Lysozyme
Description:
Lysozyme, also known as muramidase or N-acetylmuramide glycanohydrolase, is a single polypeptide chain consisting of 129 amino acid residues from 18 types of amino acids. It is rich in basic amino acids and stabilized by four disulfide bonds, making it an alkaline protein. The N-terminus is lysine, and the C-terminus is leucine. Egg white lysozyme, classified as type C, is one of the most heat-resistant enzymes known. Lysozyme is an alkaline enzyme that hydrolyzes polysaccharides in pathogenic bacteria by breaking the β-1,4 glycosidic bond between N-acetylmuramic acid and N-acetylglucosamine in the bacterial cell wall, converting insoluble polysaccharides into soluble glycopeptides, causing cell wall rupture and bacterial lysis. Additionally, lysozyme can bind directly to negatively charged viral proteins, forming complexes with DNA, RNA, and apoproteins, resulting in viral inactivation. Thus, it has antibacterial, anti-inflammatory, and antiviral properties.
Basic Information:
Chinese Name: 溶菌酶
Synonyms: Muramidase; Egg White Lysozyme; N-acetylmuramide glycanohydrolase
English Name: Lysozyme, abbreviated as LZM
Source: Egg white
CAS Number: 12650-88-3
Molecular Weight: 14300
Activity: ≥20000 u/mg
Optimal pH: 5.3-6.4
Moisture: ≤5.0%
Ash Content: ≤4.0%
Total Nitrogen Content: 15-17%
Microbial Standard: Conforms to specifications
Storage Conditions: 2-8℃
Appearance: White to off-white lyophilized powder
Applications: For research use only, primarily in biochemical studies. Lysozyme can be used to hydrolyze the cell walls of Gram-positive and Gram-negative bacteria.