Abstract
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 ovoflavoprotein 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.
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