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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

CAS Number:
12650-88-3
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
235-747-3
MDL number:
MFCD00131557
EC Number:
3.2.1.17 (BRENDA, IUBMB)
Specific activity:
~100000 U/mg
Biological source:
chicken egg white
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biological source

chicken egg white

Quality Level

100

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.

P00698

application(s)

cell analysis

storage temp.

2-8°C

Gene Information

chicken ... LYZ(396218)

Application

Enzyme breaks down the cell walls of bacteria; used to prepare spheroplasts.
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

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).
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.

Other Notes

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)
Suitable for the hydrolysis of bacterial cell walls, mucopolysaccharides, mucopolypeptides or chitin; degradability of L. lactis subsp. cremoris H2 cell walls.

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pictograms

Health hazard
GHS08

signalword

Danger

hcodes

H334

Hazard Classifications

Resp. Sens. 1

Storage Class

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

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Articles

HPLC Analysis of Proteins by Cation Exchange on Proteomix® WCX-NP5: Affect of pH

Separation of Ribonuclease A from bovine pancreas, Type I-A, powder, ≥60% RNase A basis (SDS-PAGE), ≥50 Kunitz units/mg protein; α-Chymotrypsinogen A from bovine pancreas, essentially salt-free, lyophilized powder; Cytochrome c from bovine heart, ≥95% based on Mol. Wt. 12,327 basis; Lysozyme from chicken egg white, lyophilized powder, protein ≥90 %, ≥40,000 units/mg protein

HPLC Analysis of Proteins by Cation Exchange on Proteomix® WCX: Affect of Particle Size

Separation of Ribonuclease A from bovine pancreas, Type I-A, powder, ≥60% RNase A basis (SDS-PAGE), ≥50 Kunitz units/mg protein; α-Chymotrypsinogen A from bovine pancreas, essentially salt-free, lyophilized powder; Cytochrome c from bovine heart, ≥95% based on Mol. Wt. 12,327 basis; Lysozyme from chicken egg white, lyophilized powder, protein ≥90 %, ≥40,000 units/mg protein

POTRA Domains, Extracellular Lid, and Membrane Composition Modulate the Conformational Stability of the beta Barrel Assembly Factor BamA
Thoma J, et al.
Structure, 26(7), 987-996 (2018)
Use of Protein Thin Film Organized by External Electric Field as a Template for Protein Crystallization
Walter TK, et al.
ACS Omega, 3(8), 8683-8690 (2018)
P Jollès et al.
Molecular and cellular biochemistry, 63(2), 165-189 (1984-09-01)
The present review is focused on the main achievements realized in the lysozyme research field since the meeting held in 1972 to commemorate the fiftieth anniversary of the discovery of this enzyme. Despite of extensive structural, physico-chemical, crystallographic, genetic, immunological
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Global Trade Item Number

SKUGTIN
62970-1G-F04061832713823
62970-5G-F04061835570621