Difference between Pepsin and Trypsin

Pepsin and Trypsin are two types of proteolytic enzymes that play a significant role in the digestion of proteins. However, there are several differences between the two enzymes that are discussed below.

Origin

Pepsin is produced in the stomach by chief cells while Trypsin is produced in the pancreas by pancreatic acinar cells.

Activation

Pepsin is activated by hydrochloric acid in the stomach, while Trypsin is activated by enterokinase in the small intestine.

Substrate specificity

Pepsin acts on proteins and breaks them down into smaller peptides while Trypsin acts on peptides and breaks them down into smaller amino acids.

pH optimum

Pepsin has an optimum pH of 1.5-2.5 while Trypsin has an optimum pH of 7.8-8.7.

Location of action

Pepsin works in the stomach while Trypsin works in the small intestine.

Conclusion

In summary, Pepsin and Trypsin are two different types of proteolytic enzymes that act on different substrates and are activated under different conditions. Pepsin is produced in the stomach, activated by hydrochloric acid and breaks down proteins while Trypsin is produced in the pancreas, activated by enterokinase and breaks down peptides.