Which pancreatic enzyme hydrolyzes peptide bonds in the small intestine?

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Multiple Choice

Which pancreatic enzyme hydrolyzes peptide bonds in the small intestine?

The main concept is proteolysis in the small intestine by pancreatic enzymes. Trypsin is the pancreatic protease that hydrolyzes peptide bonds in the small intestine. It is secreted as an inactive precursor (trypsinogen) and activated by enterokinase in the duodenum; once active, it cleaves peptide bonds on the carboxyl side of lysine and arginine residues and also activates other pancreatic proteases. The other options aren’t involved in peptide bond hydrolysis in the small intestine: pepsin works in the stomach (acidic environment), amylase digests carbohydrates, and lipase digests fats.

The main concept is proteolysis in the small intestine by pancreatic enzymes. Trypsin is the pancreatic protease that hydrolyzes peptide bonds in the small intestine. It is secreted as an inactive precursor (trypsinogen) and activated by enterokinase in the duodenum; once active, it cleaves peptide bonds on the carboxyl side of lysine and arginine residues and also activates other pancreatic proteases. The other options aren’t involved in peptide bond hydrolysis in the small intestine: pepsin works in the stomach (acidic environment), amylase digests carbohydrates, and lipase digests fats.

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