Description
Lysozyme (Egg White) is a high-activity, purified enzyme widely used in molecular biology and enzymology research. This lyophilized powder is highly effective at disrupting the cell walls of Gram-positive bacteria and can also aid in Gram-negative lysis when combined with membrane-permeabilizing treatments.
It is a classic model enzyme for kinetics, catalytic mechanism, and structural biology studies, including protein crystallography, making it a cornerstone tool in both teaching and advanced research laboratories.
Lysozyme is soluble in aqueous buffers and is rigorously quality-controlled, providing reproducible performance across DNA, RNA, and protein extraction workflows, enzymatic activity assays, and structural-function experiments.
Lysozyme is an enzyme capable of breaking down the bacterial cell wall, and is typically used to enhance protein extractions or nucleic acid extractions. It works by hydrolyzing the 1,4-β-linkages located between the N-acetylmuramic acid and the N-acetyl-D-glucosamine residues in peptidoglycan.
Gram-positive cells have an increased susceptibility to the actions of lysozyme since gram-positive cells have a higher quantity of peptidoglycan in the cell wall. Gram-negative cells are less vulnerable, but can still be hydrolyzed in the presence of EDTA.
Unit Definition:
1 FIP unit of lysozyme is the amount of Enzyme that hydrolyzes under the standard conditions 1 mmole of a Micrococcus lysodeikticus per minute.
Applications
- Enzymatic digestion of bacterial cell walls
- Enhancement of protein or nucleic acid extractions
- Antibacterial activity against gram positive bacteria
- Model protein
Common Research Applications
(Click each for more information)
Lysis of Gram-Positive and Gram-Negative Bacterial Cell Walls
-
Purpose: To disrupt bacterial cell walls for DNA, RNA, or protein extraction.
-
How It Works: Lysozyme hydrolyzes the β(1→4) glycosidic bond between N-acetylmuramic acid and N-acetylglucosamine in peptidoglycan, weakening the wall and causing osmotic lysis. Gram-positive bacteria are especially susceptible; Gram-negative bacteria typically require additional agents (e.g., EDTA) to permeabilize the outer membrane.
-
Applications: Used in genomic DNA extraction, plasmid minipreps, and bacterial protein extraction.
Sambrook, J., & Russell, D. W. (2001). Molecular Cloning: A Laboratory Manual (3rd ed.). Cold Spring Harbor Laboratory Press.
Enzymatic Lysis in Protein Purification Protocols
-
Purpose: To prepare cell lysates for recombinant protein purification.
-
How It Works: Used together with detergents and nucleases to ensure efficient breakdown of bacterial cell walls while preserving protein integrity.
-
Applications: Widely used in His-tag protein purification, enzyme studies, and proteomics workflows.
Walls, D., & Loughran, S. T. (2007). Protein Chromatography: Methods and Protocols, 681, 15–22. https://doi.org/10.1007/978-1-59745-588-9_2
Model Enzyme in Enzyme Kinetics and Structure-Function Studies
-
Purpose: To explore enzyme-substrate interactions, catalytic rates, and structure-function relationships.
-
How It Works: Lysozyme’s extensively studied structure makes it a model system for enzymology education and research, often serving as the "textbook enzyme."
-
Applications: Kinetics labs, inhibitor screening, and catalytic mechanism studies.
Vocadlo, D. J., Davies, G. J., Laine, R., & Withers, S. G. (2001). Nature, 412(6849), 835–838. https://doi.org/10.1038/35090589
Standardization of Muramidase Activity Assays
-
Purpose: To measure lysozyme activity for enzyme QC, inhibitor testing, or standardization.
-
How It Works: Lysozyme activity is measured via the lysis of Micrococcus lysodeikticus cells, monitoring turbidity reduction at 450 nm.
-
Applications: Used in enzyme validation, commercial product QC, and inhibitor screening.
Shugar, D. (1952). Biochimica et Biophysica Acta, 8, 302–309.
Structural Biology and Crystallography Studies
-
Purpose: To investigate protein folding, crystallization methods, and structure-based drug discovery.
-
How It Works: Hen egg-white lysozyme is one of the most widely crystallized proteins, making it a model for developing crystallographic techniques and testing protein-ligand interactions.
-
Applications: X-ray crystallography, protein folding studies, and drug binding assays.
McPherson, A. (1982). Preparation and Analysis of Protein Crystals. Wiley.
Benefits:
- Effective lysis of Gram-positive bacteria: Facilitates DNA, RNA, and protein extraction workflows. Gram-negative bacteria typically require lysozyme in combination with membrane-permeabilizing agents.
- High enzymatic activity: Validated potency ensures reliable performance in activity assays and bacterial lysis under appropriate conditions.
- Well-characterized structure: Ideal for enzymology education, mechanistic studies, and structural biology.
- Purified natural source: Derived from hen egg white and standardized for reproducible laboratory performance.
- Versatile applications: Widely used in lysis protocols, enzymatic activity assays, protein crystallography, and structure-function studies.
Storage/Handling
Store at -20°C.
Avoid freeze/thaw cycles
Working Concentration
Make stock solutions at 10 mg/ml in 10mM Tris-HCl, pH 8.0
Working concentration should be between 0.1-1.0 mg/ml.
Powered by Bioz
