L4919

Lysozyme from chicken egg white

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

• Synonym(s): Mucopeptide N-acetylmuramoylhydrolase, Muramidase
• 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)

Properties

• Product Name: Lysozyme from chicken egg white, BioUltra, lyophilized powder, ≥98% (SDS-PAGE), ≥40,000 units/mg protein
• biological source: chicken egg white
• grade: 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
• Quality Level: 200

Description

Application

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

Lysozyme from chicken egg white has been used:

• in dielectric spectroscopy studies of dynamics of protein[1]
• as a control to measure the human lysozyme activity[2]
• as a supplement in soaking solution to treat lenses[3]

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.

Lysozymes participate in the defense mechanism. It has the ability to stimulate catalysis by bringing steric stress in the substrates.[4]

Features and Benefits

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

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.[4]

Other Notes

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

Safety Information

• pictograms: GHS08
• signalword: Danger
• hcodes: H334
• pcodes: P261 - P284 - P501
• 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)