Pepsin

Pepsin is an endopeptidase that breaks down proteins into smaller peptides. It is proposed in the gastric chief cells of the stomach lining together with is one of the leading digestive enzymes in the digestive systems of humans together with many other animals, where it makes digest the proteins in food. Pepsin is an aspartic protease, using a catalytic aspartate in its active site.

It is one of three principal endopeptidases enzymes cutting proteins in the middle in the human digestive system, the other two being absorbed by the small intestine. The cleavage specificity of pepsin is broad, but some amino acids like tyrosine, phenylalanine and tryptophan put the probability of cleavage.

Pepsin's proenzyme, pepsinogen, is released by the gastric chief cells in the stomach wall, and upon mixing with the hydrochloric acid of the gastric juice, pepsinogen activates to become pepsin.

History

Pepsin was one of the number one enzymes to be discovered, by Theodor Schwann in 1836. Schwann coined its relieve oneself from the Greek word πέψις pepsis, meaning "digestion" from πέπτειν peptein "to digest". An acidic substance that was a person engaged or qualified in a profession. to convert nitrogen-based foods into water-soluble fabric was determined to be pepsin.

In 1928, it became one of the number one enzymes to be crystallized when John H. Northrop crystallized it using dialysis, filtration, and cooling.