Lysozyme vs. Lysosome

Main Difference

The main difference between Lysozyme and Lysosome is that the Lysozyme is a protein-coding gene in the species Homo sapiens and Lysosome is a small lytic vacuole with cell cycle-independent morphology, found in most animal cells; contains a variety of hydrolases, most of which have their maximal activities in the pH range 5-6.

• Lysozyme

  Lysozyme, also known as muramidase or N-acetylmuramide glycanhydrolase, is an antimicrobial enzyme produced by animals that forms part of the innate immune system. Lysozyme is a glycoside hydrolase that catalyzes the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in peptidoglycan, which is the major component of gram-positive bacterial cell wall. This hydrolysis in turn compromises the integrity of bacterial cell walls causing lysis of the bacteria.

  Lysozyme is abundant in secretions including tears, saliva, human milk, and mucus. It is also present in cytoplasmic granules of the macrophages and the polymorphonuclear neutrophils (PMNs). Large amounts of lysozyme can be found in egg white. C-type lysozymes are closely related to alpha-lactalbumin in sequence and structure, making them part of the same glycoside hydrolase family 22. In humans, the C-type lysozyme enzyme is encoded by the LYZ gene.Lysozyme is thermally stable, with a melting point reaching up to 72 ℃ at pH 5.0. However, in human milk it loses activity very quickly at that temperature. Its isoelectric point is 11.35. Lysozyme can survive in a large range of pH (6-9).

• Lysosome

  A lysosome () is a membrane-bound organelle found in many animal cells. They are spherical vesicles that contain hydrolytic enzymes that can break down many kinds of biomolecules. A lysosome has a specific composition, of both its membrane proteins, and its lumenal proteins. The lumen’s pH (~4.5–5.0) is optimal for the enzymes involved in hydrolysis, analogous to the activity of the stomach. Besides degradation of polymers, the lysosome is involved in various cell processes, including secretion, plasma membrane repair, cell signaling, and energy metabolism.

  Lysosomes act as the waste disposal system of the cell by digesting obsolete or un-used materials in the cytoplasm, from both inside and outside the cell. Material from outside the cell is taken-up through endocytosis, while material from the inside of the cell is digested through autophagy. The sizes of the organelles vary greatly—the larger ones can be more than 10 times the size of the smaller ones. They were discovered and named by Belgian biologist Christian de Duve, who eventually received the Nobel Prize in Physiology or Medicine in 1974.

  Lysosomes are known to contain more than 60 different enzymes, and have more than 50 membrane proteins. Enzymes of the lysosomes are synthesised in the rough endoplasmic reticulum. The enzymes are imported from the Golgi apparatus in small vesicles, which fuse with larger acidic vesicles. Enzymes destined for a lysosome are specifically tagged with the molecule mannose 6-phosphate, so that they are properly sorted into acidified vesicles.Synthesis of lysosomal enzymes is controlled by nuclear genes. Mutations in the genes for these enzymes are responsible for more than 30 different human genetic disorders, which are collectively known as lysosomal storage diseases. These diseases result from an accumulation of specific substrates, due to the inability to break them down. These genetic defects are related to several neurodegenerative disorders, cancers, cardiovascular diseases, and ageing-related diseases.Lysosomes should not be confused with liposomes, or with micelles.