Question

The main digestive function of enterokinase is

• A. Conversion of casein into paracasein
• B. Conversion of pepsinogen into pepsin
• C. Conversion of trypsinogen into trypsin
• D. Stimulation of gastric glands to secrete gastric juice

Answer 1

The Correct Option is C

Answer (c) Conversion of trypsinogen into trypsin

Answer 2

Ans. Trypsinogen, chymotrypsinogen, and procarboxypeptidase are the inactive zymogen forms in which the pancreatic proteolytic enzymes are released. Trypsinogen is activated by the enzyme enterokinase, which turns it into trypsin. Trypsin activates procarboxypeptidase and chymotrypsinogen. The duodenal mucosa secretes enterokinase.

The duodenal mucosa secretes enterokinase, also known as enteropeptidase, a proteolytic enzyme that converts the inactive pancreatic secretion trypsinogen into trypsin, one of the enzymes that break down proteins. It is thought that the glands of Brunner in the membrane lining of the duodenum generate enterokinase. The different enzymes in the small intestine do not break it down, but microorganisms in the large intestine do. Procarboxypeptidase, an inactive enzyme, can also be converted by enterokinase into carboxypeptidase, an active enzyme.

• The enzyme of intestinal juice is what enterokinase does.
• necessary for trypsin activation, also known as enteropeptidase
• It can be found in the epithelial cells that line the duodenal mucosa's brush edge.
• They are more easily released into the intestinal lumen thanks to bile salts.