Library.

“Pancreatic proteases such as trypsinogen and chymotrypsinogen are synthesized as inactive zymogens and are activated in the duodenum by an intestinal enzyme (enterokinase/enteropeptidase), which helps prevent autodigestion of the pancreas.”

The claim matches standard human physiology. Pancreatic proteases are secreted as inactive precursors, and enteropeptidase in the duodenum initiates their activation by converting trypsinogen to trypsin, which then activates other zymogens. Delaying activation until the intestine is an important safeguard against pancreatic autodigestion, though not the only one.

“After proteases finish digesting food in the duodenum, they move with chyme into the mid and distal small intestine and begin digesting themselves and other enzymes into amino acids.”

The evidence supports that pancreatic proteases continue moving with chyme beyond the duodenum and may be degraded during transit. But the claim misstates both timing and mechanism: protein digestion is not simply finished in the duodenum, and free amino acids are produced mainly through brush-border and intracellular peptidases, not primarily by proteases digesting themselves and other enzymes.