Lysozyme was purified from brown eared pheasant ( Crossoptilon mantchuricum ) egg white using pH treatment and cation exchange chromatography resulting in an 80-fold enhancement of the specific activity. The enzyme exhibited hydrolytic activity toward glycol chitin and chitooligosaccharides [(GlcNAc) _n ( n =5 and 6)]. The enzyme catalyzed degradation of bacterial cells of not only Micrococcus luteus but also Salmonella enterica serovar Typhimurium and Escherichia coli O157:H7 upon treatment with chloroform/tris(hydroxymethyl)aminomethane-HCl. The pH optimum of the glycol chitin hydrolytic reaction was 5.5 at 37°C. The optimal temperature for activity was 53°C in 50 mM sodium acetate buffer (pH 5.5). The enzyme mainly hydrolyzed the fourth glycosidic linkage from the nonreducing end of (GlcNAc)₆. The anomeric form of the products indicated it was a retaining enzyme.