Anatomy and Physiology II Practice Test 2025 - Free Anatomy Practice Questions and Study Guide

Trypsin is the enzyme that digests protein and is secreted in an inactive form, known as trypsinogen, in the pancreas. This process is crucial for the protection of the pancreas itself. If trypsin were secreted in its active form, it could begin digesting proteins prematurely, potentially causing harm to the pancreatic tissues.

The activation of trypsinogen occurs in the small intestine, where it is converted into active trypsin by the enzyme enterokinase, which is produced by the intestinal mucosa. Once activated, trypsin then goes on to digest proteins into smaller peptides and amino acids.

This protective mechanism ensures that the digestive enzymes are activated only when they reach the proper environment, allowing for effective digestion while safeguarding the pancreas from self-digestion. Other enzymes listed, such as amylase (which digests carbohydrates), pepsidase (not a primary term in this context), and lipase (which digests fats), do not fit the criteria of being a protein-digesting enzyme secreted in an inactive form by the pancreas.