Pepsin and Trypsin:

Definition:
Pepsin and Trypsin are two types of enzymes that help in the process of digestion in humans.

Location:
Pepsin is produced in the stomach, while trypsin is produced in the pancreas and released into the small intestine.

Function:
Pepsin helps to break down proteins into smaller peptide fragments while trypsin helps to break down proteins into even smaller peptide fragments and individual amino acids.

Optimal pH:
Pepsin works best in a highly acidic environment with a pH of around 2.0, while trypsin works best in a slightly alkaline environment with a pH of around 8.0.

Activation:
Pepsin is produced as an inactive precursor called pepsinogen, which is activated by the acidic environment in the stomach. Once activated, pepsin can begin breaking down proteins. Trypsin is also produced as an inactive precursor called trypsinogen, which is activated by an enzyme called enterokinase that is produced by cells in the small intestine.

Substrate specificity:
Pepsin is most effective at breaking down proteins that have already been partially digested by other enzymes, while trypsin is most effective at breaking down specific peptide bonds in proteins.

Conclusion:
In summary, while both pepsin and trypsin are enzymes involved in protein digestion, they have different locations, functions, optimal pH levels, activation mechanisms, and substrate specificities. Understanding these differences is important for understanding the process of protein digestion in the human body.

Pepsin is an enzyme which acts only in acidic medium ,trypsine is an enzyme which acts in alkaline medium.