• Journal of Microbiology and Biotechnology
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• v.29 no.2
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• pp.311-320
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• 2019

Fusobacterium nucleatum is a morbific agent in periodontitis and halitosis. Egg yolk antibody (IgY) was obtained from egg yolks from chickens stimulated with F. nucleatum. This study was to assess the effectiveness of IgY on periodontitis and halitosis caused by F. nucleatum in vitro and in vivo. The growth of F. nucleatum was inhibited (p <0.05) by different concentrations of IgY in vitro and the results of a Halimeter show volatile sulfur compounds (VSCs) were reduced to $904{\pm}57ppb$ at a concentration 40 mg/ml of IgY. The changes of fatty acids of F. nucleatum were determined using GC-MS. The scores for odor index of rat saliva were decreased. The major constituent of volatile organic compounds (VOCs) including short-chain acids decreased 46.2% in 10 mg/ml IgY, ammonia decreased 70% in 40 mg/ml IgY, while aldehydes and olefine ketones were almost unchanged. The ELISA assay revealed that IL-6 and TNF-${\alpha}$ were decreased after 4 weeks' IgY treatment. Morphometric (X-ray) and histological analyses (HE) showed that IgY reduced alveolar bone loss and collagen fibers became orderly in rat models. As a result, IgY may have the potential to treat periodontitis and halitosis.

• Asian-Australasian Journal of Animal Sciences
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• v.17 no.8
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• pp.1139-1144
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• 2004

In Exp. 1, a total of 36 pigs (6.55$\pm$0.10 kg average initial body weight and 21 d average age) were used in a 14 d growth study to determine the effects of replacing spray-dried plasma protein (SDPP) with spray-dried egg protein containing specific egg yolk antibody (SDEP) on growth performance and nutrient digestibility in weaned pigs. The pigs were blocked by weight and assigned to treatments based on sex. There were three pigs per pen and four pens per treatment. Dietary treatments were 0, 3, or 6% SDEP and contained 6, 3, or 0% SDPP, respectively. Through the entire experimental period, average daily gain (ADG), average daily feed intake (ADFI), and gain/feed tended to decrease as the concentration of SDEP increased in the diets. However, there were no significant differences among the treatments (p>0.05). As the addition of SDEP in the diets increased, apparent digestibilities of dry matter (DM) and nitrogen (N) were decreased without significant (p>0.05). For Exp. 2, 36 pigs (2.63$\pm$0.04 kg average initial body weight and 10 d average age) were used in a 14 d growth study to determine the effects of antibiotic replacement with SDEP on growth performance and nutrient digestibility in early-weaned pigs. The pigs were blocked by weight and assigned to treatments based on sex. There were three pigs per pen and four pens per treatment. Dietary treatments included 1) ANTIBIOTIC (corn-dried whey-soybean meal based diet+0.08% antibiotics, 4 mg of tiamuline hydrogen fumarate; 10 mg of sulfadimidine per kg of complete diet), 2) SDEP0.1 (corndried whey-SBM based diet+0.1% SDEP), and 3) SDEP0.2 (corn-dried whey-SBM based diet+0.2% SDEP). ADG and gain/feed of pigs fed the SDEP0.2 diet were higher than for pigs fed the ANTIBIOTIC diet without significant (p>0.05). Pigs fed the diet with SDEP0.2 tended to have increased apparent digestibilities of DM and N compared to pigs fed the ANTIBIOTIC diet without significant (p>0.05). In conclusion, the dietary SDEP seemed to be partial replacing the SDPP portion of high nutrient dense diet for weaned pigs. Also, dietary SDEP seemed to be approximately 0.2% or more when the pigs fed the antibiotic-free diet for early-weaned pigs.

• Journal of Animal Science and Technology
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• v.46 no.3
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• pp.495-502
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• 2004

Intimin, the product of eae gene in EHEC O157:H7, is required for intimate adherence. In this study, the C-terminaI region(281 amino acids) of the EHEC OI57:H7 intimin were expressed as a protein fusion with (His)$_6$ which was used to raise antiserum in rabbits. The antiserum reacted in western blot with a 94kDa outer membrane protein of EHEC O157:H7. It was observed that the antibody titers both in egg yolk and serum appeared in 2${\sim}$4 weeks after immunization with fusion protein. At the time of 8 weeks, the titre of egg yolk was found to be higher than that of sera. According to the results of neutralization test, chicken egg-yolk antibody(lgY) against the recombinant intimin strongly reacted to EHEC O157:H7. We conclude that a truncated recombinant intimin could be used as an immunogen to elicit antibody(lgY) against O157:H7.

• 한국생물공학회:학술대회논문집
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• 2005.10a
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• pp.571-571
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• 2005

• Korean Journal of Food Science and Technology
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• v.30 no.5
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• pp.1029-1034
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• 1998

Chick antibodies (IgY) raised against Streptococcus mutans (serotype c) were separated from egg yolk and their properties were investigated. The purity of IgY extracts prepared by the method of ${\lambda}-carrageenan$, $gammaYolk^{TM}$, and $EGGstract^{TM}$ was 20%, 46%, and 48%, respectively, and the yields of IgY extracts from a gram yolk were 11. 3 mg, 1.7 mg, and 1.8mg, respectively. Quantitative immunoprecipitation test showed that specific IgY content of crude IgY prepared by ${\lambda}-carrageenan$ method was 12.2%, which means that 0.85 g of crude IgY from an egg yolk (15 g) contains about 100 mg of specific IgY. When the reactivity of the specific IgY towards 3 caries-inducing strains (serotype: b, c, f) was examined, the strains cultured in sucrose-added medium showed higher reactivity (the orders were c(+), f(+), b(+)) than those cultured in sucrose-free medium. Heat and pH stability of specific IgY was good, for crude IgY contained 50% of antibody activity after heat treatment at $70^{\circ}C$ for 5 min and they were stable at pH $4{\sim}8$.

• Food Science of Animal Resources
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• v.24 no.2
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• pp.182-188
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• 2004

To determine the concentration of Lactoperoxidase (LPO), an indirect enzyme-linked immunosorbant assay(ELISA) was developed. Anti-LPO egg yolk immunoglobulin(IgY) was transferred to egg yolk by immunizing of Brown hens with LPO. The titer of purified anti-LPO IgY was 1: 520,000. The immunological response of anti- LPO IgY with ${\alpha}$-lactalbumin, ${\beta}$-lactoglobulin, casein and lysozyme were evaluated, resulting that the anti-LPO IgY found to be a specific antibody toward LPO and no cross-reaction was observed against ${\alpha}$-lactalbumin, ${\beta}$-lactoglobulin, casein, and lysozyme in double immunodiffusion test and ELISA test. In indirect ELISA method, coating concentration of LPO and dilution rate of anti-LPO IgY was 0.25$\mu\textrm{g}$/mL and 1:8,000 respectively. Sensitivity in the standard curve of LPO was ranged from 0.01 to 1$\mu\textrm{g}$/mL using anti-LPO IgY.

• Proceedings of the Korea Society of Poultry Science Conference
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• 2003.07b
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• pp.37-54
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• 2003

It has been recognized that the hen. like its mammalian counterparts. provides young chicks with antibodies as protection against hostile invaders. This system facilitates the transfer of specific antibodies from serum to egg yolk. and provides a supply of antibodies called immunoglobulin Y(IgY) to the developing embryo and the hatched chick. The protection against pathogens that the relatively immuno-incompetent newly hatched chick has. is through transmission of antibodies from the mother via the egg. Egg yolk. therefore. can be loaded with a large amount of IgY against pathogens which can immobilize the existing or invading pathogens during the embryo development or in day-old chicks. Thus. the immunization of laying hens to various pathogens results in production of different antigen-specific IgY in eggs. Egg yolk contains 8~20 mg of immunoglobulins (IgY) per $m\ell$ or 136~340 mg per yolk suggesting that more than 30 g of IgY can be obtained from one immunized hen in a year. By immunizing laying hens with antigens and collecting IgY from egg yolk. low cost antibodies at less than ＄10 per g compared to more than ＄20.000 per g of mammalian IgG can be obtained. This IgY technology opens new potential market applications in medicine. public health veterinary medicine and food safety. A broader use of IgY technology could be applied as biological or diagnostic tool. nut-raceutical or functional food development. oral-supplementation for prophylaxis. and as pathogen-specific antimicrobial agents for infectious disease control. This paper has emphasized that when IgY-loaded chicken eggs are produced and consumed. the specific antibody binds. immobilizes and consequently reduces or inhibits the growth or colony forming abilities of microbial pathogens. This concept could serve as an alternative agent to replace the use of antibiotics. since today. more and more antibiotics are less effective in the treatment of infections. due to the emergence of drug-resistant bacteria.

• Korean Chemical Engineering Research
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• v.50 no.5
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• pp.866-873
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• 2012

IgY (Immunoglobulin Yolk) is a specific antibody in egg yolk, and it protects human body from virus and antigen. There are a lot of egg yolk components such as lipoprotein and protein. To separate IgY, HPLC (High Performance Liquid Chromatography) and precipitation were used in a batch mode and SMB (Simulated Moving Bed) was adopted for continuous purification of yolk proteins. IgY and other proteins in yolk were separated by using three-zone and four-zone SMB chromatography. Before performing SMB experiments, batch chromatography simulation parameters and adsorption isotherms were obtained. The parameters of batch chromatography were used to simulate SMB using Aspen chromatography. To compare three-zone and four-zone SMB chromatography, simulations in $m_2-m_3$ plane on the triangle theory were carried out. In terms of concentration and purity of both IgY and other lipoproteins, 3-zone SMB process is considered as ideal at the vertex of triangle ($m_2$, $m_3$=0.1, 1.1). 4-zone SMB yields the highest IgY purity at the coordinate ($m_2$, $m_3$=0.06, 0.5), which is the pure raffinate region. In 3-zone SMB without recycle, other lipoproteins in extract are largely affected in purity by small shift from the vertex of triangle ($m_2$, $m_3$=0.1, 1.1).

• Korean Journal of Poultry Science
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• v.48 no.4
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• pp.169-176
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• 2021

An experiment was conducted to investigate the effects of varying levels of hydrolyzed yeast on egg production and egg quality in aged laying randomly allotted to three dietary treatments such that egg production was similar in each treatment (6 replicates of 10 birds each). The layers were fed diets containing 0, 0.1, or 0.2% hydrolyzed yeast for eight weeks. No significant difference was observed in egg production during the first half of the experiment. Egg production and daily egg mass in groups fed diets containing hydrolyzed yeast were significantly higher (P<0.05) than those of the control groups during the second half of the experiment. Egg weight was not affected by the dietary treatment. Eggshell strength and thickness in groups fed diets containing hydrolyzed yeast were significantly higher than those of the control groups during the overall experimental period (P<0.05). Although no significant differences were observed in the Haugh units, yolk color in the group fed diets containing 0.1% hydrolyzed yeast was significantly higher than that in the control group (P<0.05). The mammillary layer thickness increased in a linear manner and significantly following treatment with dietary hydrolyzed yeast (P<0.05). Antibody titer against avian influenza virus in the group fed diets containing 0.2% hydrolyzed yeast was significantly higher (P<0.05) than that in the control group. In conclusion, dietary hydrolyzed yeast improved egg production and eggshell quality of laying hens in the late stages of production.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.25 no.5
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• pp.432-442
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• 1992

To identify the histological site of synthesis of yolk protein precursor, vitellogenin, by immunocytochemical method in the freshwater crab Eriocheir japonicus, we purified the yolk protein, vitellin, from crude egg extracts, and prepared the anti-rabbit serum against vitellin. Then, the site of vitellogenin synthesis was demonstrated by immunotytochemical method with PAP(peroxidase-antiperoxidase) reaction using the rabbit antiserum aganist vitellin. Female specific serum protein was identified in female serum by immunoelectrophoresis and Ouchterlony's immunodiffusion test for mature male and female sera. Based on the immunoelectrophoresis and Ouchterlony's diffusion test for mature male and female sera and crude egg extracts using antiserum against vitellogenic female serum absorbed with male serum, the female specific serum protein was identified as vitellogenin, detected in female serum only. The major yolk protein, vitellin, was purified from the crude egg extracts by DEAE-cellulose ion exchange chromatography, followed by sepharose CL-4B gel filteration chromatography. The molecular weight of vitellin was estimated to be about 245,000 dalton by sepharose CL-4B gel filteration chromatography. from the results of immunological analysis for vitellin, it was found that the vitellin antiserum contained the antibody against vitellogenin. In the results of immunocytochemical reaction by PAP method with the rabbit antiserum against vitellin, the vitellogenic oocytes and the hepatopancreas of mature female showed positive PAP reaction, but not in follicle cells and previtellogenic oocytes nf ovary, muscle of female and mature male hepatopancreas. Therefore, it showed that the hepatopancreas of mature female is the site of vitellogenic synthesis.