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International Journal of Biological... Nov 2020Intestinal 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... (Review)
Review
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.
Topics: Animals; Anti-Bacterial Agents; Anti-Inflammatory Agents; Antineoplastic Agents; Antioxidants; Chickens; Egg Proteins; Eggs; Gastrointestinal Microbiome; Intestinal Mucosa; N-Acetylneuraminic Acid; Ovomucin; Peptides; Poultry; Structure-Activity Relationship
PubMed: 32569696
DOI: 10.1016/j.ijbiomac.2020.06.148 -
Food Chemistry Jan 2022Clarification of the mechanism of heat-induced gel formation by proteins under natural food systems could provide important references for the regulation of food...
Clarification of the mechanism of heat-induced gel formation by proteins under natural food systems could provide important references for the regulation of food texture. In the present study, the proteins involved in the early stage (heating at 72 °C for 8 min) of egg-white thermal gel (EWG) formation were studied quantitatively through comparative proteomic analysis. We discovered that the abundance of ovalbumin and ovomucoid increased significantly (p < 0.01), whereas that of ovotransferrin, lysozyme, ovomucin (mucin 5B and mucin 6) decreased significantly (p < 0.01), in the supernatant of EWG. If the initial interaction of egg white proteins was altered by ultrasonic pretreatment, the abundance of ovomucin and lysozyme in the supernatant of EWG increased, and was accompanied by the change from a solid gel to a fluid gel. Based on these results, we hypothesize that ovomucin has a key role in the formation and regulation of EWG properties.
Topics: Animals; Chickens; Conalbumin; Egg Proteins; Ovalbumin; Ovomucin; Proteomics
PubMed: 34293545
DOI: 10.1016/j.foodchem.2021.130596 -
Drug Delivery and Translational Research Aug 2017Ovomucin, with a similar structure to mucin and gelation ability at room temperature, is a potential mucosal carrier. To evaluate this potential, the mucoadhesive...
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.
Topics: Acrylic Resins; Alginates; Chitosan; Ciprofloxacin; Drug Carriers; Drug Liberation; Gastric Juice; Glucuronic Acid; Hexuronic Acids; Intestinal Mucosa; Intestinal Secretions; Kinetics; Nanoparticles; Ovomucin; Particle Size; Rheology; Tensile Strength
PubMed: 28717995
DOI: 10.1007/s13346-017-0406-3 -
Poultry Science Jan 2019Ovomucin 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...
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.
Topics: Animals; Chickens; Egg White; Egg Yolk; Eggs; Food Storage; Hydrogen-Ion Concentration; Ovomucin; Temperature; Time Factors; Viscosity
PubMed: 30107537
DOI: 10.3382/ps/pey349 -
Ultrasonics Sonochemistry Sep 2022The effects of ultrasonic treatment on the structure, functional properties and bioactivity of Ovomucin (OVM) were investigated in this study. Ultrasonic treatment could...
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.
Topics: Antioxidants; Enzyme-Linked Immunosorbent Assay; Hydrophobic and Hydrophilic Interactions; Ovomucin; Ultrasonics
PubMed: 36088894
DOI: 10.1016/j.ultsonch.2022.106153 -
International Journal of Biological... Oct 2018Ovomucin has a great potential because of its numerous bioactivities, which makes it an attractive molecule for industrials. However, to isolate soluble ovomucin without...
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 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 g L, 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.
Topics: Animals; Antiviral Agents; Chickens; Chromatography, Gel; Egg White; Humans; Inhibitory Concentration 50; Ovomucin; Virus Diseases; Viruses
PubMed: 29944939
DOI: 10.1016/j.ijbiomac.2018.06.101 -
Glycoconjugate Journal May 2011Ovomucin is a bioactive egg white glycoprotein responsible for the gel properties of fresh egg white and is believed to be involved in egg white thinning, a natural...
Ovomucin is a bioactive egg white glycoprotein responsible for the gel properties of fresh egg white and is believed to be involved in egg white thinning, a natural process that occurs during storage. Ovomucin is composed of two subunits: a carbohydrate-rich β-ovomucin with molecular weight of 400-610 KDa and a carbohydrate-poor α-ovomucin with molecular mass of 254 KDa. In addition to limited information on O-linked glycans of ovomucin, there is no study on either the N-glycan structures or the N-glycosylation sites. The purpose of the present study was to characterize the N-glycosylation of ovomucin from fresh eggs using nano LC ESI-MS, MS/MS and MALDI MS. Our results showed the presence of N-linked glycans on both glycoproteins. We found 18 potential N-glycosylation sites in α-ovomucin. 15 sites were glycosylated, one site was found in both glycosylated and non-glycosylated forms and two potential glycosylation sites were found unoccupied. The N-glycans of α-ovomucin found on the glycosylation sites are complex-type structures with bisecting N-acetylglucosamine. MALDI MS of the N-glycans released from α-ovomucin by PNGase F revealed that the most abundant glycan structure is a bisected type of composition GlcNAc(6)Man(3). Two N-glycosylated sites were found in β-ovomucin.
Topics: Amino Acid Sequence; Chromatography, Liquid; Egg White; Glycosylation; Molecular Sequence Data; Ovomucin; Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
PubMed: 21484392
DOI: 10.1007/s10719-011-9328-3 -
International Journal of Biological... Sep 2014Metal-protein interaction for regulating the function and structure of proteins is of major interest. We demonstrate here that the addition of 9 μmol Mg2+ per mg...
Metal-protein interaction for regulating the function and structure of proteins is of major interest. We demonstrate here that the addition of 9 μmol Mg2+ per mg ovomucin resulted in a 2.0-fold increase in the adhesion capacity of ovomucin to New Disease Virus (NDV) using ELISA method. The hemagglutinin inhibition rate of 100 μg/mL ovomucin-Mg2+ mixture (9 μmol Mg2+ per mg ovomucin) to NDV increased to 55.61%, which is significantly higher than that of the pure ovomucin (P<0.01). Binding characteristics of ovomucin to Mg2+ were then evident by fluorescence and FT-IR spectroscopy as well as dynamic light scattering (DLS) technology. Fluorescence and FT-IR spectroscopy results suggest that Mg2+ prefers to interact with the carbohydrate moiety of ovomucin without significant changes in the secondary structure when Mg2+ concentration is less than 9 μmol/mg ovomucin. When Mg2+ increases to 16 μmol/mg ovomucin, it gives rise to changes in secondary structure, and forms a more compact configuration. This is supported by the hydrodynamic radius of ovomucin with and without Mg2+ binding as examined by DLS. The Mg2+ bound in regulating the structure and activity of ovomucin provided important insight into the effect of metal ions on ovomucin binding to pathogens.
Topics: Antiviral Agents; Magnesium; Ovomucin; Protein Binding; Structure-Activity Relationship
PubMed: 25010475
DOI: 10.1016/j.ijbiomac.2014.06.056 -
Journal of Agricultural and Food... Oct 2018Ovomucin is a mucin-type glycoprotein accounting for 3.5% (w/w) of total egg white proteins. The purpose of the study was to explore the potential of ovomucin as a...
Ovomucin is a mucin-type glycoprotein accounting for 3.5% (w/w) of total egg white proteins. The purpose of the study was to explore the potential of ovomucin as a protein-resistant material. Using bovine serum albumin (BSA) as a model protein, ovomucin decreased the fluorescence intensities of the adsorbed BSA from 10.90 ± 2.18 to 0.67 ± 0.75, indicating its protein-resistant property. To understand the underlying mechanism, pure repulsive forces between ovomucin and model proteins (e.g., BSA and ovomucin) at various pHs (2.0, 6.0, and 7.2) and ionic strengths (0.1, 10, and 150 mM NaCl) were measured using a surface forces apparatus. Further studies by using atomic force microscope imaging, zeta potential, and dynamic light scattering suggested that the protein-resistant property of ovomucin was mainly attributed to strong electrostatic and steric repulsions between protein layers. This work has demonstrated that ovomucin has antifouling potential with broad applications in the areas of food processing industry and biomedical implants.
Topics: Adsorption; Glycoproteins; Hydrogen-Ion Concentration; Nanoparticles; Osmolar Concentration; Ovomucin; Protein Binding; Serum Albumin, Bovine; Static Electricity; Surface Properties
PubMed: 30277391
DOI: 10.1021/acs.jafc.8b03905 -
Journal of Food Science Jul 2012Ovomucin has been considered to contribute a lot to the excellent functional properties of egg white. This work focused on investigating the effects of pH and protein...
UNLABELLED
Ovomucin has been considered to contribute a lot to the excellent functional properties of egg white. This work focused on investigating the effects of pH and protein concentration on foaming and emulsifying properties of ovomucin to evaluate the proper use of this egg protein as a functional food ingredient, and to clarify its contribution to the functional properties of egg white under different pH conditions. Protein solubility and surface hydrophobicity were measured through the pH ranged from 2.3 to 11.0. Alkali treatment gave ovomucin improved emulsification properties, which were correlated well with the surface hydrophobicity (r ≥ 0.89, P < 0.01). Although ovomucin showed lower foaming capacity in acid and neutral solution, enhanced foaming stability was observed with weak acid-treated ovomucin (pH 5 to 6) compared to native ovomucin. These results demonstrated that acid and alkali treatment, which leads to partial unfolding of ovomucin can improve functional properties of ovomucin, with the greatest improvement for emulsification properties being from the alkali treatment and for foaming stability being from weak acid treatment. These results are helpful to produce unfolding ovomucin suitable for wide range of applications in food industry, and to provide useful information on the proper use of egg white in different food systems.
PRACTICAL APPLICATION
Ovomucin plays a critical functional role in egg white products. However, it is typically insoluble in distilled water or common salt solutions, which has thus limited its commercial applications. Alkaline treatment resulted in gradual increase in solubility, which markedly enhanced the emulsifying properties, on the other hand foaming stability of ovomucin can be promoted by weak acid treatment. The results of this work help to produce unfolding ovomucin suitable for wide range of applications in food industry, and to provide useful information on the proper use of egg white in different food systems.
Topics: Egg Proteins; Egg White; Emulsions; Food Handling; Hydrogen-Ion Concentration; Hydrophobic and Hydrophilic Interactions; Ovomucin; Solubility; Solutions
PubMed: 22694721
DOI: 10.1111/j.1750-3841.2012.02761.x