scholarly journals Evaluation of the purification process of phosvitin extracted from chicken egg yolk using liquid chromatography

2021 ◽  
Vol 13 (2) ◽  
pp. 77-84
Author(s):  
Khoa Nguyen Tran ◽  
Van Song Toan Vo
Keyword(s):  
Recovery Rate ◽  
Gel Filtration ◽  
Egg Yolk ◽  
Anion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Phosphorus Recovery ◽  
Purification Process ◽  
Factors Affecting ◽  
Chicken Egg ◽  
Chicken Egg Yolk

Phosvitin from chicken egg yolk, known as a phosphoglycoprotein, owns a very strong metal chelating property due to its polyanionic character. This study aimed to evaluate the factors affecting the purification process and suitable conditions to increase phosvitin’s purity. Phosvitin was separated from yolk granules by using 10% of NaCl solution in 0.05 M NaOH solution and heat treatment which removes lipoprotein from the extracted solution. The highest phosphorus content (58.14 mg) and phosphorus recovery rate (32.4%) were obtained at thermal treatment of 30℃ for 30 minutes. In addition, phosvitin was purified using anion-exchange chromatography (AEC) and gel-filtration chromatography (GFC). The fraction 1 (F1) obtained from AEC using UNO-Sphere Q at pH 8 had the recovery rate of phosvitin approximately 72.73%. Furthermore, fraction F1 was separated on GFC to obtain two main sub-fractions (F1 and F2). Sub-fraction F1 from gel filtration was composed mostly of β-phosvitin with a high recovery rate (81.93%) while F2 was dominant with α-phosvitin in a lower phosvitin recovery rate (16.89%). These findings will provide useful information for further researches on other properties of phosvitin so that it can be applied widely in human needs.

Preparation of immunoglobulin from chicken egg yolk by anion-exchange chromatography

2013 ◽  
Vol 30 (1) ◽  
pp. 80-85
Author(s):  
Liying WANG ◽  
Meihu MA ◽  
Zhaoxia CAI ◽  
Yongguo JIN ◽  
Xi HUANG
Keyword(s):  
Anion Exchange ◽  
Egg Yolk ◽  
Anion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Chicken Egg ◽  
Chicken Egg Yolk

scholarly journals Biotin-binding protein from chicken egg yolk. Assay and relationship to egg-white avidin

1976 ◽  
Vol 157 (2) ◽  
pp. 395-400 ◽  
Author(s):  
H B White ◽  
B A Dennison ◽  
M A Della Fera ◽  
C J Whitney ◽  
J C McGuire ◽  
...  
Keyword(s):  
Binding Protein ◽  
Gel Filtration ◽  
Egg Yolk ◽  
Egg White ◽  
Specific Protein ◽  
Chicken Egg ◽  
Biotin Binding ◽  
Lower Temperature ◽  
Chicken Egg Yolk ◽  
Kinetics Of

1. Biotin in chicken egg yolk is non-covalently bound to a specific protein that comprises 0.03% of the total yolk protein (0.8 mg/yolk). This biotin-binding protein is not detectable by the normal avidin assay owing to the biotin being tightly bound. Exchange of [14C]biotin for bound biotin at 65 degrees C is the basis of an assay for this protein. 2. Biotin-binding protein from egg yolk is distinguishable from egg-white avidin on Sephadex G-100 gel filtration, although the sizes of the two proteins appear quite similar. 3. Biotin-binding protein is denatured at a lower temperature and freely exchanges biotin at lower temperatures than does avidin. 4. The biotin-binding protein in egg yolk is postulated to be responsible for the deposition of biotin in egg yolk. D-[carboxyl-14C]Biotin injected into laying hens rapidly appears in the egg bound to yolk biotin-binding protein and avidin. Over 60% of the radioactivity is eventually deposited in eggs. The kinetics of biotin deposition in the egg suggests a 25 day half-life for an intracellular biotinyl-coenzyme pool in the laying hen.

scholarly journals CRYOPRESERVATION OF KAMPUNG ROOSTER SEMEN USING EGG YOLK DILUENT FROM FOUR TYPES OF POULTRY WITH DIFFERENT CONCENTRATIONS

2019 ◽  
Vol 13 (3) ◽  
Author(s):  
Khairuddin Khairuddin ◽  
Muhammad Erik Kurniawan ◽  
Soman Soman
Keyword(s):  
Liquid Nitrogen ◽  
Recovery Rate ◽  
Egg Yolk ◽  
Spermatozoa Motility ◽  
Chicken Egg ◽  
Nitrogen Vapor ◽  
Before And After ◽  
Egg Yolks ◽  
Chicken Egg Yolk

The aim of this study was to determine the type and the best concentration of egg yolk in maintaining the quality of kampung rooster spermatozoa during cryopreservation. This study used a completely randomized factorial pattern design with the first factor was the type of egg yolk (purebred chicken, kampung chicken, duck, and quail) and the second factor was the concentration of egg yolk (5%, 10%, and 15%). Semen was collected from twelve kampung roosters using massage method. Immediately after collection, the semen was evaluated macroscopically and microscopically. Semen with more than 70% motility was used in this study. The semen was diluted, packed in a ministraw, equilibrated, and frozen using liquid nitrogen vapor and stored in a liquid nitrogen container for 24 hours. Observation of spermatozoa motility was carried out in fresh semen, diluted semen, after equilibration and after thawing with four replications. The results showed that the type of egg yolk treatment had no effect (P0.05) on the recovery rate and motility of spermatozoa before and after cryopreservation, but egg yolk concentration had a highly significant effect (P0.01) on the quality of spermatozoa. Egg yolks in 10-15% concentration had spermatozoa motility and recovery rate higher than egg yolk with 5% concentration. In conclusion, purebred chicken egg yolk, kampung chicken egg yolk, duck egg yolk, and quail egg yolk each in diluent can be used to maintain the quality of kampung rooster spermatozoa at a concentration of 10-15% during cryopreservation.

Chicken egg yolk antibodies (IgY)-based antivenom for neutralization of snake venoms: a review

Toxin Reviews ◽  
2021 ◽  
pp. 1-12
Author(s):  
Ankit Choraria ◽  
Rajeswari Somasundaram ◽  
S. Janani ◽  
Selvakumar Rajendran ◽  
Naoual Oukkache ◽  
...  
Keyword(s):  
Egg Yolk ◽  
Snake Venoms ◽  
Chicken Egg ◽  
Egg Yolk Antibodies ◽  
Chicken Egg Yolk

scholarly journals Chemical identity of tryptensin with angiotensin

1980 ◽  
Vol 187 (3) ◽  
pp. 647-653 ◽  
Author(s):  
K Arakawa ◽  
M Yuki ◽  
M Ikeda
Keyword(s):  
Amino Acid ◽  
Thin Layer ◽  
Gel Filtration ◽  
Deae Cellulose ◽  
Anion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Cation Exchange Chromatography ◽  
Human Plasma Protein ◽  
Plasma Protein Fraction ◽  
Layer Chromatography

Tryptensin, a vasopressor substance generated from human plasma protein fraction IV-4 by trypsin, has been isolated and the amino acid composition analysed. The procedures used for the isolation were: (a) adsorption of the formed tryptensin on Dowex 50W (X2; NH4+ form); (b) gel filtration through Sephadex G-25; (c) cation-exchange chromatography on CM-cellulose; (d) anion-exchange chromatography on DEAE-cellulose; (e) re-chromatography on CM-cellulose; (f) gel filtration on Bio-Gel P-2; (g) partition chromatography on high-pressure liquid chromatography. The homogeneity of the isolated tryptensin was confirmed by thin-layer chromatography and thin-layer electrophoresis. The amino acid analysis of the hydrolysate suggested the following proportional composition: Asp, 1; Val, 1; Ile, 1; Tyr, 1; Phe, 1; His, 1; Arg, 1; Pro, 1. This composition is identical with that of human angiotensin.

Development of viper-venom antibodies in chicken egg yolk and assay of their antigen binding capacity

Toxicon ◽  
2002 ◽  
Vol 40 (7) ◽  
pp. 857-861 ◽  
Author(s):  
C Maya Devi ◽  
M Vasantha Bai ◽  
L.K Krishnan
Keyword(s):  
Binding Capacity ◽  
Egg Yolk ◽  
Antigen Binding ◽  
Chicken Egg ◽  
Chicken Egg Yolk

Isolation of Immunoglobulin from Chicken Egg Yolk using Single-Stage Ultrafiltration with 100-kDa Regenerated Cellulose Membranes

2011 ◽  
Vol 7 (1) ◽  
Author(s):  
Jianguo Liu ◽  
Juan Yang ◽  
Hai Xu ◽  
Hu Zhu ◽  
Jianbo Qu ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Egg Yolk ◽  
Single Stage ◽  
Regenerated Cellulose ◽  
Cellulose Membrane ◽  
Permeate Flux ◽  
Operational Parameters ◽  
Solution Ph ◽  
Chicken Egg ◽  
Chicken Egg Yolk

The aim of this work is to develop a membrane-based cost-effective process for the rapid isolation of immunoglobulin from chicken egg yolk. It was found that a single-stage ultrafiltration using a 100 kDa molecular weight cut-off regenerated cellulose membrane could be employed to isolate immunoglobulin from the crude feedstock. The effects of operational parameters (solution pH, ionic strength, stirring speed and permeate flux) on the transmission of immunoglobulin and the presence of impurity protein with molecular weight close to immunoglobulin were quantified using the parameter scanning ultrafiltration technique. Under optimized conditions, the purity of immunoglobulin obtained was about 85 percent after the single-stage ultrafiltration process, and the recovery of immunoglobulin from the feedstock was 91 percent.

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