Difference Between Trypsin and Chymotrypsin

Specificity: Trypsin hydrolyzes peptide bond at the C-terminal side of basic amino acids such as lysine and arginine, whereas chymotrypsin attacks the C-terminal side of aromatic amino acids like phenylalanine, tryptophan, and tyrosine. This is the main difference between these two enzymes.

1. What is the function of trypsin and chymotrypsin?
2. What is the role of chymotrypsin?
3. What is the difference between trypsin and pepsin?
4. Does trypsin activate chymotrypsin?
5. What is the meaning of chymotrypsin?
6. Where does chymotrypsin take action?
7. What foods contain chymotrypsin?
8. What are the products of chymotrypsin?
9. Is trypsin acidic or basic?
10. Why do we need pepsin and trypsin?
11. Why does trypsin not work in the stomach?

What is the function of trypsin and chymotrypsin?

Trypsin and chymotrypsin are important digestive enzymes that are secreted by the pancreas as the inactive enzyme precursors trypsinogen and chymotrypsinogen. Trypsin activates itself via positive feedback and converts chymotrypsinogen and other inactive enzymes into their active forms.

What is the role of chymotrypsin?

Description. Chymotrypsin is a digestive enzyme that breaks down proteins (i.e., it is a proteolytic enzyme; it can also be referred to as a protease). It is naturally produced by the pancreas in the human body. ... Its primary job is to produce enzymes required for the digestion and absorption of food.

What is the difference between trypsin and pepsin?

It is an enzyme secreted by pancreas. ... It is secreted as an inactive form known as trypsinogen. The one point difference between pepsin and trypsin is that pepsin is secreted in the stomach and acts only under acidic condition and trypsin is secreted in pancreas and acts under alkaline condition.

Does trypsin activate chymotrypsin?

Trypsinogen in pancreatic juice is initially activated by enterokinase to trypsin, after which it activates chymotrypsinogen to chymotrypsin, procarboxypeptidases to carboxypeptidases, proelastase to elastase, and the various prolipase enzymes to active lipases.

What is the meaning of chymotrypsin?

: a protease that hydrolyzes peptide bonds and is formed in the intestine from chymotrypsinogen.

Where does chymotrypsin take action?

Chymotrypsin is a digestive enzyme synthesized in the pancreas that plays an essential role in proteolysis, or the breakdown of proteins and polypeptides. As a component in the pancreatic juice, chymotrypsin aids in the digestion of proteins in the duodenum by preferentially cleaving peptide amide bonds.

What foods contain chymotrypsin?

The three main proteolytic enzymes produced naturally in your digestive system are pepsin, trypsin and chymotrypsin.
...
Food Sources

• Kiwifruit.
• Ginger.
• Asparagus.
• Sauerkraut.
• Kimchi.
• Yogurt.
• Kefir.

What are the products of chymotrypsin?

Chymotrypsin (EC 3.4. 21.1) is another serine protease produced by the pancreas that hydrolyzes the peptide bonds of tryptophan, leucine, tyrosine, and phenylalanine.

Is trypsin acidic or basic?

The purified trypsin belonged to an alkaline protease, as it was highly active between pH 8.0 and 10.0 with the optimum pH of 9.0.

Why do we need pepsin and trypsin?

For example, trypsin and pepsin are both enzymes in the digestive system which break protein chains in the food into smaller bits - either into smaller peptide chains or into individual amino acids. Pepsin works in the highly acidic conditions of the stomach.

Why does trypsin not work in the stomach?

Once it reaches small intestine, it is converted in active trypsin by enterokinase enzyme. Trypsin acts in alkaline medium and it is prevented from taking any damaging action on intestinal lining of lumen due to presence of protective mucus layer on it.