Preliminary study on the separation of lysozyme, ovotransferrin and ovalbumin from egg white

Separation processing of lysozyme, ovotransferrin and ovalbumin from egg white proteins was studied. The proteins were separated by ammonium sulfates and anion-exchange chromatography. Purity of the proteins was assayed by sodium dodecyl sulfatepolyacrylamide gel electrophoresis (SDS-PAGE). The results showed that the proteins were electrophoresis-pure. The specific activity of lysozyme was increased from 144.13 U/mg to 2 235 U/mg, and purification factor was 15-fold. Lysozyme recoveries were estimated to be 15.76%. Antibacterial probability of ovotransferrin was 48.84%. The procedure for separation lysozyme, ovotransferrin and ovalbumin from egg white was simple, fast, low-cost and suitable for industry.