Is Lysozyme an Enzyme? How It Breaks Down Bacteria

Lysozyme is a substance found naturally throughout the human body, serving as one of the first biological defenses against foreign invaders. It is present in many bodily fluids, acting as a chemical guard against potential threats. We explore the nature of lysozyme and the precise mechanism it employs to break down the tough outer layers of bacteria.

Lysozyme is an Enzyme: Classification and Function

Lysozyme is definitively classified as an enzyme, a protein that acts as a biological catalyst to speed up specific chemical reactions without being consumed. Enzymes are grouped into classes based on the reaction they accelerate, and lysozyme belongs to the hydrolase category. Hydrolases utilize a water molecule to cleave a chemical bond in a process called hydrolysis.

Lysozyme is specifically identified as a glycoside hydrolase because it targets and breaks the bonds between sugar molecules. Its catalytic action involves binding to a complex sugar structure and separating the components using water. This function enables a relatively small number of lysozyme molecules to destroy a vast quantity of bacterial cell walls.

How Lysozyme Breaks Down Bacterial Walls

Lysozyme’s antibacterial action targets the peptidoglycan layer, a mesh-like polymer that gives the bacterial cell wall its structural rigidity. This layer is particularly thick and exposed in Gram-positive bacteria, making them especially susceptible. Peptidoglycan is built from alternating sugar derivatives, N-acetylglucosamine (NAG) and N-acetylmuramic acid (NAM), linked together in long chains.

The enzyme specifically cleaves the beta-(1,4) glycosidic linkage that connects the NAM and NAG sugar units within the peptidoglycan backbone. Lysozyme’s active site is a groove that accommodates a segment of the peptidoglycan chain, positioning the bond precisely for cleavage. This process involves two key amino acid residues, Glutamic acid-35 and Aspartic acid-52, which facilitate the bond-breaking reaction.

The successful cleavage of these sugar linkages damages the structural integrity of the cell wall. Once the rigid support is compromised, the high internal osmotic pressure inside the bacterial cell can no longer be contained. This imbalance causes water to rush into the bacterium, leading to osmotic lysis, where the cell membrane ruptures and the bacterium dies.

Lysozyme’s Role in Innate Immunity

Lysozyme functions as a widely distributed component of the innate immune system, acting as a first line of non-specific defense against invading microorganisms. Its presence is concentrated in secretions that bathe the body’s most vulnerable mucosal surfaces, which are prime entry points for bacteria.

Lysozyme Distribution

Lysozyme is found in several key locations:

  • Tears, protecting the surface of the eye from airborne pathogens.
  • Saliva and mucus, providing a protective barrier in the oral cavity and the respiratory tract.
  • The gastrointestinal tract, where it helps control the bacterial population.
  • Breast milk, where it plays a protective role in developing the infant’s gut microflora.

Beyond external secretions, lysozyme is stored inside specialized immune cells, specifically phagocytes like neutrophils and macrophages. When these cells engulf a bacterium, they deliver lysozyme into the internal compartment, called the phagosome, where it works to destroy the ingested invader.