Introduction & Objective: Egg white contains four high-quantity proteins which have numerous applications. In this research, a simple and efficient method for the purification of those proteins was designed and performed based on ion exchange chromatography.

Materials & Methods: In this experimental study egg white was initially separated from insoluble substances by acidic pH. The resulting extract was isolated after two steps of ion exchange chromatography using CM-Sepharose and DEAE-Sepharose columns, respectively. Purification degree and yield of each fraction were analyzed by electrophoresis densitometry.

Results: The results showed that purification degrees of ovalbumin, ovotransferrin, ovomucoid and lysozyme were 97, 98, 85 and 99 percent and their yields were 98, 98 95 and 99 percent, respectively.

Conclusion: High yields, reproducibility and feasibility on low or high scales are considered as the strengths of this method.