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How does lysozyme work?

Published in Biochemistry 2 mins read

Lysozyme works as an antimicrobial enzyme by essentially dissolving bacterial cell walls, leading to cell death.

Here's a more detailed explanation:

  • What is Lysozyme? Lysozyme is a naturally occurring enzyme found in various bodily secretions like tears, saliva, breast milk, and mucus. It is also present in egg white. Its primary function is to protect the body against bacterial infections.

  • The Target: Peptidoglycan: Lysozyme specifically targets the peptidoglycan layer, a major component of bacterial cell walls, particularly in Gram-positive bacteria. Peptidoglycan provides structural integrity to the bacterial cell.

  • The Mechanism: Cleavage: Lysozyme acts as a glycoside hydrolase. This means it catalyzes the hydrolysis (breaking down using water) of the β-1,4-glycosidic bonds between N-acetylmuramic acid (NAM) and N-acetylglucosamine (NAG) residues, which are the building blocks of peptidoglycan.

  • Weakening the Cell Wall: By breaking these bonds, lysozyme weakens the structural integrity of the bacterial cell wall.

  • Cell Lysis and Death: This weakening can eventually lead to cell lysis (bursting) due to osmotic pressure, resulting in the death of the bacterium.

In summary, lysozyme destroys bacteria by breaking down their cell walls, causing them to rupture and die.

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