Concept:Proteases are secreted as inactive zymogens (proenzymes) to prevent them from digesting the organs that synthesize them. They require a specific activator in the gut.
Formula:$$ \text{Trypsinogen (inactive)} \xrightarrow{\text{Enterokinase}} \text{Trypsin (active)} $$
Solution:- Trypsinogen is produced by the pancreas and released into the duodenum.
- The mucosal cells of the duodenum secrete an enzyme called enteropeptidase (also known as enterokinase).
- Enterokinase cleaves a specific peptide bond in trypsinogen, converting it into the highly active protease, trypsin.
Why other options are incorrect:HCl activates pepsinogen in the stomach, not trypsinogen in the intestine. Glucokinase phosphorylates glucose. Amylase digests starch.
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