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Co-purification of chicken egg white proteins using polyethylene glycol precipitation and anion-exchange chromatography

机译：聚乙二醇沉淀和阴离子交换色谱法共纯化鸡蛋白

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摘要

Obtaining several proteins from chicken egg whites from a single extraction in a continuous process is imperative because there are potential applications for egg white proteins in the pharmaceutical and food industries. In this study, chicken egg whites were divided into four components using polyethylene glycol precipitation. All precipitates, except for ovomucin (Precipitate A), were further purified through Q Sepharose Fast Flow anion-exchange chromatography. Lysozyme, ovotransferrin, ovalbumin and ovofl-avoprotein were purified from Precipitate B, Precipitate C and Supernatant D, respectively, which were determined to be 91.84%, 94.55%, 96.45% and 88.16% pure, respectively, by HPLC. The results showed that this method is feasible for the co-purification of major egg white proteins with high purity. This method is scientifically practical and easy to use and thus will suitable for industrial-scale production.
机译：必须从连续的过程中一次提取蛋清中获得几种蛋白质，因为蛋清蛋白在制药和食品工业中有潜在的应用。在这项研究中，使用聚乙二醇沉淀将鸡蛋白分为四个成分。除卵粘蛋白（沉淀物A）外，所有沉淀物均通过Q Sepharose Fast Flow阴离子交换色谱法进一步纯化。溶菌酶，卵转铁蛋白，卵清蛋白和卵磷脂-av蛋白分别从沉淀物B，沉淀物C和上清液D中纯化，通过HPLC测定纯度分别为91.84％，94.55％，96.45％和88.16％。结果表明，该方法对于高纯度主要蛋清蛋白的共纯化是可行的。该方法在科学上实用且易于使用，因此适用于工业规模的生产。

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