L7773

Sigma

 

Lysozyme from chicken egg white

aseptically filled

Synonym:Mucopeptide N-acetylmuramoylhydrolase, Muramidase
CAS Number:12650-88-3
Enzyme Commission (EC) Number:3.2.1.17   ( BRENDA | IUBMB )
EC Number:235-747-3
MDL number:MFCD00131557

Description

ApplicationEnzyme breaks down the cell walls of bacteria; used to prepare spheroplasts.
Other NotesView more information on enzymes for complex carbohydrate analysis at www.sigma-aldrich.com/enzymeexplorer
Preparation NotePrepared from L6876
Unit DefinitionOne unit will produce a ΔA450 of 0.001 per min at pH 6.24 at 25 °C, using a suspension of Micrococcus lysodeikticus as substrate, in a 2.6 mL reaction mixture (1 cm light path).
Biochem/physiol ActionsLysozyme 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).

Properties

sterilityaseptically filled
mol wtsingle-chain mol wt 14.3 kDa
storage temp.−20°C

Safety

Personal Protective EquipmentEyeshields, Gloves, type N95 (US), type P1 (EN143) respirator filter
Safety Statements22-24/25
WGK Germany3
RTECSOL5989000

Related Products

SubstrateN8638, 4-Nitrophenyl β-D-N,N′,N′′-triacetylchitotriose
 M5639, 4-Methylumbelliferyl β-D-N,N′,N′′-triacetylchitotrioside

References

referenceJolles, P. Angew. Chem. Int. Ed. Engl. 8, 227-239, (1969)
 Rupley, J.A. Biochim. Biophys. Acta 83, 245-255, (1964)
 Holler, H., et al. Biochemistry 14, 2377-2385, (1975)
 Canfield, R.E. J. Biol. Chem. 238, 2698-2707, (1963)
 Davies, R.C., et al. Biochim. Biophys. Acta 178, 294-305, (1969)