Question

Trypsin enzyme in mammals is formed from the
A Trypsinogen by action of enterokinase
B Trypsinogen by the action of protein
C Trypsinogen by the action of fat
D None of these

Answer 1

Trypsin is a serine protease belonging to the PA clan that hydrolyzes proteins in the digestive tract of many vertebrates. When the pancreas' proenzyme form, trypsinogen, is activated, trypsin is generated in the small intestine.

Complete answer:
The precursor form of trypsin, a digestive enzyme, is trypsinogen. Along with amylase, lipase, and chymotrypsinogen, it is produced by the pancreas and present in pancreatic juice. Enteropeptidase, which is located in the intestinal mucosa, cleaves it to its active form, trypsin.
When trypsin is activated, it can cleave additional trypsinogen into trypsin, a process known as autoactivation. Basic amino acids such as arginine and lysine have their peptide bonds cleaved by trypsin on the carboxyl side.
The proenzyme precursor of trypsin is trypsinogen. The dormant form of trypsin is kept in the pancreas and released when protein digestion is necessary. Because active trypsin would cause significant harm to pancreatic tissue, the pancreas maintains the inactive form of trypsinogen.
The pancreas, along with other digesting enzymes, releases trypsinogen into the second section of the duodenum via the pancreatic duct.

As a result, option A is right.

Additional information:
To guarantee that trypsin is only activated where it is needed, it is created, stored, and released as the inactive trypsinogen. Premature trypsin activation can be harmful, as it can set off a chain of events that result in pancreatic self-digestion.

Note: Around 5% of trypsinogen are thought to be triggered in the normal pancreas thus there are a lot of defences in place to prevent this.In the pancreas, trypsinogen is kept in zymogen granules, intracellular vesicles with membrane walls that are hypothesised to be resistant to enzymatic destruction.