Native lysozyme from human neutrophils. occur in specific granules of human polymorphonuclear leukocytes and takes part in the antibacterial activity of leukocytes. Hydrolyzes β1,4 linkages between N-acetylmuramic acid (2-acetamido-2-deoxy-3-O-[1′-carboxymethyl]-glucopyranose) residues in chitin.
CAT No: R1851
CAS No:9001-63-2
Synonyms/Alias:9001-63-2;LYSOZYME;Lysozyme derived-peptide;RVVRDPQGIRAWVAWRNR;HL18;NH2-Arg-Val-Val-Arg-Asp-Pro-Gln-Gly-Ile-Arg-Ala-Trp-Val-Ala-Trp-Arg-Asn-Arg-COOH;
Lysozymum, also known as lysozyme, is a naturally occurring enzyme with significant biochemical importance due to its ability to hydrolyze the β(1,4) glycosidic bonds in the peptidoglycan layer of bacterial cell walls. As a cationic, globular protein commonly found in egg whites, tears, and other secretions, lysozyme plays a fundamental role in innate immunity across various organisms. Its well-characterized structure, catalytic mechanism, and specificity for bacterial substrates have made it a model system in enzymology and structural biology. Owing to its robust lytic activity and stability, lysozyme is widely utilized in a range of research, analytical, and biotechnological applications.
Antibacterial mechanism studies: Lysozyme serves as a prime tool for investigating the molecular basis of bacterial cell wall degradation. Researchers employ it to study the structural vulnerabilities of Gram-positive bacteria, elucidate the enzymatic cleavage of peptidoglycan, and characterize the factors influencing bacterial resistance. Its defined catalytic activity allows for controlled dissection of lytic processes, supporting the development of new antibacterial strategies and the understanding of host-pathogen interactions at the molecular level.
Protein crystallography and structural analysis: As one of the first enzymes to have its three-dimensional structure solved by X-ray crystallography, lysozyme remains a cornerstone in structural biology. It is frequently used as a model protein for crystallization trials, method development, and validation of new analytical techniques. Its amenability to high-resolution structural studies enables researchers to explore protein folding, stability, and ligand interactions, making it invaluable for both educational and advanced research purposes.
Cell lysis and biomolecule extraction: In molecular biology and microbiology laboratories, lysozyme is routinely applied to facilitate the lysis of bacterial cells, particularly for the extraction of intracellular components such as nucleic acids and proteins. Its selective action on peptidoglycan provides a gentle yet effective means of disrupting cell envelopes without compromising the integrity of target biomolecules. This application is critical in workflows involving plasmid DNA isolation, recombinant protein recovery, and downstream analytical procedures.
Analytical reagent in enzyme kinetics and assay development: The well-characterized kinetic properties of lysozyme make it a standard reagent for enzyme activity assays and kinetic studies. Its use in spectrophotometric and fluorometric assays enables precise quantification of lytic activity, substrate specificity, and inhibitor screening. Researchers leverage its predictable behavior to calibrate instruments, validate assay protocols, and benchmark new enzymatic methodologies, enhancing the reliability and reproducibility of experimental results.
Food safety and quality control research: Lysozyme's ability to inhibit the growth of spoilage and pathogenic bacteria has led to its adoption in studies focused on food preservation and safety. Researchers utilize it to evaluate antimicrobial interventions, monitor microbial contamination, and investigate the mechanisms underlying food spoilage. Its natural origin and specificity for certain bacterial strains provide a valuable model for developing and testing biopreservation strategies in dairy, beverage, and other food-related research contexts.
1. An Open-label, Single-center, Safety and Efficacy Study of Eyelash Polygrowth Factor Serum
5. Myotropic activity of allatostatins in tenebrionid beetles
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