Lysozyme is a glycoside hydrolase enzyme (EC 3.2.1.17) that catalyzes the hydrolysis of beta-1,4-glycosidic bonds between N-acetylmuramic acid and N-acetylglucosamine residues in peptidoglycan, the primary structural component of bacterial cell walls. Naturally occurring in egg whites, tears, saliva, and milk, it exhibits potent antimicrobial activity against Gram-positive bacteria. In food applications, it serves as a preservative to control spoilage organisms in cheese, wine, and processed meats. The protein consists of 129 amino acid residues with a compact globular structure stabilized by four disulfide bonds. It is heat-labile and denatures above approximately 75°C. Lysozyme is approved for food use and demonstrates high solubility in aqueous solutions at neutral to slightly acidic pH.