Lysozyme from chicken egg white is a bactericidal enzyme, and it lyses gram-positive bacteria. Lysozyme from chicken egg white can also be used for the research of HIV infection and pulmonary emphysema^[1][2][3].

Bacteria^[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].
Lysozyme (1 mg/mL) impairs the ability of hyaluronan (HA) to prevent elastase injury to elastic fibers^[3].

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.

• [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.  [Content Brief]

  [2]. Jing T, et al. Magnetic molecularly imprinted nanoparticles for recognition of lysozyme. Biosens Bioelectron. 2010 Oct 15;26(2):301-6.  [Content Brief]

  [3]. Cantor JO, et al. The effect of lysozyme on elastase-mediated injury. Exp Biol Med (Maywood). 2002 Feb;227(2):108-13.  [Content Brief]