Soluble in 10 mg/ml,(water 1.5% solution.), Clear to slightly hazy solution.

One unit will cause a decrease in OD450 of 0.001 per minute at pH 6.24 and 25 °C using Micrococcus lysodeikticus as substrate.

Chloride <3.5%; Inhibitors: The enzyme is inhibited by surface-active reagents such as dodecyl sulfate, alcohols and fatty acids. Imidazole and indole derivatives are inhibitors via formation of change-transfer complexes. Stability: Solutions at pH 4 to 5 are stable for several weeks refrigerated and for days at ambient temperatures.

Lysozyme has been used for lysing E. coli and Streptomycetes for extraction purposes such as extracting group specific antigen. It would appear that lysozyme may act as a germinative agent of bacterial spores. The enzyme is often used for lysing bacterial cells by hydrolyzing the peptidoglycan present in the cell walls. Used to prepare spheroplasts.

Lysozyme hydrolyzes β(1→4) linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrin. Gram-positive cells are quite susceptible to this hydrolysis as their cell walls have a high proportion of peptidoglycan. Gram-negative bacteria are less susceptible due to the presence of an outer membrane and a lower proportion of peptidoglycan. However, these cells may be hydrolyzed in the presence of EDTA that chelates metal ions in the outer bacterial membrane.