Pepsin vs Trypsin
Structure
- **Pepsin**: Pepsin is an enzyme that is produced in the stomach. It is a protease enzyme that breaks down proteins into smaller peptides.
- **Trypsin**: Trypsin is an enzyme produced in the pancreas. It is also a protease enzyme that breaks down proteins into smaller peptides.
Optimal pH
- **Pepsin**: Pepsin works best in an acidic environment with a pH of around 2. This is because it is produced in the stomach, which has a low pH due to the presence of hydrochloric acid.
- **Trypsin**: Trypsin works best in a slightly alkaline environment with a pH of around 8. This is because it is produced in the pancreas, which secretes bicarbonate to neutralize the acidic chyme that comes from the stomach.
Substrate Specificity
- **Pepsin**: Pepsin specifically cleaves peptide bonds between certain amino acids, such as phenylalanine and leucine.
- **Trypsin**: Trypsin specifically cleaves peptide bonds on the carboxyl side of basic amino acids like lysine and arginine.
Activation
- **Pepsin**: Pepsin is produced in its inactive form, pepsinogen, which is activated by the acidic environment in the stomach.
- **Trypsin**: Trypsin is produced in its inactive form, trypsinogen, which is activated by an enzyme called enterokinase in the small intestine.
Function
- **Pepsin**: Pepsin helps in the digestion of proteins in the stomach.
- **Trypsin**: Trypsin helps in the digestion of proteins in the small intestine after food leaves the stomach.
In conclusion, both pepsin and trypsin are important enzymes involved in the digestion of proteins, but they have different structures, optimal pH levels, substrate specificities, activation processes, and functions in the digestive system.