Chemical studies on the enzymatic specificity of goose egg white lysozyme.

In comparison with hen egg white lysozyme, goose lysozyme is known to be aberrant in both its structure and its enzymatic behavior in the presence of polymers of N-acetylglucosamine or cell suspensions of Micrococcus luteus. Our chemical studies show, however, that like the hen enzyme, goose lysozyme has muramidase activity. At several pH levels ranging from 3.5 to 7.1 the goose enzyme liberated the reducing ends of N-acetyhnuramic acid residues in purified preparations of Escherichia coli and M. Zuteus peptidoglycans. In contrast to what is known about hen lysozyme, however, our results suggest that the goose enzyme has a distinct preference for N-acetyhnuramic acid residues which are substituted with a peptide moiety. This difierence in specificity towards the peptide portion of the peptidoglycan may be related to the biological function of lysozyme.