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Pepsin / ˈ p ɛ p s ɪ n / is an endopeptidase that breaks down proteins into smaller peptides and amino acids. It is one of the main digestive enzymes in the digestive systems of humans and many other animals, where it helps digest the proteins in food. Pepsin is an aspartic protease, using a catalytic aspartate in its active site. [2]
Pepsin breaks down the protein in the food into smaller particles, such as peptide fragments and amino acids. Protein digestion, therefore, primarily starts in the stomach, unlike carbohydrate and lipids, which start their digestion in the mouth (however, trace amounts of the enzyme kallikrein , which catabolises certain protein, is found in ...
Chronic inflammatory diseases such as rheumatoid arthritis may involve the release of lysosomal enzymes into extracellular space that break down surrounding tissues. Abnormal proteolysis may result in age-related neurological diseases such as Alzheimer 's due to the generation and ineffective removal of peptides that aggregate in cells.
Protein catabolism often begins with pepsin, which converts proteins into polypeptides. These polypeptides are then further degraded. In humans, the pancreatic proteases include trypsin, chymotrypsin, and other enzymes. In the intestine, the small peptides are broken down into amino acids that can be absorbed into the bloodstream.
The breaking down into micelles creates a much larger surface area for the pancreatic enzyme, lipase to work on. Lipase digests the triglycerides which are broken down into two fatty acids and a monoglyceride. These are then absorbed by villi on the intestinal wall. If fats are not absorbed in this way in the small intestine problems can arise ...
The proenzyme Pepsinogen, with the exposure to hydrochloric acid gets converted into the active enzyme pepsin, the proteolytic enzyme of the stomach. Hydrochloric acid (HCl) provides the acidic pH (pH 1.8) optimal for pepsins. Rennin is a proteolytic enzyme found in gastric juice of infants which helps in the digestion of milk proteins.
Deamination is the removal of an amino group from a molecule. [1] Enzymes that catalyse this reaction are called deaminases. In the human body, deamination takes place primarily in the liver; however, it can also occur in the kidney. In situations of excess protein intake, deamination is used to break down amino acids for energy.
Biological hydrolysis is the cleavage of biomolecules where a water molecule is consumed to effect the separation of a larger molecule into component parts. When a carbohydrate is broken into its component sugar molecules by hydrolysis (e.g., sucrose being broken down into glucose and fructose), this is recognized as saccharification. [2]