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.
D000818:Animals; D049872:Bivalvia / Q000201:enzymology*; D002241:Carbohydrates / Q000494:pharmacology; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D009113:Muramidase / Q000378:metabolism*; D009994:Osmolar Concentration; D010457:Peptidoglycan; D012623:Seawater; D013379:Substrate Specificity
D002241:Carbohydrates; D010457:Peptidoglycan; D009113:Muramidase