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

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.

► PEG precipitation was effective and suitable for the separation of EW proteins.
► Five proteins were co-purified from chicken egg white.
► Proteins were purified with high purity and satisfying recovery yield.
► This method should be adequate for larger scale.