Lysozyme, also known as muramidase, is a bacteriolytic enzyme found in phagocytic cells like leukocytes. The name "lysozyme" is derived from its ability to dissolve or hydrolyze the β-1-4-glycosidic bond between N-acetylglucosamine (NAG) and N-acetylmuramic acid (NAM) in the walls of certain bacteria. This protein is present in animals, plants, bacteria, and viruses. It can also be found in granules of neutrophils, macrophages, as well as in serum, saliva, milk, honey, and hen egg white. There are different types of lysozymes, including the c-type (chicken type), the g-type (goose-type), and the i-type (invertebrates).

Lysozyme chloride form from chicken egg white has been used:

• as a component in the protein mixture to study the effects of yeast cells on membrane fouling caused by a protein mixture in dead-end filtration
• in dip system to study its bacteriostatic or bactericidal effects on Salmonella-contaminated broiler parts
• in viscometric assay for determining lysozyme activity    

Lysozyme serves as an indicator of macrophage-mediated host response, correlates with white cell death, and exhibits a high turnover rate. Elevated levels of serum lysozyme have been observed in various chronic inflammatory conditions, inflammatory bowel diseases, hematological disorders, and renal disorders. The c-type lysozyme from hen egg white is commonly used as a model for studying protein structure and function. Muramidase primarily exhibits bactericidal activity against Gram-positive bacteria.

One unit will lyse 0.6 μg of Micrococcus lysodeikticus per minute by turbidimetric detection at 600 nm when suspended in buffer at pH 6.2 at 25 °C.

Lyophilized powder containing sodium chloride and sodium acetate

3× Crystallized