共查询到19条相似文献,搜索用时 62 毫秒
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对鸡卵黄免疫球蛋白(IgY)的分离纯化进行了研究.工艺流程为:卵黄→8倍水稀释并搅拌10 min→用HCl调Ph至5.2后在4 ℃静置2 h去沉淀→在上清夜中加入95 %冰乙醇(-20 ℃)使终浓度为60 %(v/v)→4 ℃搅拌20 min后离心(22000 r/min,4 ℃,25 min)→收集沉淀并加入0.028 mol/L NaCl溶液在4 ℃下过滤除去脂蛋白沉淀→收集的滤液用SDS-PAGE法进行纯化得纯度为98 %的1gY.用大肠杆菌(E.coli)对其活性进行测定,效果良好,此方法能保持免疫球蛋白的活性. 相似文献
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对鸡卵黄抗体(简称IgY)的制备工艺进行研究。通过低温乙醇沉淀、DEAE葡萄糖凝胶A-50离子交换层析、Tris-HCl缓冲液洗脱及Sephadex G200凝胶过滤等逐步纯化免疫球蛋白。研究卵黄稀释倍数、pH值、乙醇添加量以及盐浓度对纯化效果的影响。分离纯化后所得的提取物经检测IgY纯度可达98%。用大肠杆菌(E.coli)对其活性进行测定,效果良好,此方法能很好保持免疫球蛋白的活性。 相似文献
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采用冰乙醇分级离心法提取鸡卵黄免疫球蛋白 (Immunoglobulin of egg yolk,IgY).通过低温乙醇沉淀、DEAE 葡萄糖凝胶 A-50 离子交换层析、Tris-HCl 缓冲液洗脱及 Sephadex G200 凝胶过滤等逐步纯化免疫球蛋白.研究卵黄稀释倍数、pH 值、乙醇添加量以及盐浓度对纯化效果的影响.分离纯化后所得的提取物经检测 IgY 纯度可达98%,且很好地保持了免疫球蛋白的活性. 相似文献
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水稀释法分离鸡卵黄免疫球蛋白的研究 总被引:5,自引:2,他引:3
本研究详细探讨了水稀释法分离鸡卵黄免疫球蛋白(Immunoglobulin of Yolk:IgY)的主要工艺条件,当蛋黄液的稀释倍数为6、pH5.2时,IgY的提取率和纯度分别是6.73mg IgY/ml蛋黄、14.66%。比较了水稀释法和聚乙二醇法分离IgY的效果。结果表明,水稀释法更适合于大规模分离食品级IgY。 相似文献
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本文比较了分离纯化鸡卵黄免疫球蛋白(IgY)的四种方法(即水稀释法,聚乙二醇法,葡聚糖硫酸盐法和黄原胶法)。包括IgY产量,纯度,活性,简便性及扩大生产规模的潜力。试验表明:水稀释法(DS)产量最高,然后依次为葡聚糖硫酸盐法(DS),黄原胶法(Xan),聚乙二醇法(PEG);同时发现水稀释法简便、快速、高效,适用于工业化生产。 相似文献
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一种新型的食品添加剂——鸡卵黄免疫球蛋白 总被引:7,自引:0,他引:7
当用某种抗原免疫产蛋母鸡时,鸡可产生相应的多克隆抗体─—免疫球蛋白,并被运送和储存于鸡卵的卵黄中,此种免疫球蛋白称为IgY(ImmumoglobulinofYolk)。一只母鸡一经免疫应答后,即可从其不断生产的鸡卵的卵黄中获得大量的、均一的、高效价的IgY,而且lgY有许多独到的优点,具有许多潜在的应用价值,可代替由免疫小鼠、兔等哺乳动物制备的抗体。因而近年来,国外对IgY的研究应用十分活跃,特别是将IgY作为食品的免疫型强化剂的应用研究正在不断开展,前景非常广阔。一、IgY的特点:1.IgY类似于哺乳动物的igY.分子量为180lH>,… 相似文献
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以远缘链球菌(S.sorbrinus 6715血清型g)免疫产卵母鸡,应用酶联免疫吸附测定法(ELISA)测定鸡卵黄中免疫球蛋白(Immunoglobulin of Yolk,IgY)的活性,研究鸡免疫应答并制备出高免抗-S.sorbrinus IgY.结果显示以109 cfu/只剂量免疫的母鸡,第一次免疫后的第七天卵黄中出现特异性IgY,加强免设后抗体效价上升更快,经ELISA法检测,卵黄中的抗体效价到1384.而冷冻干燥后的IgY,其效价要超过12000. 相似文献
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TOSHIO HORIKOSHI JUNICHIRO HIRAOKA MARIKO SAITO SHIGEYUKI HAMADA 《Journal of food science》1993,58(4):739-742
A procedure was developed for large-scale preparation of IgG antibodies from egg yolks. The supernatant from egg yolks was obtained after an initial 9–fold dilution with water. The lipids in the supernatant were then almost completely eliminated from the water-soluble protein fraction containing the antibody, by precipitation with 60% ethanol and filtration. Yolk antibody was purified from the lipid-free water-soluble protein fraction by ethanol fractionation at final concentration 30% (pH unadjusted), and again at 25% (pH 7.4). The purified fraction was composed of >99% pure IgG. Recovery of antibody was calculated as 40%. 相似文献
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鸡蛋清中溶菌酶的应用性研究 总被引:12,自引:0,他引:12
介绍了鸡蛋清中溶菌酶的生物化学特性,研究了它在食品、医学、生物工程、日化用品等工业上的应用性,提出其潜在的应用价值和发展前景。 相似文献
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A water-soluble fraction (WSF) was prepared by filtering 10 times diluted yolk (pH 5.0) stored at 4–6°C through Whatman No. 52 or No.1 filter paper for delipidation. However, solid-phase delipidation using an octadecyl column after filtration through a cellulose powder column was more practical for industrial application. After ultrafiltration (UF) of the WSF (pH 9.0,1.5M NaCl), results showed: Amicon 80–85% recovery, 74–99% purity; Harp 72–74% recovery, 81–84% purity; A/G 75% recovery, 89% purity; Koch 88% purity. 相似文献
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Nassim Naderi James D. House Yves Pouliot Alain Doyen 《Comprehensive Reviews in Food Science and Food Safety》2017,16(4):707-720
High hydrostatic pressure (HHP), used alone or with other processes, is an emerging technology increasingly used in the food industry to improve microbial safety, and the functionality and bioactive properties of food products. HHP provides a way to reduce energy requirements for food processing and may contribute to improved energy efficiency in the food industry. Hen egg is used by the food industry to formulate many food products. To improve the microbiological safety of egg and egg‐derived products, HHP processing is an attractive alternative to heat‐ pasteurization and a potential technology. However, HHP treatment induces structural modifications of egg components (such as proteins) which could positively or negatively affect the physicochemical and functional properties of egg‐derived products. Improving our knowledge regarding the potential of HHP in the egg industry will add value to the final food products and increase profitability for egg producers and the food industry. 相似文献
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ABSTRACT: The aim of this study was to evaluate the ability of unfractionated hen egg yolk to prevent the attachment of Salmonella typhimurium to murine intestinal epithelial cells in vitro. Inhibition of adherence was examined microscopically and by an ELISA. Both methods showed that egg yolk from immunized and unimmunized hens significantly reduced bacterial adherence. Optical density (OD) readings ± SD of 0.825 ± 0.016 for untreated bacteria were reduced to 0.335 ± 0.024 and 0.267 ± 0.021 for bacteria pretreated with egg yolk from immunized hens and unimmunized hens, respectively. Microscopic analysis showed that egg yolk from either immunized or unimmunized hens reduced bacterial adherence from 17 ± 2.7 bacteria per epithelial cell to less than 4 bacteria per epithelial cell. These results show that hen egg yolk significantly inhibits adherence of S. typhimurium to intestinal epithelial cells in vitro. Boosting of specific antibody levels does not enhance this antiadhesive effect, suggesting that egg yolk contains novel antiadhesive factors. 相似文献
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A serial filtration system was developed for separating immunoglobulin from egg yolk (IgY). Egg yolk was diluted 10 times with water, adjusted to pH 5.0, frozen, then thawed. The diluted yolk was diafiltered through a hard filter paper at 4-6°C to produce a clear water-soluble fraction (WSF). The WSF was then delipidated by filtering through a hydrophobic membrane filter. Ultrafiltration of delipidated WSF at pH 9.0, at 4-6°C, in the presence of 1.5M NaCl resulted in electrophoretically pure (>90%) IgY with a recovery of about 92%. Advantages of this method are the use of only a few mild chemicals and the potential of developing a continuous process. 相似文献
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High-purity immunoglobulins (Ig), which may be useful for immunologic supplementation of food products, were isolated from Cheddar cheese whey in a one-step process using avidin-biotinylated yolk immunoglobulin (IgY) column chromatography. Yolk antibodies specific to bovine IgG (IgYIgG ) were biotinylated with biotinyl amido-hexanoic acid-N-hydroxy-sulfo-succinimide ester without any notable effect on antigen-binding activity, and coupled to immobilized avidin columns. The resulting avidin-biotinylated IgYIgG columns, with binding capacity of 50–55% (w/w percent ratio of IgG to immobilized IgYIgG ), were used for specific binding of IgG from cheese whey. Elution with a commercially available eluent (Actisep) or 0.1 M glycine-HCl buffer at pH 2.8 yielded IgG with purity of 99% by radial immunodiffusion. 相似文献