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.
- Extracts group specific antigens
- Germinative agent of bacterial spores
- In humans, may be the mediator in the anti-tumor function of macrophages
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).
Specific Activity: ≥20,000 u/mg solid
Key Applications: Cell Lysis
Product Type: Proteins, Enzymes & Peptides
Biochemical Category: Proteins, Enzymes & Peptides
Extinction Coefficient (E1%): 26.4 (280 nm) (Lit.)
Presentation: White powder
Format: 3X Crystallized, Salt-Free, Albumin-Free, Lyophilized
Isoelectric point (pI): pH 11.0 (lit)
pH: 9.2 (optimum)
NOTES: Chloride ≤3.5%
Storage & Handling: -20°C