Characterization of Lysozyme from Brown Eared Pheasant Egg White

Abstract

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.