
The trypsin enzyme is secreted by
(a)Stomach
(b)Duodenum
(c)Pancreas
(d)Liver
Answer
585.3k+ views
Hint: Trypsin is an enzyme that catalyzes the catabolism of proteins as it acts on proteins and breaks them into simpler forms. The organ which secretes this enzyme has two main functions; an exocrine function that helps in digestion and an endocrine function that regulates blood sugar.
Complete answer:
The pancreas is a compound of both exocrine and endocrine glands; it is an elongated organ situated between the limbs of the U-shaped duodenum. Pancreatic juice mostly contains inactive enzymes that get activated in the small intestine. Trypsinogen, chymotrypsinogen, procarboxypeptidase are some of the inactivated enzymes secreted in pancreatic juice.
Trypsinogen is activated by an enzyme, enterokinase secreted by intestinal mucosa into active trypsin which successively activates the opposite enzyme in pancreatic juices. Trypsin is a proteolytic enzyme that cleaves peptide chains. Proteins, Proteoses, and peptones in the chyme (bolus) reaching the intestine are acted upon by proteolytic enzymes of pancreatic juice.
Tryptic digestion is necessary for protein absorption as protein is last to be absorbed through the small intestine. Human trypsin has an optimal temperature of about 37° C and optimum pH of 7.1 to 8.3.
If trypsin is inadequate i.e. pancreas doesn’t produce enough trypsin one can experience protein malabsorption and decreased ability to digest food which can lead to anemia and malnutrition.
So, the correct answer is, “Pancreas.”
Note: Trypsinogen is secreted by the pancreas and is activated into active trypsin by the intestinal mucosa. In predatory animals, trypsin can hydrolyze fibrinogen of blood into fibrin leading to coagulation of blood but it is unable to bring about coagulation of milk. Also, trypsin cannot hydrolyze keratin which is a type of protein.
Complete answer:
The pancreas is a compound of both exocrine and endocrine glands; it is an elongated organ situated between the limbs of the U-shaped duodenum. Pancreatic juice mostly contains inactive enzymes that get activated in the small intestine. Trypsinogen, chymotrypsinogen, procarboxypeptidase are some of the inactivated enzymes secreted in pancreatic juice.
Trypsinogen is activated by an enzyme, enterokinase secreted by intestinal mucosa into active trypsin which successively activates the opposite enzyme in pancreatic juices. Trypsin is a proteolytic enzyme that cleaves peptide chains. Proteins, Proteoses, and peptones in the chyme (bolus) reaching the intestine are acted upon by proteolytic enzymes of pancreatic juice.
Tryptic digestion is necessary for protein absorption as protein is last to be absorbed through the small intestine. Human trypsin has an optimal temperature of about 37° C and optimum pH of 7.1 to 8.3.
If trypsin is inadequate i.e. pancreas doesn’t produce enough trypsin one can experience protein malabsorption and decreased ability to digest food which can lead to anemia and malnutrition.
So, the correct answer is, “Pancreas.”
Note: Trypsinogen is secreted by the pancreas and is activated into active trypsin by the intestinal mucosa. In predatory animals, trypsin can hydrolyze fibrinogen of blood into fibrin leading to coagulation of blood but it is unable to bring about coagulation of milk. Also, trypsin cannot hydrolyze keratin which is a type of protein.
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