62970
Lysozyme from chicken egg white
dialyzed, lyophilized, powder, ~100000 U/mg
Synonym(s):
Mucopeptide N-acetylmuramoylhydrolase, Muramidase
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About This Item
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biological source
chicken egg white
Quality Level
form
powder
quality
dialyzed
lyophilized
specific activity
~100000 U/mg
mol wt
single-chain 14.3 kDa
Mr ~14600
technique(s)
cell based assay: suitable
suitability
suitable for cell lysis
UniProt accession no.
application(s)
cell analysis
storage temp.
2-8°C
Gene Information
chicken ... LYZ(396218)
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Application
Lysozyme from chicken egg white has been used:
- as a standard in small-angle neutron scattering experiments and infrared absorbance spectroscopy
- as a constituent of cell lysis buffer
- in protein crystallization experiments
Enzyme breaks down the cell walls of bacteria; used to prepare spheroplasts.
Biochem/physiol Actions
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).
Unit Definition
1 U corresponds to the amount of enzyme which decreases the absorbance at 450 nm by 0.001 per minute at pH 7.0 and 25°C (Micrococcus luteus, ATCC 4698, as substrate)
Other Notes
Suitable for the hydrolysis of bacterial cell walls, mucopolysaccharides, mucopolypeptides or chitin; degradability of L. lactis subsp. cremoris H2 cell walls; Review
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Resp. Sens. 1
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
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Structures and interactions among lysozyme proteins below the isoelectric point in presence of divalent ions
Chemical Physics Letters, 711, 8-14 (2018)
Comp. Biochem. Physiol., B: Comp. Biochem., 100, 1-1 (1991)
Use of Protein Thin Film Organized by External Electric Field as a Template for Protein Crystallization
ACS Omega, 3(8), 8683-8690 (2018)
POTRA Domains, Extracellular Lid, and Membrane Composition Modulate the Conformational Stability of the beta Barrel Assembly Factor BamA
Structure, 26(7), 987-996 (2018)
Applied and environmental microbiology, 58(10), 3263-3270 (1992-10-01)
The cell wall-associated proteinase from Lactococcus lactis subsp. cremoris H2 (isolate number 4409) was released from the cells by treatment with lysozyme, even in the presence of 50 mM calcium chloride. Cell lysis during lysozyme treatment was minimal. The proteinase
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