chicken ovalbumin extracts could promote cell survival and proliferation. In the present study, the different components in chicken ovalbumin extracts were further...
The chicken ovalbumin extracts could promote cell survival and proliferation. In the present study, the different components in chicken ovalbumin extracts were further separated to find the component primarily responsible for promoting cell proliferation. Components of differing molecular weight were separated from chicken ovalbumin extracts by ultrafiltration. Different components were co—cultured with different cells at different final concentrations, and the effects on cell proliferation were subsequently determined by a CellTiter 96 Aqueous One Solution Cell Proliferation Assay kit (Promega). Components from chicken ovalbumin extracts less than 3 kD in size can promote 293T cell and 293T—GFP cell proliferation. The components from chicken ovalbumin extract more than 3 kD in size can promote bone marrow or umbilical cord mesenchymal stem cell (MSC) proliferation. The separation of components from chicken ovalbumin less than and more than 3 kD in size that are able to function as active components for the promotion of different cellular proliferation. This discovery may identify a new and convenient additive for cell culture media, promoting cell growth and proliferation.
Topics: Animals; Bone Marrow Cells; Cell Proliferation; Cell Survival; Cells, Cultured; Chickens; Coculture Techniques; Electrophoresis, Polyacrylamide Gel; HEK293 Cells; Humans; Mesenchymal Stem Cells; Mice; Mice, Inbred C57BL; Ovalbumin; Ovum; Umbilical Cord
PubMed: 26255140
DOI: No ID Found -
International Journal of Biological... Jun 2022This study explored the mechanism underlying the interactions between polysaccharides and ovalbumin-ferulic acid (OVA-FA) and the effect of polysaccharides on...
This study explored the mechanism underlying the interactions between polysaccharides and ovalbumin-ferulic acid (OVA-FA) and the effect of polysaccharides on OVA-FA-stabilized emulsions. Fourier transform infrared spectroscopy (FTIR) and X-ray diffraction (XRD) were used to study the polysaccharide OVA-FA interactions mechanism and to resolve the changes in the protein secondary structure and crystal structure. OVA-FA-polysaccharide-stabilized emulsions were studied using confocal laser scanning microscopy (CLSM), and their rheological properties and stability were determined. The results showed that the non-covalent interactions between polysaccharides and OVA-FA led to an increase in the β-sheet content of OVA and a decrease in the α-helix and random coil contents. The stability of the OVA-FA-polysaccharide-stabilized emulsions was better compared with that of the OVA-FA-stabilized emulsions. By comparing the different OVA-FA-polysaccharide-stabilized emulsions, we observed that OVA-FA-agar did not stabilize the emulsion well, while the OVA-FA-SA- and OVA-FA-KC-stabilized emulsions had good elasticity, and the microstructure and storage stability of the OVA-FA-KC-stabilized emulsion were better. Our findings provide a new perspective for the application of OVA-FA-KC in complex food emulsions.
Topics: Coumaric Acids; Emulsions; Ovalbumin; Polysaccharides
PubMed: 35568148
DOI: 10.1016/j.ijbiomac.2022.05.078 -
Food Chemistry Jul 2019Dried egg white powders are used in many segments of the food industry in place of traditional liquid egg materials. Dry heating during the processing of these products...
Dried egg white powders are used in many segments of the food industry in place of traditional liquid egg materials. Dry heating during the processing of these products plays an essential role in obtaining their excellent functionalities, which are associated with protein aggregation. The objective of this study was to understand the aggregation behaviour of ovalbumin (OVA), the major component of egg-white proteins, during dry heating at 75 °C for 21 days. The results indicated that OVA aggregation increased from 28.7 ± 1.23% to 57.5 ± 2.45% as the reaction time increased, resulting in the generation of insoluble aggregates that were often 1-100 nm in diameter. However, a few soluble OVA aggregates became insoluble precipitates as their morphology changed from long strands to denser networks after 15 days of heat treatment. Moreover, covalent bonds, hydrophobic interactions and electrostatic repulsion played important roles in the formation of the small aggregates.
Topics: Heating; Hydrophobic and Hydrophilic Interactions; Ovalbumin; Particle Size; Static Electricity
PubMed: 30797348
DOI: 10.1016/j.foodchem.2019.01.170 -
International Journal of Biological... Apr 2023In this study, ovalbumins (OVAs) were glycosylated with fructo-oligosaccharide (FO) at different temperatures (80 °C, 100 °C, 120 °C, and 140 °C) and durations...
In this study, ovalbumins (OVAs) were glycosylated with fructo-oligosaccharide (FO) at different temperatures (80 °C, 100 °C, 120 °C, and 140 °C) and durations (1 h and 2 h) via wet-heating. The glycosylated OVAs (GOVAs) were characterized by the degree of glycosylation (DG), particle size, zeta potentials, and structural changes. GOVAs-stabilized high-internal-phase emulsions (HIPEs) were then prepared to compare their macro- and microstructure and freeze-thaw stability. The results showed that the DG of GOVAs increased with the increase in glycosylation temperature and the protein structure unfolded with it. Glycosylation decreased the particle size, zeta potential, and α-helical structures and increased the β-sheets and surface hydrophobicity (H) of GOVAs compared with unmodified OVAs. Moreover, GOVAs-stabilized HIPEs exhibited smaller particle sizes, zeta potentials, agglomeration indexes, oil loss rates, and freezing points and higher viscoelasticity, centrifugal stabilities, flocculation indexes, and freeze-thaw stabilities. Notably, HIPEs prepared by GOVAs (glycosylated higher than 120 °C) showed the least changes in macro- and microscopic appearances after freeze-thawing. These findings will provide a novel method for improving and broadening the functionalities of OVAs and potentially develop HIPEs with enhanced freeze-thaw stabilities.
Topics: Freezing; Ovalbumin; Temperature; Molecular Structure; Emulsions; Glycosylation; Particle Size
PubMed: 36746301
DOI: 10.1016/j.ijbiomac.2023.123560 -
Inorganic Chemistry Apr 2024This study aims to design an artificial metalloprotease based on a Zr-containing polyoxometalate Na[Zr(WO)] [Zr(W)] for the hydrolysis of ovalbumin (OVA) in the presence...
This study aims to design an artificial metalloprotease based on a Zr-containing polyoxometalate Na[Zr(WO)] [Zr(W)] for the hydrolysis of ovalbumin (OVA) in the presence of different surfactants, which can be used in many areas of the biological and medical sciences, particularly for targeted proteolytic drug design. For this reason, parameters, including the free energy of binding, the chemical nature of amino acid residues, secondary structures, and electrostatic potentials, of Zr(W)-OVA and Zr(W)-OVA-surfactant were analyzed by molecular docking simulations. The investigations showed that the presence of surfactants decreases the binding affinity of Zr(W) for OVA amino acids, and hydrogen bonds and van der Waals interactions are formed between Zr(W) and OVA amino acids. Additionally, GROMACS further illustrated the significance of SDS and CTAB surfactants in influencing the conformational changes of the OVA that lead to selective protein hydrolysis. In agreement with molecular dynamics simulation results, the experimental analysis showed more protein hydrolysis for the Zr(W)-OVA-surfactant systems. For instance, circular dichroism spectroscopy indicated that Zr(W)-OVA-CTAB and Zr(W)-OVA-TX-100 were more hydrolytically efficient due to the increased level of β-structures rather than α-chains, which showed that surfactants can facilitate the accessibility of Zr(W) to the cleavage sites by inducing partial unfolding of the OVA structure.
Topics: Surface-Active Agents; Ovalbumin; Hydrolysis; Cetrimonium; Molecular Docking Simulation; Amino Acids
PubMed: 38530420
DOI: 10.1021/acs.inorgchem.3c03411 -
Journal of Molecular Biology Oct 1991Ovalbumin, the major protein in avian egg-white, is a non-inhibitory member of the serine protease inhibitor (serpin) superfamily. The crystal structure of uncleaved,...
Ovalbumin, the major protein in avian egg-white, is a non-inhibitory member of the serine protease inhibitor (serpin) superfamily. The crystal structure of uncleaved, hen ovalbumin was solved by the molecular replacement method using the structure of plakalbumin, a proteolytically cleaved form of ovalbumin, as a starting model. The final refined model, including four ovalbumin molecules, 678 water molecules and a single metal ion, has a crystallographic R-factor of 17.4% for all reflections between 6.0 and 1.95 A resolution. The root-mean-square deviation from ideal values in bond lengths is 0.02 A and in bond angles is 2.9 degrees. This is the first crystal structure of a member of the serpin family in an uncleaved form. Surprisingly, the peptide that is homologous to the reactive centre of inhibitory serpins adopts an alpha-helical conformation. The implications for the mechanism of inhibition of the inhibitory members of the family is discussed.
Topics: Animals; Chickens; Chromatography, Ion Exchange; Data Interpretation, Statistical; Hydrogen Bonding; Metals; Models, Molecular; Ovalbumin; Peptide Fragments; Protein Processing, Post-Translational; Solvents; Temperature; X-Ray Diffraction; alpha 1-Antitrypsin
PubMed: 1942038
DOI: 10.1016/0022-2836(91)80185-w -
Rapid immunoassay exploiting nanoparticles and micromagnets: proof-of-concept using ovalbumin model.Bioanalysis Mar 2017We present a fast magnetic immunoassay, combining magnetic nanoparticles and micromagnets. High magnetic field gradients from micromagnets are used to develop a new...
AIM
We present a fast magnetic immunoassay, combining magnetic nanoparticles and micromagnets. High magnetic field gradients from micromagnets are used to develop a new approach to the standard ELISA. Materials & methods/results: A proof-of-concept based on colorimetric quantification of antiovalbumin antibody in buffer is performed and compared with an ELISA. After optimization, the magnetic immunoassay exhibits a limit of detection (40 ng/ml) and a dynamic range (40-2500 ng/ml) similar to that of ELISAs developed using same biochemical tools.
CONCLUSION
Micromagnets can be fully integrated in multiwell plates at low cost to allow the efficient capture of immunocomplexes carried by magnetic nanoparticles. The method is generic and permits to perform magnetic ELISA in 30 min.
Topics: Antibodies, Monoclonal; Biosensing Techniques; Colorimetry; Enzyme-Linked Immunosorbent Assay; Immunoassay; Limit of Detection; Magnetic Fields; Magnets; Nanoparticles; Ovalbumin
PubMed: 28225302
DOI: 10.4155/bio-2016-0232