L4919
Lysozyme from chicken egg white
BioUltra, lyophilized powder, ≥98% (SDS-PAGE), ≥40,000 units/mg protein
Synonym(s):
Mucopeptide N-acetylmuramoylhydrolase, Muramidase
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About This Item
CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
235-747-3
MDL number:
EC Number:
eCl@ss:
32150313
Specific activity:
≥40,000 units/mg protein
Assay:
≥98% (SDS-PAGE)
Biological source:
chicken egg white
biological source
chicken egg white
Quality Segment
grade
Molecular Biology
product line
BioUltra
assay
≥98% (SDS-PAGE)
form
lyophilized powder
specific activity
≥40,000 units/mg protein
mol wt
single-chain 14.3 kDa
composition
Protein, ≥90%
technique(s)
cell based assay: suitable
input
bacteria and yeast sample(s)
optimum pH
6.2
suitability
suitable for cell lysis
application(s)
cell analysis
storage temp.
−20°C
General description
Lysozyme is abundantly found in animal and plant kingdoms. It is a natural food preservative and also found to be present in specific bacterial cell walls. Lysozyme is usually present in tears, milk, urine and saliva.
Substrate Specificity
Hydrolysis of (1→4)-β-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins
Hydrolysis of (1→4)-β-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins
Application
Lysozyme from chicken egg white has been used:
- in dielectric spectroscopy studies of dynamics of protein
- as a control to measure the human lysozyme activity
- as a supplement in soaking solution to treat lenses
Enzyme breaks down the cell walls of bacteria; used to prepare spheroplasts.
Biochem/physiol Actions
Lysozymes participate in the defense mechanism. It has the ability to stimulate catalysis by bringing steric stress in the substrates.
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).
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).
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.
Features and Benefits
- Highly purified by repeated crystallization and dialysis
- Each lot is use-tested for isolation of plasmid DNA from E. coli
Preparation Note
3× crystallized
Other Notes
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.
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Signal Word
Danger
Hazard Codes
Precautionary Statements
Hazard Classifications
Resp. Sens. 1
Storage Class
11 - Combustible Solids
WGK
WGK 3
Flash Point (°F)
Not applicable
Flash Point (°C)
Not applicable
PPE (personal protective equipment)
Eyeshields, Gloves, type N95 (US)
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