scholarly journals Soybean and Lupine Addition in Hen Nutrition—Influence on Egg Immunoreactivity

Molecules ◽  
2021 ◽  
Vol 26 (14) ◽  
pp. 4319
Author(s):  
Aneta Tomczak ◽  
Michalina Misiak ◽  
Magdalena Zielińska-Dawidziak
Keyword(s):  
Protein Profile ◽  
Protein Composition ◽  
Egg Yolk ◽  
Egg White ◽  
Tween 20 ◽  
Western Blot Method ◽  
Sds Page ◽  
Allergenic Proteins ◽  
Hen Egg White ◽  
Page Electrophoresis

Modifying hen fodder is a common way of changing eggs composition today. However, there is no information on the effect of the source of protein in the fodder replacement on egg allergenicity. This research aimed to detect potential differences in the immunoreactivity and protein composition of eggs from hens fed with fodder containing legume. The aim of the first step of the study was to select the proper solvent for extracting allergenic proteins from hen eggs. Two of them (containing Tween 20 and Triton 100) were selected, based on protein profile and concentration analysis. Egg-white- and egg-yolk-proteins extracts prepared with them were checked for potential differences, using SDS-PAGE electrophoresis, and then the Western-blot method, using sera from children allergic to eggs and soy. Preliminary studies on the influence of fodder composition on the composition of egg proteins suggest that the addition of soy and lupine to fodder modifies the expression of egg proteins. The observed differences in the immunoreactivity of proteins contained in hen egg-white samples do not seem to be as significant as the appearance of protein with a molecular weight of ~13 kDa in the yolk of eggs obtained from soybean-fed hens. This protein may increase the immunoreactivity of eggs for children allergic solely to soy.

scholarly journals Comparative Analysis of Electrophoretic Profile of Major Proteins of Milk from Alpine and Carpathian Goats

2017 ◽  
Vol 74 (1) ◽  
pp. 20 ◽  
Author(s):  
Alina NASALEAN ◽  
Laurentiu OGNEAN ◽  
Sergiu MUNTEAN ◽  
Stefana BALICI ◽  
Horea MATEI
Keyword(s):  
Protein Profile ◽  
Milk Proteins ◽  
Goat Milk ◽  
Protein Composition ◽  
Raw Milk ◽  
Biologically Active ◽  
Protein Fractions ◽  
Animal Nutrition ◽  
Sds Page ◽  
Percentage Data

The milk’s proteins provide nutritional and biologically active values, essential in human and animal nutrition. In the case of goat milk, the proteins’ concentration and quality represent basic indices for the evaluation of the nutritional and biologically active values. The proposal is to comparatively analyse the protein profile of milk. The milk was collected from two different breeds: French Alpine and Romanian Carpathian. During March and April 2016 there were collected samples of raw milk in hygienic and sanitation conditions. There were two lots: first lot has 10 Carpathian goats and the second lot has 10 Alpine goats. The protein composition of goat milk was established with SDS-PAGE, after the evaluation of the total proteins’ concentration with the Bradford method. The quantitative and percentage data obtained with electrophoresis revealed few differences between those 8 identified protein fractions. Between those two lots, regarding the levels of β-CN, k-CN and β-lactoglobulines there were significant differences. The other protein fractions have values almost identical. Statistical analysis of obtained data shaped the differences in the protein profile at those two breeds. Based on those differences it is to note the superior potential of the Alpine breed regarding the content in biologically active milk proteins. Regarding the obtained data, this study brings new contributions for the evaluation and analysis of protein profile as a nutritive and biologically active component of goat milk, confirming its character as a functional aliment.

scholarly journals Variation of egg proteins between bird varieties by using SDS-PAGE

2019 ◽  
Vol 12 (1) ◽  
pp. 68-73
Author(s):  
Questan Amin ◽  
Hemn Zhahir ◽  
Ahmed Shaker
Keyword(s):  
Sodium Dodecyl Sulfate ◽  
Trypsin Inhibitor ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Egg Yolk ◽  
Egg White ◽  
Yolk Proteins ◽  
Egg White Proteins ◽  
Sds Page

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.

scholarly journals Biological and Immunogenicity Property of IgY Anti S. mutans ComD

2016 ◽  
Vol 10 (1) ◽  
pp. 308-314 ◽  
Author(s):  
E.W. Bachtiar ◽  
B.M. Bachtiar ◽  
R.D. Soejoedono ◽  
I.W. Wibawan ◽  
A. Afdhal
Keyword(s):  
Dental Caries ◽  
Streptococcus Mutans ◽  
Dna Vaccine ◽  
Biofilm Formation ◽  
Protein Profile ◽  
Egg Yolk ◽  
Biological Properties ◽  
Coding Region ◽  
Dna Coding ◽  
Sds Page

Objective:This study aims to elucidate the effect of IgY anti ComD on the biological properties ofStreptococcus mutans. (S. mutans)ComD is an interspecies quorum-sensing signaling receptor that plays an important role in biofilm formation byS. mutans.Materials and Methodology:Egg yolk IgY was produced by the immunization of chickens with a DNA vaccine containing the ComD DNA coding region. We evaluated the effect of the antibody on biofilm formation byS. mutansisolated from subjects with or without dental caries. We also assessed the immunoreactivity of the antibody against all isolates, and analyzed the protein profile ofS. mutansby SDS-PAGE.Results:The ComD antibody was successfully induced in the hens’ eggs. It inhibited biofilm formation by allS. mutansisolates. In addition, the expression of some protein bands was affected after exposure to the antibody.Conclusion:IgYanti-S. mutansComD reduces biofilm formation by this bacterium and alters the protein profile ofS. mutans.

scholarly journals Stalk Senescence, Sugars, Proteins, and Minerals in Stalks of a Supersweet Corn at Developmental Stages

HortScience ◽  
1996 ◽  
Vol 31 (4) ◽  
pp. 687e-687
Author(s):  
K. Roberts ◽  
J. Williamson ◽  
J. Wright ◽  
C. Biles ◽  
V. Russo
Keyword(s):  
Developmental Stages ◽  
Chemical Shifts ◽  
Protein Profile ◽  
Resonance Spectroscopy ◽  
Fresh Market ◽  
Sds Page ◽  
Mineral Concentrations ◽  
Supersweet Corn ◽  
C Nmr ◽  
Page Electrophoresis

Senescence and levels of minerals, sugars, and proteins were determined in stalk internodes of corn (Zea mays L.) cv. Illini Gold, a shrunken2 hybrid, from from mid-whorl (V9; internodes completely juvenile) to fresh-market maturity (FM; internodes exhibiting stages of senescence). Senescence was rated in internodes near the base of the stalk (I7), below the ear (I9), and between the ear and tassel (I11). Tissues were extracted and analyzed by carbon-nuclear magnetic resonance spectroscopy (C-nmr) and SDS-PAGE electrophoresis. Senescence rating increased from V9 to FM. Through silk emergence (R1) C-nmr carbohydrate spectra were similar, regardless of internode, with chemical shifts between 61 and 104 ppm, mostly of glucose, fructose, and sucrose. At FM, additional lines were found that were not associated with a saccaride. The highest concentration of sucrose was at R1, fructose at tasseling (VT), and R1, and for glucose from VT to FM. The protein profile present through R1 in I7 was not present at FM. In I9, the protein profile was similar throughout. In I11, numbers, or density, of protein bands decreased through FM. Mineral concentrations did not change, decreased, or fluctuated. Levels of N, Cl, or Na at VT, R1, and FM, respectively, were negatively correlated with senescence. In I7 and I9, senescence ratings were negatively correlated with levels of Mg, NO–3, or SO2–4. Senescence appears to be associated with concentrations of some minerals, a reduction in levels of sucrose, and with the presence or absence of some proteins; however, cause and effect remains to be established. This research was hosted by USDA/SCARL at Lane, Okla., and made use of NMR equipment provided through USAF/AFOSR Grant F49620-95-1-0316 and NIH/NIGMS Grant GM 08003.

Analysis Metallothionein of Carp fish in The Brantas River, Indonesia

2020 ◽  
Vol 20 (2) ◽  
pp. 139-146
Author(s):  
Putri Ayu Ika Setiyowati ◽  
Rofiatun Solekha ◽  
Sri Bintang Sahara ◽  
Febianti Dwi Hapsari
Keyword(s):  
Molecular Weight ◽  
Western Blot ◽  
Protein Profile ◽  
Western Blot Method ◽  
Sds Page ◽  
Imagej Software ◽  
Carp Fish

This study aimed to detection of protein profile, expression of metalothionein (MT) protein, and analyze difference of MT density in liver and gill in one of Carp fish that is Barbonymus balleroides in the upstream and downstream of Brantas river. The method used observasional analytic, Two individual of Barbonymus balleroides samples taken three times (with difference of month) from two station there are upstream and downstream of Brantas river. Analysis protein profile used electrophoresis SDS-PAGE (15%), expression and density of MT used western blot method and imageJ software. Difference between MT density in liver and gill of Barbonymus balleroides in the upstream and downstream of Brantas river analyzed with Two-way ANOVA. The results showed, protein profile in liver and gill Barbonymus balleroides in the upstream and downstream Brantas river have molecular weight about 8-93 kDa, expression of MT showed band of MT with molecular weight 24 kDa, results of MT density in liver and gill on upstream and downstream, continuously 231.29 MT/µm2 and 229.87MT/µm2, 232.41 MT/µm2 and  231.56 MT/µm2 but there is not significant.

scholarly journals Effects of Pasteurization and High-Pressure Processing of Camel and Bovine Cheese Quality, and Proteolysis Contribution to Camel Cheese Softness

2021 ◽  
Vol 8 ◽  
Author(s):  
Mustapha Mbye ◽  
Huda Mohamed ◽  
Tholkappiyan Ramachandran ◽  
Fathalla Hamed ◽  
Ahlam AlHammadi ◽  
...  
Keyword(s):  
Heat Treatment ◽  
High Pressure ◽  
Protein Profile ◽  
Bovine Milk ◽  
High Pressure Processing ◽  
Camel Milk ◽  
Thermal Treatments ◽  
Sds Page ◽  
Page Electrophoresis

The effects of high-pressure processing (HPP) compared to thermal treatments on the quality of camel vs. bovine cheeses were studied. The study showed that camel milk has a lower microbial load compared to bovine milk, which is maintained during 7 days' storage of the processed milk. The effect of three HPP treatments (350, 450, and 550 MPa for 5 min at 4°C) and two pasteurization treatments (65°C for 30 min and 75°C for 30 s) on the quality of soft unripened camel and bovine milk cheeses were accessed. The cheeses were evaluated for pH, yield, proximate composition, textural and rheological properties, microstructure, and protein profile by SDS-PAGE electrophoresis. The effects of the treatments on cheese's hardness were different between the camel and bovine cheeses; while heat treatment at 65°C for 30 min gave the hardest bovine milk cheese (1,253 ± 20), HPP treatment at 350 MPa for 5 min gave the highest value for camel milk cheese (519 ± 5) (p < 0.05). The hardness of the cheeses was associated with low yield and moisture content. SDS-PAGE electrophoresis revealed that extensive proteolysis might have contributed to the softness of camel cheeses compared to bovine and suggested the involvement of some residual enzyme activities.

scholarly journals Inter-protein bonding and other molecular interactions in hen egg white

2000 ◽  
Vol 65 (3) ◽  
pp. 157-166 ◽  
Author(s):  
Marija Vuckovic ◽  
Marija Radojcic ◽  
Bratoljub Milosavljevic
Keyword(s):  
Electrostatic Interactions ◽  
Polyacrylamide Gel Electrophoresis ◽  
Three Dimensional ◽  
Egg White ◽  
Viscosity Data ◽  
Protein Gel ◽  
Sds Page ◽  
The Matrix ◽  
Hen Egg White ◽  
Hen Egg

The analysis of the SDS-polyacrylamide gel electrophoresis (SDS-PAGE) data, combined with the comparison of viscosity data corresponding to the thin fraction of hen egg white and 2 mM purefied ovalbumin solution, showed that the thin fraction is a protein solution. Dissolution of the thick fraction of hen egg white in SD Sandurea solutions followed by SDS-PAGE, in the presence or absence of b-mercaptoethanol, revealed that it is a protein gel. It was also found that the gel structure consists of the three-dimensional ovomucine- ovomucoid network (matrix) held together by S.S bridges which captures the rest of the proteins (ovalbumin, conalbumin, etc). The captured proteins can also be interconnected by S.S bridges thus forming agglomerates or conglomerates, but they are predominantly held by weak electrostatic interactions, as demonstrated by the washing out and dissolving experiments. The matrix structure does not prevent denaturation of the captured proteins as indecated by the 50% decrease in turbidity following gel swelling by the addition of 1 part of an8Murea solution to 9 parts of the gel.

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