Enzidase enzymatic action works to improve the hydrolysis of proteins--a chemical process by which they are combined with water and broken own into smaller compounds; it is the same process by which starches are converted to glucose.

Lysozyme is an enzyme that damages bacterial cell walls. It can be found in a number of secretions, such as tears, saliva, and mucus, and can come from egg whites, for example.

Most of the bacteria affected by lysozyme are not pathogenic. In some cases, lysozyme is a primary reason these organisms do not become pathogenic.

Lysozyme serves as a non-specific innate opsonin (any molecule that acts as a binding enhancer for the process of phagocytosis) by binding to the bacterial surface, reducing the negative charge and facilitating phagocytosis of the bacterium before opsonins from the acquired immune system arrive at the scene. In other words, lysozyme makes it easier for phagocytic white blood cells to engulf bacteria.

The enzyme functions by attacking peptidoglycans (found in the cells walls of bacteria, especially Gram-positive bacteria) and hydrolyzing the glycosidic bond that connects N-acetylmuramic acid with the fourth carbon atom of N-acetylglucosamine. It does this by binding to the peptidoglycan molecule in the binding site within “the prominent cleft between its two domains”.

The amino acid side chains glutamic acid 35 (Glu35) and aspartate 52 (Asp52) have been found to be critical to the activity of this enzyme. Glu35 acts as a proton donor to the glycosidic bond, whilst Asp52 acts as a nucleophile to generate a glycosyl enzyme intermediate. The glycosyl enzyme intermediate then reacts with a water molecule, to give the product of hydrolysis and leaving the enzyme unchanged.