The function of Pepsin Enzymes in the Digestive Process

The function of Pepsin Enzymes in the Digestive Process

The function of the Pepsin Enzyme / Enzyme is a biological polymer that catalines more than one dynamic process in life as we know it today. Enzymes play a central role in the body's metabolism of organisms as determinants of the rapidity of physiological events. The breakdown and digestion of food, the assembly of chemical bonds of the body builders into proteins, cell membranes, and DNA that encode genetic information, until the use of energy to produce cell motion, all due to the presence of carefully coordinated enzymes. One of the enzymes that play a role in the breakdown and digestion of food is pepsin.

Function of Pepsin Enzyme

Just like the trypsin enzyme, the function of pepsin enzyme is closely related to protein digestion process. Protein digestion begins in the stomach. The secretion of food in the stomach is aided by gastric secretions known as gastric juices. The gastric sap comprises about 97-99% water. The rest consists of mucin (mucus) as well as inorganic salts, digestive enzymes (pesin and renin), and lipase. This event is the main digestive function of the stomach.

Function of Pepsin Enzyme

Gastric Phase

Gastric secretion occurs when food is already in the stomach. Stimulants that act on the stomach are proteins, especially peptide fragments. Proteins directly stimulate gastrin expenditure. Gasrin is a strong stimulant for further secretion of acids and pepsinogens. Protein induces a very acidic and rich pepsin gastric acid, which continues the protein digestion that first begins the process. In the stomach, hydrochloric acid (HCL) describes the protein sequence (protein denaturation) and activates pepsinogen enzymes into pepsin. Pepsin is secreted in the form of pepsinogen. 

Pepsinogen secretion

Pepsin is produced by chief cells as inactive zymogen, pepsinogen. The main gastrointestinal constituent of gastric sap is pepsinogen, an inactive enzyme molecule that is synthesized and packed by the ultimate cell endoplasmic golgi and reticulum complexes. Pepsinogen is deposited in the main cell cytoplasm inside the secretory vesicles known as the zymogen granules, and from there pepsinogen is excreted through the process of exocytosis. Pepsinogen is activated into pepsin by H +, which breaks up a protective polypeptide to display active peptin; And by the peptin itself, which rapidly enables the pepsinogen molecule (autocatalysis).

Denaturation of Proteins by Pepsin

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.