Abstract: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 … Show more
“…Protein profiles of raw and heat-treated egg samples recorded using SDS-PAGE analysis were given in Figure 1. Egg yolk and white proteins belonging to each poultry species were well-fractionated on the gels in consistency with the previous studies [4,7,15,17,18]. Based on their molecular weights, the identification of the protein fractions in egg white and yolk were carried out by the help of marker proteins (M) run in the corresponding lanes of each gel.…”
Section: Protein Profilingsupporting
confidence: 62%
“…Besides these beneficial effects, one adverse effect is associated with allergic reactions in the human body due to egg proteins [2,3]. In comparison to hen and quail eggs, turkey and goose eggs' proteins can exhibit higher allergic potential since they are big and comprising of the high amount of protein fraction [4]. A whole egg is composed of proteins (~10-14%), carbohydrates (~0.5-2.2 %), water (~88%), fat (~10-13%) , and ash (~1%) [5].…”
Poultry eggs are highly important in human nutrition due to their content of essential amino acids, vitamins, minerals, and enzymes. Eggs of edible poultries such as hen, turkey, quail, and goose may have some differences in their nutritional composition. Various heat treatments applied before consumption lead to some alterations in their nutrients, especially proteins. The purpose of this study was to investigate compositional and structural changes in the protein fractions of hen, quail, turkey, and goose eggs when exposed to soft-and hard-boiling (11-16 min and 18-19 min), and frying (2-7 min). Electrophoresis and spectroscopy were used to determine the effects of these heat treatments on egg white and yolk proteins separately. It was observed that the heat degradation of proteins in egg white was higher than that in egg yolk. As expected, protein degradation was increased when heat exposure was extended. Hard-boiling treatment completely denatured egg white proteins almost in all poultry species. Ovomucoid was the most resistant fraction against heat denaturation in white proteins, while livetins in yolk. Soft-boiling under the given conditions resulted in mostly retained profiles of proteins in egg yolk of all species. Relevant to protein degradation, remarkable structural changes were detected in the protein secondary structure of hard-boiled and fried egg samples. Significant data obtained in this research revealed the influence of heat treatment on the protein content of edible eggs. Those findings are expected to help in developing the processes and consumption methods of egg products for dietary purposes and improvement of human health.
“…Protein profiles of raw and heat-treated egg samples recorded using SDS-PAGE analysis were given in Figure 1. Egg yolk and white proteins belonging to each poultry species were well-fractionated on the gels in consistency with the previous studies [4,7,15,17,18]. Based on their molecular weights, the identification of the protein fractions in egg white and yolk were carried out by the help of marker proteins (M) run in the corresponding lanes of each gel.…”
Section: Protein Profilingsupporting
confidence: 62%
“…Besides these beneficial effects, one adverse effect is associated with allergic reactions in the human body due to egg proteins [2,3]. In comparison to hen and quail eggs, turkey and goose eggs' proteins can exhibit higher allergic potential since they are big and comprising of the high amount of protein fraction [4]. A whole egg is composed of proteins (~10-14%), carbohydrates (~0.5-2.2 %), water (~88%), fat (~10-13%) , and ash (~1%) [5].…”
Poultry eggs are highly important in human nutrition due to their content of essential amino acids, vitamins, minerals, and enzymes. Eggs of edible poultries such as hen, turkey, quail, and goose may have some differences in their nutritional composition. Various heat treatments applied before consumption lead to some alterations in their nutrients, especially proteins. The purpose of this study was to investigate compositional and structural changes in the protein fractions of hen, quail, turkey, and goose eggs when exposed to soft-and hard-boiling (11-16 min and 18-19 min), and frying (2-7 min). Electrophoresis and spectroscopy were used to determine the effects of these heat treatments on egg white and yolk proteins separately. It was observed that the heat degradation of proteins in egg white was higher than that in egg yolk. As expected, protein degradation was increased when heat exposure was extended. Hard-boiling treatment completely denatured egg white proteins almost in all poultry species. Ovomucoid was the most resistant fraction against heat denaturation in white proteins, while livetins in yolk. Soft-boiling under the given conditions resulted in mostly retained profiles of proteins in egg yolk of all species. Relevant to protein degradation, remarkable structural changes were detected in the protein secondary structure of hard-boiled and fried egg samples. Significant data obtained in this research revealed the influence of heat treatment on the protein content of edible eggs. Those findings are expected to help in developing the processes and consumption methods of egg products for dietary purposes and improvement of human health.
“…In the preparation of the system butein/zinc a red precipitate was immediately formed, therefore it was not possible to perform the measurements. Pekal et al [ 49 ] provided the antioxidant properties of a Cu 2+ /quercetin complex and Bratu et al [ 26 ] on a Zn 2+ /rutin complex using the DPPH method. Both studies conclude that the radical scavenging activity of the metal flavonoid-complexes is higher than the one of the ligands alone.…”
Section: Resultsmentioning
confidence: 99%
“…Copper(II) and zinc(II) are our metals of interest, since they are endogenous metals and they have shown promising features as metallodrug candidates [ 24 , 25 ]. In fact Cu(II) and Zn(II) complexes of the flavonoids quercetin and rutin have been shown to greatly increase the antioxidant activity of this class of compounds [ 26 , 27 ]. In many complexes Zn(II) prefers a tetrahedral coordination sphere [ 28 ] while the Cu(II) cation prefers a square planar coordination.…”
Four new metal complexes [Cu(ISO)2], [Cu(BUT)2] and [Zn(ISO)2], [Zn(BUT)2] of the polyhydroxychalcones (isoliquiritigenin and butein) are synthesized, structurally characterized and their antioxidant activity is investigated. The formation of the complexes [Cu(ISO)2] and [Zn(ISO)2] is followed by Job’s plot using NMR titration. The resulting compounds are characterized by mass spectrometry, IR spectroscopy, and elemental analysis. Studies on the radical scavenging activity are performed using DPPH as substrate. The results showed that the antioxidant activities of isoliquiritigenin and butein are enhanced after binding to copper or zinc.Graphical abstract
Electronic supplementary materialThe online version of this article (doi:10.1007/s00706-016-1822-7) contains supplementary material, which is available to authorized users.
“…Due to the fact that it is a flavonoid of flavonol type which contains five hydroxyl groups in positions 3,3',4'5,7 and a carbonyl group in fourth position, quercetin easily forms complexes with a lot of metals [3]. Complexation of metal cations by quercetin has already been reported for a large number of metals (Mg (II), Fe(III), Zn (II), Al (III), Pb(II), Ni(II), Cd (II)) [4][5][6][7].…”
Complexes of cooper (II) and iron (II) with flavonoid quercetin have been synthesized. The structure of compounds has been confirmed by means of UV-Vis and FTIR spectroscopic techniques. The antioxidant activity of the flavonoid complexes has been evaluated by using the 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical scavenging method. These complexes of flavonoids are much more effective free radical scavengers than the free flavonoids, an aspect which recommends them for further studies on possible therapeutic applications.
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.