Lysozyme C (HEWL)

Hen egg white lysozyme (HEWL), also known as Lysozyme C or Muramidase, is a small, globular enzyme that plays a critical role in the innate immune system by hydrolyzing the cell walls of bacteria [1, 4, 13]. Specifically, it cleaves the beta-1,4-glycosidic bonds between N-acetylmuramic acid and N-acetyl-D-glucosamine in peptidoglycan, leading to bacterial lysis, particularly in Gram-positive species [4, 13, 17]. Beyond its antibacterial properties, HEWL exhibits antiviral, anti-inflammatory, and immunomodulatory activities, making it a versatile molecule in both medicine and the food industry [1, 9, 11, 12]. In clinical practice, it is used as a therapeutic agent for treating infections of the upper respiratory tract, skin, and eyes, and it is being investigated for its potential in cancer therapy and managing inflammatory conditions [1, 9, 14, 15]. HEWL is also a cornerstone of structural biology and drug discovery, serving as a primary model protein for studying enzyme kinetics, protein folding, and ligand binding [12, 18, 21]. However, its use in humans is limited by its status as a major egg allergen (Gal d 4), which can trigger severe hypersensitivity reactions in susceptible individuals [3, 5, 8, 10].

Other names

Hen egg white lysozymeMuramidase1,4-beta-N-acetylmuramidase CAllergen Gal d 4Mucopeptide N-acetylmuramoylhydrolase

Hydrolysis of the beta-1,4-glycosidic bonds between N-acetylmuramic acid and N-acetyl-D-glucosamine in peptidoglycan