Courses
Courses for Kids
Free study material
Offline Centres
More
Store Icon
Store

Proteases

Reviewed by:
ffImage
hightlight icon
highlight icon
highlight icon
share icon
copy icon
SearchIcon

What is Protease?

There are different enzymes produced by our gastrointestinal system and in cells for the various biochemical functions. One such type is a protease. It is a genre of protein-digesting enzyme found in different chemical shapes. In this article, we will study the different types of proteolytic enzymes and their respective functions.

The enzyme that reduces the complex protein molecules into smaller chains of polypeptides (amino acids) for easier assimilation is called protease. A protease enzyme catalyzes and breaks down the peptide bonds present in bigger protein molecules to reduce them into constituent amino acids. It is a process of digestion that takes place in our stomach and small intestine.

There are different kinds of protein-digesting enzymes with distinct functions. This type of enzyme can also be found in other primitive and advanced animals. The most essential function is to digest and break down protein into smaller units for easier assimilation.

(image will be updated soon)

Types of Protease Enzyme

The proteolytic enzymes list can be segmented into three broader groups in terms of their mechanism and site of action.

  • Endopeptidase

This type of proteolytic enzyme acts on the peptide bonds presents internally in the protein molecules. It helps in breaking down macromolecules of protein by dissociating the internal peptide bonds to form smaller polypeptide units. example - trypsin, pepsin, elastase, chymotrypsin, etc.

  • Exopeptidase

This type of protease enzyme acts on the terminal peptide bonds and dissociates the amino acids present at the end of protein molecules. Example - carboxypeptidases, aminopeptidases, etc.

  • Oligopeptidase

According to its protease definition, this enzyme acts on specific amino acid bonds in a protein and performs catalysis.

Mechanism of Action of Protease

As mentioned earlier, the proteolytic enzymes act on the peptide bonds in a protein molecule and hydrolyze them to form smaller polypeptide molecules for absorption. The process is facilitated by activating a water molecule in the peptide bond and then catalyzing it to break.

The protease function depends on the mechanism of action. For instance, cysteine, serine, and threonine hydrolyzing enzymes form an acyl-enzyme as an intermediate and then hydrolyze in presence of water to get the product. The enzymes in this action are set free once the hydrolysis is done.

Apart from digestive enzymes, there are proteases taking part in other biochemical reactions. For instance, thrombin participates in blood clotting reactions. On the other hand, trypsin cleaves protein molecules to form smaller molecules of polypeptides for easier absorption in the digestive system.

The digestion of protein present in our diet takes place in different phases considering the locations. Pepsin is one of the proteolytic enzymes examples present in gastric juice. It comes out as pepsinogen, an inactive form of this enzyme. Due to the acidic environment in the stomach, it gets converted into pepsin by the influence of HCl. The partial hydrolysis of protein takes place in the stomach to form peptones.

Peptones then reach the small intestine where the proteases act in an alkaline environment. The bile salts convert the acidic chyme of the stomach into an alkaline one. In this environment, the inactive precursors such as trypsinogen, chymotrypsinogen, and procarboxypeptidase are activated to form trypsin, chymotrypsin, and carboxypeptidase respectively. Trypsin functions as a precursor to activate other proteolytic enzymes and the rest of the protein digestion take place.

In the small intestine, peptones, proteoses, and protein macromolecules are then digested to form polypeptide molecules. This process can also take place further to dissociate polypeptides to produce amino acids. Dipeptidase is an enzyme that functions as a hydrolytic agent to produce amino acids.

Application of Protease Enzyme

These enzymes are highly essential for the digestion of protein to produce absorbable polypeptides. These polypeptides are used in different biological processes.

The applications of proteases are:

  • The breakdown of protein into polypeptides is done by the proteolytic enzymes in the digestive system of higher-order animals. These enzymes can be found in unicellular animals performing the same function at the cellular level.

The catabolic process leads to the formation of amino acids. These structural units of protein are used for creating specific proteins according to the need of cells.

  • Specific proteases are required to conduct blood coagulation.

  • These enzymes are also used in the growth, cell division, migration, and apoptosis.

  • Another important function of these enzymes is to recycle protein and to produce smaller units for easier transportation through the cell membranes.

  • Some of the proteases act as precursors for other proteolytic enzymes. Some activate precursor zymogens and proteins.

  • They also regulate tumor growth, inflammation, and metastasis and support the immune system.

  • They also aid in healing wounds and cure soreness in muscles.

This is all you need to know to answer what is proteolytic enzyme. Study the different types of proteases and their specific functions with examples. Find out the locations of secretion of these enzymes and correlate with their functions.  

FAQs on Proteases

1. What is an enzyme?

An enzyme is a complex biochemical substance produced and secreted in the different organ systems to conduct a catalytic process. This substance has the specific function of targeting a biochemical reaction and regulating it. During the process, the reactants transform into different compounds but the enzymes do not change. They are again used in the same reactions when needed.

2. Where is protease produced?

The function and mechanism of action of proteases define their site of production. For instance, peptidase is produced in the ileum wall of the small intestine. It is used in the digestion of protein. Pepsin is produced by the gastric glands present in the stomach and is used to reduce protein molecules into simpler peptones. Thrombin, on the other hand, is produced in the hepatic cells in the form of prothrombin as an inactive substance. It is activated and used for blood coagulation.

3. Why proteases do not digest cell membranes at the site?

They are produced in an inactive form in the respective sites and then carried elsewhere. In other cases, the protective mucosal layer of the cells protects them from self-digestion.