Inhalant allergy to egg yolk and egg white proteins

Proteins are essential constituents of all organisms; both egg white proteins and egg yolk are source of protein. The aim of this study was conducted to perform preliminary studies to analyses and compare egg white proteins and yolk proteins from different avian species (guineafowl, dwarf hens, local hen, Shami, turkey, duck, geese, partridge and quail) via or with SDS-PAGE (Sodium Dodecyl Sulfate–Polyacrylamide Gel Electrophoresis ). 18 Fresh eggs of different poultry species (guineafowl, dwarf hens, local hen, Shami, turkey, duck, geese, partridge and quail) were collected from various farms in the Sulaimani province. Data on egg proteins were analyzed using Statistical Xlstate used for dendrogram construction and PCA. The main egg white proteins were Ovomicin, Ovotransferrin, Ovalbumin, Flavoprotein, α- chymotrypsinogen, and Trypsin inhibitor. The main lipoproteins were Apovitellenin VI, Apovitellenin Vb, Apovitellenin V, Apovitellenin IIIa, Apovitellenin III, Apovitellin 7, B-Livetin, Apovitellenin IIa, Apovitellenin II, and Apovitellenin I. All these lipoproteins were observed in the nine birds species. The egg white proteins and yolk lipoproteins for nine species were examined. It can be concluded the large differences were found in a mount of egg white proteins and yolk lipoproteins of the nine species of birds.

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Ultracentrifugal and electrophoretic analysis of the water-soluble fraction of chick embryo yolk

Development ◽

10.1242/dev.19.1.95 ◽

1968 ◽

Vol 19 (1) ◽

pp. 95-101

Author(s):

P. Carinci ◽

L. Manzoli-Guidotti

Keyword(s):

Soluble Fraction ◽

Relative Proportion ◽

Egg Yolk ◽

Electrophoretic Analysis ◽

Egg White ◽

Water Soluble ◽

Water Soluble Fraction ◽

Egg White Proteins ◽

Proportional Increase ◽

Quantitative Changes

Water-soluble proteins, mainly livetins (α-, β-, γ-), are present in hen egg yolk (Martin, Vandegaer & Cook, 1957). They represent 5% of fresh yolk solids (Saito, Martin & Cook, 1965). During the later stages of incubation the watersoluble proteins (water-soluble fraction, WSF) undergo a marked increase in relative proportion; after 15 days of incubation they form over 15% and at 18 days over 40% of yolk-residual solids (Saito et al. 1965). This proportional increase of the WSF is tentatively explained by the passage of egg-white proteins into yolk (Mclndoe, 1960; Saito et al. 1965). Indeed some egg-white proteins (ovalbumin, conalbumin and lysozyme) have been found in the yolk from 14 to 15 days of incubation (Saito & Martin, 1966; Carinci, Wegelin & Manzoli-Guidotti, 1966). At these stages ovalbumin is present in the yolk in such a great quantity that it is difficult to detect qualitative and quantitative changes of other proteins without resorting to further fractionations.

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Immunoreactivity of hen egg allergens: Influence on in vitro gastrointestinal digestion of the presence of other egg white proteins and of egg yolk

Food Chemistry ◽

10.1016/j.foodchem.2012.07.106 ◽

2013 ◽

Vol 136 (2) ◽

pp. 775-781 ◽

Cited By ~ 30

Author(s):

Gustavo Martos ◽

Rosina López-Fandiño ◽

Elena Molina

Keyword(s):

Egg Yolk ◽

Egg White ◽

Gastrointestinal Digestion ◽

In Vitro Gastrointestinal Digestion ◽

Egg White Proteins ◽

Hen Egg

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Triacylglycerides and Phospholipids from Egg Yolk Differently Influence the Immunostimulating Properties of Egg White Proteins

Nutrients ◽

10.3390/nu13103301 ◽

2021 ◽

Vol 13 (10) ◽

pp. 3301

Author(s):

Leticia Pérez-Rodríguez ◽

Mónica Martínez-Blanco ◽

Daniel Lozano-Ojalvo ◽

Javier Fontecha ◽

Elena Molina ◽

...

Keyword(s):

Lipid Fraction ◽

Egg Yolk ◽

Egg White ◽

Egg Allergy ◽

Egg White Proteins ◽

Lipid Fractions ◽

Adjuvant Effects ◽

The Impact ◽

Whole Egg

As part of a whole egg, egg white proteins are embedded in a lipid matrix that could modify their presentation to the immune system and their allergenic properties. The present study examines the impact of the main egg lipid components, triacylglycerides and phospholipids, in the early events of sensitization to egg. To this end, BALB/c mice were exposed intragastrically to egg lipids and egg lipid fractions, alone and in mixtures with egg white proteins, and Th2-promoting and proinflammatory effects were investigated. Our results highlight that the egg lipid fraction is responsible for Th2 adjuvant effects and point at a different influence of triacylglycerides and phospholipids on the bioavailability and immunomodulating properties of egg white proteins. While triacylglycerides promote type 2 responses at the small intestine level, phospholipids reduce the solubility of EW proteins and induce Th2 skewing in lymphoid intestinal tissues, which may have a direct impact on the development of egg allergy.

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DISTRIBUTION OF EGG WHITE PROTEINS IN CHICKEN BLOOD SERUM AND EGG YOLK

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)56088-9 ◽

1951 ◽

Vol 189 (1) ◽

pp. 1-9 ◽

Cited By ~ 3

Author(s):

Margaret E. Marshall ◽

H.F. Deutsch

Keyword(s):

Blood Serum ◽

Egg Yolk ◽

Egg White ◽

Egg White Proteins ◽

Chicken Blood

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Foaming characterization of fresh egg white proteins as a function of different proportions of egg yolk fractions

Food Hydrocolloids ◽

10.1016/j.foodhyd.2018.12.014 ◽

2019 ◽

Vol 90 ◽

pp. 118-125 ◽

Cited By ~ 9

Author(s):

Xin Li ◽

Junhua Li ◽

Cuihua Chang ◽

Chenying Wang ◽

Mengqi Zhang ◽

...

Keyword(s):

Egg Yolk ◽

Egg White ◽

Egg White Proteins

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Electrophoretic Method For Edible Eggs Species Identification

Revista de Chimie ◽

10.37358/rc.17.9.5806 ◽

2017 ◽

Vol 68 (9) ◽

pp. 1983-1987

Author(s):

Mihaela Mirela Bratu ◽

Semaghiul Birghila ◽

Horatiu Miresan ◽

Ticuta Negreanu Pirjol

Keyword(s):

Molecular Weight ◽

Gel Electrophoresis ◽

Protein Pattern ◽

Egg Yolk ◽

Egg White ◽

Native Page ◽

Electrophoretic Method ◽

Standard Curve ◽

Egg White Proteins ◽

Routine Identification

The present paper describes a simple and efficient electrophoretic method to identify the species provenience of edible eggs in food products. The proteic pattern of egg yolk and egg white was described using polyacryl amide gel electrophoresis under denaturating conditions (PAGE-SDS) separately for the egg yolk and for the egg white proteins from five edible egg species, as follows: hen, goose, duck, turkey and quail. The molecular weight of each protein strip was calculated using a molecular weight standard curve. Separately, an electrophoretic protein pattern of all the mentioned samples was done using polyacryl amide gel electrophoresis under undenaturating conditions (native PAGE). The results show clearly distinct patterns in electrophoregrams resulted both in denaturating and undenaturating conditions for each species. These methods could be useful tools for egg species routine identification in various food industrial mixtures.

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Egg Quality from Avian Species: Electrophoretic Characterization of Egg White Proteins

ANIMAL PRODUCTION ◽

10.20884/1.jap.2021.23.1.2 ◽

2021 ◽

pp. 34-43

Author(s):

Meziani Samira ◽

Drici Amine El-Mokhtar ◽

Menadi Noureddine ◽

Diaf Mustapha ◽

Zairi Mohammed ◽

...

Keyword(s):

Gel Electrophoresis ◽

Quantitative Difference ◽

Qualitative Difference ◽

Bird Species ◽

Egg Yolk ◽

Egg White ◽

Agarose Gel ◽

Agarose Gel Electrophoresis ◽

Egg White Proteins

The aim of the present study was to evaluate and to compare the physicochemical composition of egg white, and to characterize and estimate the quantitative variations of egg white proteins of different birds’ species (duck, quail, Chicken, partridge and goose). For each bird species, the whole egg temperature, weight, height, density and shape index were evaluated. After breaking the eggs, a visual examination was performed then vitelline (VI) and albumen (AI) indexes and the haugh unit (HU) were measured. The study of the quality and the characterization of egg white proteins were performed by Agarose Gel Electrophoresis. The total egg weight varied within a range of (8.98±0.82 g to 142.91±10.34 g) for quail and goose, respectively. The thickness of the egg yolk was almost three times higher than that of the egg white in all breeds. The egg freshness, measured by HU, was higher in partridge, followed by quail and chicken breeds with values of 88.81±0.09, 87.45±3.33, 81.53±2.16, respectively. The VI shows values of about 0.40. The egg yolk/ white ratio ranged from 47 and the pH varied from 8.37 to 8.95 for all local species studied. The egg white protein content was higher for all species (up to 14.45g/100 g). Three types of proteins are identified by agarose gel electrophoresis (ovalhibitor, ovotransferrin and ovalbumin) with a quantitative difference between bird species. Densitometric analysis shows a qualitative difference due to the presence of type C lysozyme in chicken egg white.

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