Effect of different concentrations of calcium chloride and potassium chloride on egg white proteins during isoelectric precipitation of ovomucin.

The effect of various concentrations of CaCl2 and KCl on egg white proteins during isoelectric precipitation of ovomucin was investigated in this study. At low concentrations of CaCl2 (<50 mM), lysozyme was the major contaminant in the precipitated ovomucin, whereas ovalbumin was the predominant one at high concentrations (>or=100 mM). At 50 mM CaCl2 concentration, the concentrations of both lysozyme and ovalbumin were moderate. Ovomucin with a purity of 97.3% was prepared using a 2-step method: egg white was first precipitated in the presence of 50 mM CaCl2 followed by a second 500 mM CaCl2 extraction. The concentrations of other proteins in the precipitate were 1.3% of ovalbumin, 1.1% of lysozyme, and 0.4% of ovomucoid. Unlike CaCl2-treated samples, ovotransferrin was found to be the second major contaminant in all KCl-treated precipitates. Compared with the control, adding KCl at the lowest concentration of 2.5 mM increased significantly the content of ovalbumin (from 7.6 to 68.0%) and reduced significantly the content of lysozyme (from 25.5 to 6.4%) in the precipitates; however, increasing the concentrations of KCl up to 500 mM did not affect the content of ovalbumin, but the content of lysozyme showed a general reduction trend. Although KCl was used widely in literature as the last step of ovomucin washing, our results show that KCl is not an efficient salt in purifying ovomucin.