Difference between Trypsin and Pepsin

Trypsin and pepsin are two types of enzymes that play important roles in the digestion of proteins in the human body.

Trypsin is a proteolytic enzyme that is synthesized and secreted by the pancreas in an inactive form called trypsinogen. Trypsinogen is activated to trypsin in the small intestine by the action of another enzyme called enterokinase. Trypsin then catalyzes the hydrolysis of peptide bonds in proteins, specifically at the carboxyl group of lysine and arginine residues. This helps to break down large protein molecules into smaller peptides and amino acids, which can be absorbed by the intestinal cells and used for various physiological functions.

Pepsin, on the other hand, is a proteolytic enzyme that is synthesized and secreted by the stomach in an inactive form called pepsinogen. Pepsinogen is activated to pepsin in the stomach by the action of hydrochloric acid, which creates an acidic environment that favors pepsin activity. Pepsin then catalyzes the hydrolysis of peptide bonds in proteins, specifically at the carboxyl group of aromatic amino acids, such as phenylalanine, tyrosine, and tryptophan. This helps to break down large protein molecules into smaller peptides, which can be further digested by other proteolytic enzymes in the small intestine.

The main difference between trypsin and pepsin is their optimal pH range and substrate specificity. Trypsin has an optimal pH range of 7.5-8.5 and targets lysine and arginine residues, while pepsin has an optimal pH range of 1.5-2.5 and targets aromatic amino acids.

Trypsin and pepsin also differ in their location and timing of activity in the digestive system. Trypsin is synthesized and secreted by the pancreas and activated in the small intestine, while pepsin is synthesized and secreted by the stomach and activated in the stomach.

In summary, trypsin and pepsin are two types of enzymes that play important roles in the digestion of proteins in the human body. Trypsin is synthesized and secreted by the pancreas in an inactive form called trypsinogen and is activated in the small intestine, where it catalyzes the hydrolysis of peptide bonds in proteins at the carboxyl group of lysine and arginine residues. Pepsin, on the other hand, is synthesized and secreted by the stomach in an inactive form called pepsinogen and is activated in the stomach, where it catalyzes the hydrolysis of peptide bonds in proteins at the carboxyl group of aromatic amino acids. The main difference between trypsin and pepsin is their optimal pH range and substrate specificity.

Difference between Trypsin and Pepsin

Trypsin and pepsin are two types of digestive enzymes that play a role in breaking down protein molecules into smaller fragments. Following are the key differences between trypsin and pepsin:

Trypsin:

  • Source:
  • Trypsin is produced by the pancreas as trypsinogen which is then activated by other enzymes, such as enteropeptidase, to become trypsin.
  • Optimal Environment:
  • Trypsin works optimally at an alkaline pH (pH around 8), which is suitable for the environment of the small intestine.
  • Specificity:
  • Trypsin has specificity for peptide bonds containing amino acids with positively charged side chains, such as lysine and arginine.
  • Activity:
  • Trypsin catalyzes the cleavage of peptide bonds at the C-terminal side of the amino acids lysine and arginine.
  • Workplace:
  • Trypsin works in the small intestine to digest proteins that have been broken down by pepsin in the stomach.

Pepsin:

  • Source:
  • Pepsin is produced in the form of pepsinogen by stomach cells, and then activated by stomach acid to become pepsin.
  • Optimal Environment:
  • Pepsin works optimally at an acidic pH (pH around 2), which corresponds to the acidic environment of the stomach.
  • Specificity:
  • Pepsin has specificity for peptide bonds containing aromatic amino acids, such as phenylalanine and tyrosine.
  • Activity:
  • Pepsin catalyzes the breakdown of peptide bonds at the N-terminal side of the amino acids phenylalanine and tyrosine.
  • Workplace:
  • Pepsin works in the stomach to start the process of protein digestion.

Key Differences:

  • Source:
  • Trypsin is produced by the pancreas.
  • Pepsin is produced by stomach cells.
  • Optimal Environment:
  • Trypsin works optimally at an alkaline pH (around 8).
  • Pepsin works optimally at an acidic pH (around 2).
  • Specificity:
  • Trypsin has specificity for peptide bonds containing lysine and arginine.
  • Pepsin has specificity for peptide bonds containing phenylalanine and tyrosine.
  • Activity:
  • Trypsin catalyzes the cleavage of peptide bonds at the C-terminal side of amino acids.
  • Pepsin catalyzes the breakdown of peptide bonds at the N-terminal side of amino acids.
  • Workplace:
  • Trypsin works in the small intestine.
  • Pepsin works in the stomach.

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