Skip to Content
MilliporeSigma
All Photos(5)

Documents

L4919

Sigma-Aldrich

Lysozyme from chicken egg white

BioUltra, lyophilized powder, ≥98% (SDS-PAGE), ≥40,000 units/mg protein

Synonym(s):

Mucopeptide N-acetylmuramoylhydrolase, Muramidase

Sign Into View Organizational & Contract Pricing


About This Item

CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

biological source

chicken egg white

grade

for 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

suitability

suitable for cell lysis

application(s)

cell analysis

storage temp.

−20°C

Looking for similar products? Visit Product Comparison Guide

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.

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

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).
Lysozymes participate in the defense mechanism. It has the ability to stimulate catalysis by bringing steric stress in the substrates.

Features and Benefits

  • Highly purified by repeated crystallization and dialysis
  • Each lot is use-tested for isolation of plasmid DNA from E. coli

Unit Definition

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.

Preparation Note

3× crystallized

pictograms

Health hazard

signalword

Danger

hcodes

Hazard Classifications

Resp. Sens. 1

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

Protein dynamics in a broad frequency range: Dielectric spectroscopy studies
Nakanishi M and Sokolov AP
Journal of Non-Crystalline Solids, 407, 478-485 (2015)
Natural Food Antimicrobial Systems (2000)
Metabolic engineering of probiotic Saccharomyces boulardii
Liu JJ, et al.
Applied and Environmental Microbiology, 82(8), 2280-2287 (2016)
Corneal cell adhesion to contact lens hydrogel materials enhanced via tear film protein deposition
Elkins CM, et al.
Testing, e105512-e105512 (2014)
Jordi van Gestel et al.
Nature ecology & evolution, 3(8), 1184-1196 (2019-07-25)
Microbes are exposed to changing environments, to which they can respond by adopting various lifestyles such as swimming, colony formation or dormancy. These lifestyles are often studied in isolation, thereby giving a fragmented view of the life cycle as a

Articles

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

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

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

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

See All

Protocols

This enzymatic rate determination may be used for Lysozyme products. It is not to be used to assay recombinant or insoluble Lysozyme on agarose.

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service