Answer:
small intestine
Explanation:
The pancreatic juice that secretes the exocrine portion is formed by enzymes produced by the acini cells referred to earlier, and by an alkaline solution that is actively secreted by the duct cells. The alkaline solution is rich in sodium bicarbonate. Pancreatic enzymes are stored in acinar cells inside zymogen granules and released into the small intestine when necessary. The pancreas secretes a wide range of enzymes, which includes proteases, carbohydrases (pancreatic amylase and, in some cases, chitinase) and pancreatic lipase.
The three main proteases produced by the pancreas are trypsinogen, chymotrypsinogen and procarboxyaminopeptidase. As it is deduced from their names, they are inactive forms, which is how they are secreted. The reason for them to be stored like this is that, otherwise, they would digest the acini's own cellular proteins. Trypsinogen is activated once discharged into the duodenum due to the action of enterokinase, an enzyme found in the epithelial cells of the duodenal mucosa; It happens to be trypsin. It is active, autocatalytically, more trypsinogen. And it also does the same with the other two proteolytic zymogens, the chymotrypsinogen and the procarboxypeptidase. Each of these enzymes act on different bonds in the peptide chains resulting in a mixture of amino acids and small peptides. The intestinal epithelium is safe from the action of these proteases thanks to the protection provided by mucus secreted by cells of the intestine wall.
Pancreatic amylase degrades polysaccharides and converts them into disaccharides. That is, it acts in the same way as salivary amylase does. The other pancreatic carbohydrase is chitinase, although it is only present in fish and some seabirds. Chitin is a structural polysaccharide that is part of the cuticle of the arthropods and the fungal cell wall, fulfilling in these a function similar to that fulfilled by cellulose in plants.
