Sourced from Egg Whites, Lysozyme preferentially hydrolyzes the β-1,4 glycosidic linkages between N-acetylmuramic acid and N-acetylglucosamine which occur in the mucopeptide cell wall structure of certain microorganisms, such as Micrococcus lysodeikticus. It has a molecular weight of 14,388 daltons. Optimum pH is 9.2. Lysozyme is inhibited by surface active agents such as dodecyl sulfate, alcohol and fatty acids. Imidazole and indole derivatives form inhibitory charged transfer complexes.