Canadian National Institute Of Health (CNIH) Entrance Practice Exam

Trypsin and pepsin play crucial roles in the digestive system, specifically in the process of protein digestion. Both of these enzymes are proteases, which means their primary function is to cleave the peptide bonds in proteins, breaking them down into smaller peptides and ultimately into amino acids that the body can absorb and utilize for various functions, including building and repairing tissues. Pepsin is secreted in an inactive form known as pepsinogen by the gastric mucosa and is activated in the acidic environment of the stomach. This activation allows pepsin to begin the digestion of proteins in the food we consume. Trypsin, on the other hand, is produced in the pancreas and secreted into the small intestine in its inactive form (trypsinogen). Once it reaches the small intestine, it is activated by another enzyme (enterokinase), and it continues the work initiated by pepsin, further breaking down proteins into even smaller peptides. Understanding that these enzymes specifically target proteins clarifies why the main function of trypsin and pepsin is to break down proteins rather than lipids, carbohydrates, or neutralizing acids. Their effectiveness in protein digestion is essential for proper nutrition and absorption of amino acids essential for bodily functions