It is an enzyme that can be found in tears, saliva, sweat, mucus, etc. It has the ability to attack and destroy bacteria that try to enter our body through passageways such as eyes, mouth or skin. It is a part of the first level defense in our body which prevents germs from entering the body.
The condensed structure of lysozyme from hen egg white is made up of a single peptide chain with around 129 amino acids (hen egg white lysozyme or egg lysozyme). The amino acid residues are numbered starting with the terminal -group (N) and ending with the terminal carboxyl-group (C). The circles indicate that each fifth and tenth residue is given a number. The four disulfide bridges are indicated by the broken lines as well. Alpha-helices can be seen in the ranges of 25 to 35, 90 to 100, and 120 to 125.
The lysozyme enzyme hydrolyzes, attacks, and breaks glycosidic linkages in peptidoglycans. Additionally, although less effectively than real chitinases, this specific lysozyme enzyme can break glycosidic linkages in chitin. The Lysozyme's active site binds the peptidoglycan molecule in the noticeable cleft that separates its two domains. It targets the peptidoglycans by interacting with the fourth carbon atoms of N-acetylglucosamine (NAG) and N-acetylmuramic acid (NAM) (which are found in the cell walls of bacteria, especially Gram-positive bacteria).