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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

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About This Item

CAS Number:
12650-88-3
Enzyme Commission number:
3.2.1.17 (BRENDA, IUBMB)
EC Number:
235-747-3
MDL number:
MFCD00131557
UNSPSC Code:
12352204
NACRES:
NA.54

biological source

chicken egg white

Quality Level

200

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

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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 produce a ΔA450 of 0.001 per min at pH 6.24 at 25°C, using a suspension of Micrococcus lysodeikticus as substrate, in a 2.6 mL reaction mixture (1 cm light path).

Preparation Note

3× crystallized

pictograms

Health hazard
GHS08

signalword

Danger

hcodes

H334

Hazard Classifications

Resp. Sens. 1

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’.

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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
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HPLC Analysis of Proteins on Proteomix® SCX-NP5

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

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Protocols

Enzymatic Assay of Lysozyme (EC 3.2.1.17)

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

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