Endopeptidase

Endopeptidase is a digestive enzyme (such as pepsin) that catalyzes the breakdown of protein into small peptide fractions. This occurs due to the cleavage of peptide bonds within the protein molecule.

By comparison, exopeptidase cleaves peptide bonds at the ends of the peptide chain, rather than inside it.

Endopeptidase belongs to the class of peptidase enzymes that generally catalyze the hydrolysis of peptide bonds. Thus, endopeptidase is one of the important components of the digestive system, ensuring the breakdown of proteins into simpler compounds.

Endopeptidase is a digestive enzyme (such as pepsin) that catalyzes the breakdown of protein into small peptide fractions. This occurs due to the cleavage of peptide bonds within the protein molecule.

Unlike endopeptidases, exopeptidases cleave peptide chains from the ends of the molecule. Endopeptidases also belong to the group of peptidase enzymes, which are generally responsible for the cleavage of peptide bonds.

Thus, endopeptidases play an important role in the digestion process because they break down proteins into small fragments, which can then be absorbed into the blood and used by the body. The key representative of endopeptidases is the enzyme pepsin, produced in the stomach to digest protein foods.

Endopeptide aza (End op ep t id a se) is a specific enzyme that breaks down the internal part of a protein molecule by hydrolysis of the peptide bond. Outwardly, it resembles pepsin, a gastromucular enzyme of cattle, used in various fields: cooking, medicine, cosmetology and veterinary medicine. In the article we will analyze endopeptidase in more detail, the main properties,