[Separation and purification of lysozyme from egg white by high performance cation-exchange chromatography].
A new method used to separate and purify lysozyme from egg white by high performance cation-exchange chromatography has been established. The process conditions for purifying lysozyme were also discussed in detail. The procedure involved that homogenization of the egg white sample, preliminary purification with sodium chloride, and chromatographic separation by the weak cation exchange column (XIDACE-WCX). The experimental results showed that the purified lysozyme and other impurity proteins were completely separated. By using bioactivity assay, the recovery of lysozyme was 107%, and the specific activity was 15,467 U/mg through the column. Its purity was raised 5.6-fold. The collected fraction with activity was detected by size-exclusion chromatography (SEC). The purified lysozyme was homogeneous. Compared with the traditional soft-based low pressure ion-exchange chromatography, the developed method is rapid and effective.
Li
Rong
R
Department of Chemical Engineering, Northwest University, Xi'an 710069, China.
Chen
Guo-liang
GL
D002412:Cations; D002852:Chromatography, Ion Exchange / Q000379:methods*; D004529:Egg White / Q000032:analysis*; D009113:Muramidase / Q000302:isolation & purification*; D012680:Sensitivity and Specificity
D002412:Cations; D009113:Muramidase