Studies on the lysozyme isolation by ion-exchange chromatography

Various ion-exchange column chromatography for efficient isolation of lysozyme from egg white were investigated. Homogenized egg white adsorbed through the resin and eluted with 0.5 % NaCl. Eluate was precipitated at isoelectric point (pH 9.5) and then dried at 90deg C and freeze dryer. CM Sephadex C-25 was highly efficient in adsorbing lysozyme from egg white. But it has some drawbacks due to volumn change and resin clogging by egg white compared with Duolite C-464. Densitometric peaks on the SDS-PAGE showed high purity of isolated lysozyme using CM Sephadex C-25. The process for lysozyme isolation achieved 95 % recovery at Duolite C-464 and 36,000 units/mg activity at CM Sephadex C-25, respectively