Enteropeptidase converts trypsinogen into active trypsin, which not only hydrolyses some peptide bonds of food proteins but also activates a number of pancreatic zymogens. For this reason enteropeptidase is a key enzyme in the digestion of dietary proteins and its absence may result in gross protein malabsorption.
How trypsinogen and chymotrypsinogen is activated?
Trypsinogen is optimally activated by purified enterokinase at 30°C after 2 hr in the presence of 25 mm Tris-HCl, pH 8.1, containing 25 mm CaCl2. Chymotrypsinogen is optimally activated by trypsin at 4° after 2 hr in the presence of 50 mm Tris-HCl, pH 8.1.
What activates inactive trypsinogen?
Trypsinogen is an inactive pancreatic enzyme which gets activated by an enzyme enterokinase secreted by the intestinal mucosa into active trypsin. The enzyme trypsin in turn activates other enzymes present in the pancreatic juice.
