Once pepsinogen is activated, pepsin then breaks down the protein into small polypeptides and some free amino acids. Pepsin will break down proteins into a simpler form, namely proteosa and peptone. Pepsin begins protein digestion by breaking down certain amino acid bonds in proteins to produce peptide fragments (short chain amino acids).
In the lumen, hydrochloric acid (HCl) activates pepsinogen into its active form by deciding on a small fragment. Once activated, pepsin autocatalically activates more pepsinogens and initiates protein digestion. The secretion of pepsinogen in the inactive form prevents the digestion of the stuntramental protein of the cell in which the enzyme is produced. The activation of pepsinogen does not occur until the enzyme function of the pepsin reaches the lumen and contacts with HCl secreted by other cells in the gastric sacs.
After pepsin enzyme function is no longer needed, this enzyme is then stored again in inactive form, so this substance does not digest itself the cells in which it is formed. Therefore, pepsin is maintained in the inactive form of pepsinogen until it reaches the intestinal lumen, where it is activated by HCl.
Pepsin breaks down denatured proteins into large polypeptide derivatives. Pepsin is an endopeptidase enzyme because it hydrolyzes the peptide bonds located within the main polypeptide structure, not those located at the amino or carboxylic terminal residues, which are characteristic of exopeptidase. The nature of this enzyme is specific to peptide bonds formed by aromatic amino acids (such as tyrosine) or dicarboxylic amino acids (such as glutamate).
Thus a brief discussion of the function of pepsin enzymes in the digestive system of proteins in the human body. Hopefully useful and read our next article which is about how the enzyme works according to the theory of lock and key and induced fit.