Background:

Lysozyme from chicken egg white is a bactericidal enzyme present in chicken eggs, and it lyses gram-positive bacteria.IC50 & Target: Bacteria[1]In Vitro: Lysozyme is an ubiquitous enzyme. The hen egg is the most abundant source of lysozyme, which constitutes approximately 3.4% of the albumen proteins. Lysozyme is a natural antimicrobial that hydrolyzes the β(1-4) glycosidic linkage between N-acetylmuramic acid and N-acetylglucosamine found in the peptidoglycan layer of the bacterial cell wall and causing cell lysis. The bactericidal effect of lysozyme is primarily limited to gram-positive bacteria, including pathogens such as Listeria monocytogenes and certain Clostridium species as well as some spoilage organisms, including thermophilic spore-forming bacteria and certain yeasts. The gram-negative bacteria are more resistant to lysozyme action because of their complex cell wall structure[1].

Lysozyme is an ubiquitous enzyme. The hen egg is the most abundant source of lysozyme, which constitutes approximately 3.4% of the albumen proteins. Lysozyme is a natural antimicrobial that hydrolyzes the β(1-4) glycosidic linkage between N-acetylmuramic acid and N-acetylglucosamine found in the peptidoglycan layer of the bacterial cell wall and causing cell lysis. The bactericidal effect of lysozyme is primarily limited to gram-positive bacteria, including pathogens such as Listeria monocytogenes and certain Clostridium species as well as some spoilage organisms, including thermophilic spore-forming bacteria and certain yeasts. The gram-negative bacteria are more resistant to lysozyme action because of their complex cell wall structure[1].

[1]. Banerjee P, et al. Influence of carbon dioxide on the activity of chicken egg white lysozyme. Poult Sci. 2011 Apr;90(4):889-95.