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Analytical Biochemistry Jan 2022Ovalbumin particles are reduced to nano size using heat treatment techniques. Their structural patterns in their native state and in their pH denatured state were...
Ovalbumin particles are reduced to nano size using heat treatment techniques. Their structural patterns in their native state and in their pH denatured state were attempted. Denaturation is also a part of conformation and hence conformations due to pH and glucose were analyzed using FTIR spectroscopy. The interactions behind these conformations are unraveled and the role of glucose as cosolvent in restricting the denaturation is also revealed from the observed secondary structures of ovalbumin. Further, the characterization of these synthesized nano particles reveals the extent of their applications. The obtained results indicate that consideration of ovalbumin nanoparticles seems to favor a very clear trend of protein denaturation and the observed structural modifications are the result of development of non-covalent interactions by the cosolvent molecules.
Topics: Nanoparticles; Ovalbumin; Protein Structure, Secondary; Spectroscopy, Fourier Transform Infrared
PubMed: 34774535
DOI: 10.1016/j.ab.2021.114456 -
Recent Progress in Hormone Research 1979
Review
Topics: Animals; Base Sequence; Chickens; DNA, Recombinant; Female; Genes; Hormones; Ovalbumin; Oviducts; RNA, Messenger; Receptors, Cell Surface; Transcription, Genetic
PubMed: 229523
DOI: 10.1016/b978-0-12-571135-7.50005-9 -
Food Chemistry May 2024When subjected to dry-heating, egg white ovalbumin, a phosphoglycoprotein, undergoes fragmentation and forms soluble aggregates. We investigated the mechanisms of...
When subjected to dry-heating, egg white ovalbumin, a phosphoglycoprotein, undergoes fragmentation and forms soluble aggregates. We investigated the mechanisms of dry-heat-induced fragmentation of ovalbumin. SDS-PAGE analysis showed that ovalbumin fragmented into five polypeptides, and their amount increased over 6 h of dry-heat treatment at 120 °C. The fragments contained fewer or no phosphoserine, compared with that in crude ovalbumin. Liquid chromatography-tandem mass spectrometry analysis of tryptic digests revealed that the fragmentation sites were located on phosphoserine residues, S and S. During fragmentation, the phosphoserine residues underwent conversion into dehydroalanine residues, which were subsequently hydrolyzed. The nitrogen from the dehydroalanine became a newly formed terminal amide group on the N-terminal fragment, while the remaining molecule predominantly formed a new terminal pyruvoyl group. Furthermore, the fragments were incorporated into monomers or soluble aggregates of ovalbumin via covalent and non-covalent bonds. This study demonstrated a novel mechanism for dry-heat-induced fragmentation of phosphoproteins.
Topics: Ovalbumin; Phosphoserine; Hot Temperature; Peptides; Egg White
PubMed: 38159316
DOI: 10.1016/j.foodchem.2023.138263 -
Journal of Materials Chemistry. B Aug 2020We designed a pH intelligently driven self-assembled nano-platform (GOx@ZIF-OVA). The nano-platform was composed of glucose oxidase (GOx), ovalbumin (OVA) and zeolitic...
We designed a pH intelligently driven self-assembled nano-platform (GOx@ZIF-OVA). The nano-platform was composed of glucose oxidase (GOx), ovalbumin (OVA) and zeolitic imidazolate skeleton-8 (ZIF-8). The goal was to address the depth and cumulative limits of the drug at the tumor site. Firstly, OVA-modified GOx@ZIF could greatly increase tumor accumulation due to spontaneous self-assembly from 142.2 ± 9.1 to 705.5 ± 52.1 nm and the 5779.4 ± 598.3 nm giant at pH values of 7.4, 6.5, and 5.0, respectively. More importantly, the tumor-like sphere experiments demonstrated that the encapsulated GOx "vampires" can cut off the energy source of tumors and poisonous tumor cells without depth limitations. Furthermore, immunofluorescence assay and cytotoxicity assay tests in vivo proved that T cell infiltration could be significantly increased, triggering an effective anti-tumor immune response and inhibiting lung metastasis. Therefore, the experimental results demonstrated that the acid-smart-driven nano-platform has the potential to address the limitations of tumor depth and drug accumulation in solid tumors.
Topics: Cell Line, Tumor; Glucose Oxidase; Humans; Hydrogen-Ion Concentration; Metal-Organic Frameworks; Nanoparticles; Ovalbumin; Tumor Microenvironment; Zeolites
PubMed: 32678404
DOI: 10.1039/d0tb00542h -
Bioelectrochemistry (Amsterdam,... Aug 2021A novel, sensitive and selective electrochemical sensor based on epitope-imprinted polydopamine (PDA) was developed for ovalbumin (OVA) detection. Molecularly imprinted...
A novel, sensitive and selective electrochemical sensor based on epitope-imprinted polydopamine (PDA) was developed for ovalbumin (OVA) detection. Molecularly imprinted polydopamine was synthesized on an AuNP-coated screen-printed carbon electrode (SPCE) via electropolymerization in the presence of OVA IgE-binding epitope as the template. Key process parameters including template concentration, electropolymerization cycle, pH, time required for template removal and rebinding were optimized. Electrochemical detection of OVA was performed by differential pulse voltammetry (DPV) in 5 mM KFe(CN) and 0.1 M KCl as the supporting electrolyte. Under optimized conditions, the sensor demonstrated excellent sensitivity toward OVA with linear range from 23.25 to 232.50 nM (1 to 10 ppm), limit of detection (LOD) of 10.76 nM (0.46 ppm), and limit of quantification (LOQ) of 35.87 nM (1.54 ppm). The sensor also exhibited good selectivity against other proteins such as human serum albumin (HSA), bovine serum albumin (BSA), and lysozyme (LYZ). OVA in wine samples was detected with RSD of 5.63-10.82%, and recovery percentage of 104.74-105.96%. The developed method can be easily adapted to detect other allergic proteins in the food supply chain.
Topics: Animals; Carbon; Cattle; Electrochemistry; Electrodes; Epitopes; Humans; Indoles; Limit of Detection; Ovalbumin; Polymers
PubMed: 33838516
DOI: 10.1016/j.bioelechem.2021.107805 -
International Journal of Biological... Jun 2023The polymeric materials formed by proteins and polysaccharides through molecular interactions have attracted public attention. In this study, a novel binary complex...
The polymeric materials formed by proteins and polysaccharides through molecular interactions have attracted public attention. In this study, a novel binary complex consisting of ovalbumin (OVA) and fucoidan (FUC) was obtained by electrostatic self-assembly. The self-assembly properties and the formation mechanism of the OVA-FUC binary complex were investigated by changing the charging degree and density of complex through altering pH value and polysaccharides proportion. Structural changes during the OVA-FUC electrostatic self-assembly process were investigated by a phase diagram, ζ-potential, and particle size. The optimal conditions for preparing soluble OVA-FUC binary complex were determined by the protein retention rate and insoluble solids content. Results showed that the soluble OVA-FUC binary complex could be obtained at the pH of 3.5 to 5, and the insoluble OVA-FUC binary complex was generated at the pH of 2.5 to 3.5. The OVA-FUC binary complex (19 ± 0.29 mN/m) possessed a medium ability to reduce interfacial tension of the water-oil interface compared with OVA (15 ± 1.13 mN/m) and FUC (24 ± 0.3 mN/m), indicating that OVA-FUC binary complex has good amphiphilicity and can be applied as a potential pH-controlled emulsifier in function food systems for delivering bioactive substances.
Topics: Ovalbumin; Polysaccharides; Emulsifying Agents
PubMed: 37121411
DOI: 10.1016/j.ijbiomac.2023.124644 -
Food Chemistry Jul 2018Hen egg is commonly used in some cereal-based food, including cakes and bread. Ovalbumin, one of the major components of egg white protein, can affect the performance of...
Hen egg is commonly used in some cereal-based food, including cakes and bread. Ovalbumin, one of the major components of egg white protein, can affect the performance of the food product. The interaction between ovalbumin and gluten protein and its effect on property of dough and quality of Chinese steamed bread was investigated in this study. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) patterns indicated that ovalbumin was surprisingly not incorporated in glutenins by covalent bond, whereas size-exclusion high-performance liquid chromatography showed that glutenin macropolymer content in glutenins increased slightly. Furthermore, dynamic rheology experiments indicated ovalbumin led to a decrease inG' andG″ of dough. Based on molecular dynamic simulation and SDS-PAGE results, it was inferred that ovalbumin was not hydrolyzed by endopeptidases during dough fermentation and crosslinked to gluten proteins during steaming. Finally, ovalbumin improved maximum dough height (Hm) during dough development and specific volume of Chinese steamed bread.
Topics: Animals; Bread; Chickens; China; Chromatography, Gel; Cooking; Electrophoresis, Polyacrylamide Gel; Endopeptidases; Female; Fermentation; Glutens; Hydrolysis; Ovalbumin; Steam; Triticum
PubMed: 29502822
DOI: 10.1016/j.foodchem.2018.01.150 -
Brazilian Journal of Medical and... Nov 1998Oral tolerance is a phenomenon that may occur in animals exposed to protein antigens for the first time by the oral route. They become unable to produce immune responses... (Review)
Review
Oral tolerance is a phenomenon that may occur in animals exposed to protein antigens for the first time by the oral route. They become unable to produce immune responses at the levels normally observed when they are immunized parenterally with antigen in the presence of adjuvants. Lipids have been used as adjuvants for both parenteral and oral immunization. In the present study we coupled ovalbumin with palmitate residues by incubating the protein with the N-hydroxysuccinimide palmitate ester and tested the preparation for its ability to induce oral tolerance. This was performed by giving 20 mg of antigen to mice by the oral route 7 days prior to parenteral immunization in the presence of A1(OH)3. Mice were bled one week after receiving a booster that was given 2 weeks after primary immunization. Specific antibodies were detected by ELISA. Despite the fact that the conjugates are as immunogenic as the unmodified protein when parenterally injected in mice, they failed to induce oral tolerance. This discrepancy could be explained by differences in the intestinal absorption of the two forms of the antigen. In fact, when compared to the non-conjugated ovalbumin, a fast and high absorption of the lipid-conjugated form of ovalbumin was observed by "sandwich" ELISA.
Topics: Animals; Immune Tolerance; Mice; Ovalbumin; Palmitates; Serine Proteinase Inhibitors
PubMed: 9921278
DOI: 10.1590/s0100-879x1998001100009 -
The Journal of Allergy and Clinical... Jun 2011
Topics: Animals; Chickens; Egg Hypersensitivity; Humans; Influenza Vaccines; Ovalbumin; Time Factors
PubMed: 21397313
DOI: 10.1016/j.jaci.2011.02.003 -
International Journal of Molecular... Feb 2017The aim of the present study was to investigate whether glycated ovalbumin (OVA) showed novel activity at the lipid-water interface. Mannosylated OVA (Man-OVA) was...
The aim of the present study was to investigate whether glycated ovalbumin (OVA) showed novel activity at the lipid-water interface. Mannosylated OVA (Man-OVA) was prepared by modification of the carboxyl groups with -aminophenyl α-dextro (d)-mannopyranoside. An increase in the number of modified carboxyl groups increased the membrane-damaging activity of Man-OVA on cell membrane-mimicking vesicles, whereas OVA did not induce membrane permeability in the tested phospholipid vesicles. The glycation of carboxyl groups caused a notable change in the gross conformation of OVA. Moreover, owing to their spatial positions, the Trp residues in Man-OVA were more exposed, unlike those in OVA. Fluorescence quenching studies suggested that the Trp residues in Man-OVA were located on the interface binds with the lipid vesicles, and their microenvironment was abundant in positively charged residues. Although OVA and Man-OVA showed a similar binding affinity for lipid vesicles, the lipid-interacting feature of Man-OVA was distinct from that of OVA. Chemical modification studies revealed that Lys and Arg residues, but not Trp residues, played a crucial role in the membrane-damaging activity of Man-OVA. Taken together, our data suggest that glycation of carboxyl groups causes changes in the structural properties and membrane-interacting features of OVA, generating OVA with membrane-perturbing activities at the lipid-water interface.
Topics: Amino Acids; Animals; Cell Membrane; Glycosylation; Membrane Lipids; Ovalbumin; Phospholipids; Protein Stability; Spectrometry, Fluorescence; Temperature
PubMed: 28264493
DOI: 10.3390/ijms18030520