Characterization of the lysozyme of Mytilus edulis (L)

1. Lysozyme isolated from the crystalline style of Mytilus edulis is a true N-acetylmuramyl-hydrolase (E.C. 3.2.1.17). 2. THe enzyme is optimally active at approx pH 7.1, I = 0.011, with a secondary optimum at pH 4.6, I = 0.054. 3. Cell walls of Micrococcus luteus, Escherichia coli, and Bacillus subtilis were degraded by the lysozyme but chitin or cell walls of Staphylococcus aureus were resistant to its activity. 4. Tetra-N-acetyl chitotetraose inhibited enzyme activity more than N-acetylglucosamine, di-N-acetyl chitobiose, tri-N-acetyl chitotriose or penta-N-acetyl chitopentaose.