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Poultry Science Dec 2013Egg white contains many functionally important proteins. Ovalbumin (54%), ovotransferrin (12%), ovomucoid (11%), ovomucin (3.5%), and lysozyme (3.5%) are among the major... (Review)
Review
Egg white contains many functionally important proteins. Ovalbumin (54%), ovotransferrin (12%), ovomucoid (11%), ovomucin (3.5%), and lysozyme (3.5%) are among the major proteins that have high potentials for industrial applications if separated. The separation methods for these proteins from egg white have been developed since early 1900, but preparation methods of these proteins for commercial applications are still under development. Simplicity and scalability of the methods, use of nontoxic chemicals for the separation, and sequential separation for multiple proteins are very important criteria for the commercial production and application of these proteins. The separated proteins can be used in food and pharmaceutical industry as is or after modifications with enzymes. Ovotransferrin is used as a metal transporter, antimicrobial, or anticancer agent, whereas lysozyme is mainly used as a food preservative. Ovalbumin is widely used as a nutrient supplement and ovomucin as a tumor suppression agent. Ovomucoid is the major egg allergen but can inhibit the growth of tumors, and thus can be used as an anticancer agent. Hydrolyzed peptides from these proteins showed very good angiotensin I converting enzyme inhibitory, anticancer, metal binding, and antioxidant activities. Therefore, separation of egg white proteins and the productions of bioactive peptides from egg white proteins are emerging areas with many new applications.
Topics: Animals; Avian Proteins; Chickens; Dietary Supplements; Egg Proteins; Egg White; Food Handling; Pharmaceutical Preparations
PubMed: 24235241
DOI: 10.3382/ps.2013-03391 -
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 -
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 -
Foods (Basel, Switzerland) Aug 2022Chicken egg whites contain hundreds of proteins, and are widely used in the food, biological and pharmaceutical industries. It is highly significant to study the... (Review)
Review
Chicken egg whites contain hundreds of proteins, and are widely used in the food, biological and pharmaceutical industries. It is highly significant to study the separation and purification of egg white proteins. This review first describes the structures and functional properties of several major active proteins in egg whites, including ovalbumin, ovotransferrin, ovomucoid, lysozyme, ovomucin, ovomacroglobulin and avidin. Then, the common techniques (including precipitation, chromatography and membrane separation) and some novel approaches (including electrophoresis, membrane chromatography, aqueous two-phase system and molecular imprinting technology) for the separation and purification of egg white proteins broadly reported in the current research are introduced. In addition, several co-purification methods for simultaneous separation of multiple proteins from egg whites have been developed to improve raw material utilization and reduce costs. In this paper, the reported techniques in the last decade for the separation and purification of chicken egg white proteins are reviewed, discussed and prospected, aiming to provide a reference for further research on egg proteins in the future.
PubMed: 36010434
DOI: 10.3390/foods11162434 -
Frontiers in Nutrition 2022Albumen quality is recognized as one of the major yardsticks in measuring egg quality. The elasticity of thick albumen, a strong bond in the ovomucin-lysozyme complex,... (Review)
Review
Albumen quality is recognized as one of the major yardsticks in measuring egg quality. The elasticity of thick albumen, a strong bond in the ovomucin-lysozyme complex, and excellent biological properties are indicators of high-quality albumen. The albumen quality prior to egg storage contribute to enhance egg's shelf life and economic value. Evidence suggests that albumen quality can deteriorate due to changes in albumen structure, such as the degradation of β-ovomucin subunit and -glyosidic bonds, the collapse of the ovomucin-lysozyme complex, and a decrease in albumen protein-protein interaction. Using organic minerals, natural plants and animal products with antioxidant and antimicrobial properties, high biological value, no residue effect and toxicity risk could improve albumen quality. These natural products (e.g., tea polyphenols, marigold extract, magnolol, essential oils, Upro (small peptide), yeast cell wall, species, a purified amino acid from animal blood, and pumpkin seed meal) are bio-fortified into eggs, thus enhancing the biological and technological function of the albumen. Multiple strategies to meeting laying hens' metabolic requirements and improvement in albumen quality are described in this review, including the use of amino acids, vitamins, minerals, essential oils, prebiotics, probiotics, organic trace elements, and phytogenic as feed additives. From this analysis, natural products can improve animal health and consequently albumen quality. Future research should focus on effects of these natural products in extending shelf life of the albumen during storage and at different storage conditions. Research in that direction may provide insight into albumen quality and its biological value in fresh and stored eggs.
PubMed: 35757269
DOI: 10.3389/fnut.2022.875270 -
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 -
Trends in Food Science & Technology Sep 2010Ovomucin, accounting for ∼3.5% of total egg white protein, is responsible for the thick gel characteristics of liquid egg white. Besides its excellent foaming and... (Review)
Review
Ovomucin, accounting for ∼3.5% of total egg white protein, is responsible for the thick gel characteristics of liquid egg white. Besides its excellent foaming and emulsion capacities, it possesses anti-viral, anti-bacterial, anti-tumor and other bioactivities. This paper reviews compositional, structural, physicochemical, functional and biological properties of ovomucin, as well as development of methods of extraction. As one of the least defined proteins in egg white, further study is required to characterize the structure and to explore its full potential in new applications as functional foods and nutraceuticals.
PubMed: 32288227
DOI: 10.1016/j.tifs.2010.07.001 -
International Journal of Biological... Nov 2018Ovomucin (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...
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 HN and HN, 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.
Topics: Antiviral Agents; Hemagglutinins; Influenza A Virus, H1N1 Subtype; Influenza A Virus, H5N1 Subtype; N-Acetylneuraminic Acid; Ovomucin
PubMed: 30071221
DOI: 10.1016/j.ijbiomac.2018.07.186 -
Antioxidants (Basel, Switzerland) Mar 2022Enhanced albumen quality is reflected in increased thick albumen height, albumen weight, and Haugh unit value, while the antimicrobial, antioxidant, foaming, gelling,... (Review)
Review
Enhanced albumen quality is reflected in increased thick albumen height, albumen weight, and Haugh unit value, while the antimicrobial, antioxidant, foaming, gelling, viscosity, and elasticity attributes are retained. Improved albumen quality is of benefit to consumers and to the food and health industries. Egg quality often declines during storage because eggs are highly perishable products and are most often not consumed immediately after oviposition. This review provides insights into albumen quality in terms of changes in albumen structure during storage, the influence of storage time and temperature, and the mitigation effects of natural dietary antioxidants of plant origin. During storage, albumen undergoes various physiochemical changes: loss of moisture and gaseous products through the shell pores and breakdown of carbonic acid, which induces albumen pH increases. High albumen pH acts as a catalyst for structural changes in albumen, including degradation of the β-ovomucin subunit and -glycosidic bonds, collapse of the ovomucin-lysozyme complex, and decline in albumen protein-protein interactions. These culminate in declined albumen quality, characterized by the loss of albumen proteins, such as ovomucin, destabilized foaming and gelling capacity, decreased antimicrobial activity, albumen liquefaction, and reduced viscosity and elasticity. These changes and rates of albumen decline are more conspicuous at ambient temperature compared to low temperatures. Thus, albumen of poor quality due to the loss of functional and biological properties cannot be harnessed as a functional food, as an ingredient in food processing industries, and for its active compounds for drug creation in the health industry. The use of refrigerators, coatings, and thermal and non-thermal treatments to preserve albumen quality during storage are limited by huge financial costs, the skilled operations required, environmental pollution, and residue and toxicity effects. Nutritional interventions, including supplementation with natural antioxidants of plant origin in the diets of laying hens, have a promising potential as natural shelf-life extenders. Since they are safe, without residue effects, the bioactive compounds could be transferred to the egg. Natural antioxidants of plant origin have been found to increase albumen radical scavenging activity, increase the total antioxidant capacity of albumen, reduce the protein carbonyl and malondialdehyde (MDA) content of albumen, and prevent oxidative damage to the magnum, thereby eliminating the transfer of toxins to the egg. These products are targeted towards attenuating oxidative species and inhibiting or slowing down the rates of lipid and protein peroxidation, thereby enhancing egg quality and extending the shelf life of albumen.
PubMed: 35453315
DOI: 10.3390/antiox11040630 -
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