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Merck

62970

Lysozyme from chicken egg white

dialyzed, lyophilized, powder, ~100000 U/mg

Synonym(s):

Mucopeptide N-acetylmuramoylhydrolase, Muramidase

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1 G

682,00 kr

5 G

2 390,00 kr

682,00 kr


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About This Item

CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
235-747-3
MDL number:
EC Number:

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Product Name

Lysozyme from chicken egg white, dialyzed, lyophilized, powder, ~100000 U/mg

biological source

chicken egg white

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

Quality Level

Gene Information

chicken ... LYZ(396218)

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This Item
L37904403-ML7773
technique(s)

cell based assay: suitable

technique(s)

cell based assay: suitable

technique(s)

cell based assay: suitable

technique(s)

-

biological source

chicken egg white

biological source

chicken egg white

biological source

chicken egg white

biological source

-

specific activity

~100000 U/mg

specific activity

-

specific activity

≥20,000 Shugar units/mg dry wt

specific activity

-

Gene Information

chicken ... LYZ(396218)

Gene Information

chicken ... LYZ(396218)

Gene Information

-

Gene Information

chicken ... LYZ(396218)

suitability

suitable for cell lysis

suitability

suitable for cell lysis

suitability

suitable for cell lysis

suitability

-

application(s)

cell analysis

application(s)

cell analysis

application(s)

cell analysis

application(s)

-

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 [1] and infrared absorbance spectroscopy[2]
  • as a constituent of cell lysis buffer[3]
  • in protein crystallization experiments[4]

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.

pictograms

Health hazard

signalword

Danger

hcodes

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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R.W. Franck
Bioorganic Chemistry, 20, 77-77 (1992)
T Coolbear et al.
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
Infrared absorbance spectroscopy of aqueous proteins: Comparison of transmission and ATR data collection and analysis for secondary structure fitting
Corujo MP, et al.
Chirality, 30(8), 957-965 (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
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)

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