What is the Difference Between Trypsin and Pepsin?
🆚 Go to Comparative Table 🆚Trypsin and pepsin are both proteolytic enzymes involved in the digestion process, but they have some key differences:
- Origin and Secretion: Pepsin is secreted by the gastric juice in the stomach, while trypsin is secreted by the pancreatic juice in the small intestine.
- Optimal pH: Pepsin acts in an acidic environment (pH 1.8), while trypsin acts in an alkaline environment (pH 7.5-8).
- Activation: The inactive form of pepsin, pepsinogen, is activated by the hydrochloric acid (HCl) of the gastric juice. In contrast, the inactive form of trypsin, trypsinogen, is activated by an enzyme called enterokinase.
- Catalysis Mechanism: Pepsin is an aspartic protease that uses a catalytic aspartate in its active site, while trypsin is a serine protease employing the serine residue in its active site.
- Function: Pepsin acts on proteins and converts them into peptones, while trypsin converts peptones into polypeptides.
- Types: Pepsin has four different types: A, B, C, and D. Trypsin has two types: α-trypsin and β-trypsin.
In summary, pepsin and trypsin are both involved in breaking down proteins in the digestive system, but they function in different environments (acidic vs. alkaline) and have distinct activation mechanisms, functions, and types.
Comparative Table: Trypsin vs Pepsin
Here is a table comparing the differences between trypsin and pepsin:
Feature | Trypsin | Pepsin |
---|---|---|
Origin | Produced by the pancreas | Produced by the gastric glands of the stomach |
Component | Component of pancreatic juice | Component of gastric juice |
Activation | Inactive form is trypsinogen, activated by enteropeptidase | Inactive form is pepsinogen, activated by HCl of the gastric juice |
Catalysis Mechanism | Serine protease, uses a serine residue in the active site | Aspartic protease, uses a catalytic aspartate in the active site |
Optimal pH | Works best in alkaline pH (pH 7.5-8) | Optimum pH for activity is 1.8 |
Types | Two types: α- and β-trypsin | Four types: pepsin A, B, C, and D |
Specificity | Hydrolyzes peptide bonds at the C-terminal side of lysine or arginine | Hydrolyzes peptide bonds between large hydrophobic amino acid residues |
Function | Converts peptones into polypeptides | Acts on proteins and converts them into peptones |
Both trypsin and pepsin are proteolytic enzymes that act on proteins and break them down into peptides and amino acids. However, they have different origins, catalysis mechanisms, optimal pH, types, and specificities.
Read more:
- Trypsin vs Chymotrypsin
- Pepsin vs Protease
- Pepsin vs Pepsinogen
- Protease vs Peptidase
- Tryptone vs Peptone
- Pepsin vs Renin
- Proteolytic Enzymes vs Digestive Enzymes
- Protease vs Proteinase
- Proteinase K vs Protease
- Peptones vs Proteoses
- Endopeptidase vs Exopeptidase
- Warm vs Cold Trypsinization
- Acid Phosphatase vs Alkaline Phosphatase
- Peptide vs Dipeptide
- Lipase vs Amylase
- Proteasome vs Protease
- Peptide vs Protein
- Acid Hydrolysis vs Enzymatic Hydrolysis
- Renin vs Rennin