Lysozyme (muramidase) hydrolyzes preferentially the β-1,4 glucosidic linkages between N-acetylmuramic acid and N-acetylglucosamine which occur in the mucopeptide cell wall structure of certain microorganisms, such as Micrococcus lysodeikticus.

• Presentation: White Powder
• Extinction Coefficient (E1%): 26.4 (280 nm) (Lit.)
• 3X Crystallized, Salt-Free, Albumin-Free, Lyophilized
• Isoelectric point (pl): pH 11.0 (lit)
• pH: 9.2 (optimum)

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. In humans, lysozyme may be the mediator in the anti-tumor function of macrophages which, it has been shown, secrete the enzyme. There is evidence that cartilage lysozyme has a role in cartilage calcification. Enzyme breaks down the cell walls of bacteria; 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. The enzyme is active over a broad pH range (6.0 to 9.0). At pH 6.2, maximal activity is observed over a wider range of ionic strengths (0.02 to 0.100 M) than at pH 9.2 (0.01 to 0.06 M).