The human digestive system is a fascinating set of digestive organs and enzymes working together. These organs along with important enzymes work together to help absorb and assimilate the food that we eat efficiently. Pepsin is concerned with breaking down different proteins in our food. The protein in our food is converted into amino acids and peptides by pepsin along with two other principal proteases of our body namely chymotrypsin and trypsin.
This enzyme was first discovered in 1936 by Theodore Schwann. Pepsin was named so after the Greek word Pepsis which literally means digestion. Refer to the official website of Vedantu or download the app for an elaborate and comprehensive explanation.
In the following article you will learn in detail about the following:
Sources of Pepsin
Structure of Pepsin
Characteristics of Pepsin
Classification of Pepsin
Working Mechanism of pepsin
Applications of Pepsin.
Pepsin is an endopeptidase enzyme that degrades proteins into peptides. It is formed in the chief cells of the stomach lining and is one of the most important digestive enzymes in humans and many other animals' digestive systems, where it aids in the digestion of proteins. Pepsin is an aspartic protease with an active site that contains a catalytic aspartate.
Pepsin enzymes are found in the stomach. Pepsin is a stomach enzyme that aids in the digestion of proteins in food. Pepsin is secreted by gastric chief cells as pepsinogen, an inactive zymogen. Hydrochloric acid is secreted by parietal cells in the stomach lining, which lowers the pH of the stomach. Pepsin is activated by a low pH (1.5 to 2).
Pepsin is a monomer (chain protein) made up of two folding domains that are separated by a deep cleft. Pepsin's catalytic site is formed at the domain junction, with two aspartic acid residues, Asp32 and Asp215, in each domain. The water molecule aids pepsin's catalysis by allowing the active carboxyl group to bear positive and negative charges with aspartic acid 215 and 32, respectively, breaking the peptide bond in the protein.
In acidic environments with a pH of 1.5 to 2.5, pepsin is most active. Pepsin works best at temperatures between 37 and 42 degrees Celsius. As a result, the stomach is the main site of synthesis and function (pH 1.5 to 2).
In humans, pepsin concentrations in the stomach range from 0.5 to 1 mg/mL. At pH 6.5 and above, pepsin is inactive, but it is not completely denatured or irreversibly inactivated until pH 8.0. As a result, re-acidification will reactivate pepsin in solutions up to pH 8.0. The safety of pepsin at high pH has important consequences for laryngopharyngeal reflux disease.
Following a gastric reflux case, pepsin persists in the larynx. Pepsin will be inactive at the mean pH of the laryngopharynx (pH = 6.8), but it may be reactivated during subsequent acid reflux events, causing damage to local tissues. Pepsin has a wide range of cleavage specificity.
Pepsin is expressed as a zymogen called pepsinogen, which has an additional 44 amino acids in its primary structure than the active enzyme.
Pepsinogen is generated by chief cells in the stomach. Hydrochloric acid (HCl), which is released from parietal cells in the stomach lining, activates this zymogen. When food is consumed, the hormone gastrin and the vagus nerve trigger the release of pepsinogen and HCl from the stomach lining.
The acidic environment produced by hydrochloric acid allows pepsinogen to unfold and cleave itself in an autocatalytic manner, resulting in the development of pepsin (the active form). To make more pepsin, pepsin cleaves the 44 amino acids in pepsinogen.
Pepsinogens are divided into five categories based on their primary structure: pepsinogen A (also known as pepsinogen I), pepsinogen B, progastricsin (also known as pepsinogen II and pepsinogen C), prochymosin (also known as prorennin), and pepsinogen F. (also called pregnancy-associated glycoprotein).
Pepsin is a proteolytic enzyme released by chief cells, which are specialized in the stomach. It is a component of gastric juice that aids in food digestion. Pepsin is a digestive enzyme that breaks down large polypeptides into smaller peptide fragments in the stomach's acidic environment (pH 1.5-2.5).
Pepsin preferentially hydrolyzes peptide bonds containing the aromatic amino acids' amine group (tryptophan, phenylalanine, and tyrosine). Pepsin is a stomach enzyme that aids in the digestion of proteins in food. Pepsin is secreted by gastric chief cells as pepsinogen, an inactive zymogen. Hydrochloric acid is secreted by parietal cells in the stomach lining, which lowers the pH of the stomach.
The function of pepsin in the stomach is to break down proteins in foods like meat and eggs into smaller pieces (polypeptides). It just breaks down proteins at specific stages, so the protein isn't fully digested to the amino acid level.
Pepsin can be used in the food industry.
Pepsin is found in pancreatic curd that condenses and twists during the processing of cheese.
Pepsin may be used to add whipping qualities to soybean protein and gelatin.
It can also turn pre-cooked cereals into instant hot cereals and change the plant protein used in non-dairy snacks.
Pepsin can also be used to make protein hydrolysates from animal and plant sources for seasoning food and beverages.
It is used in the leather industry to extract hair and residual tissue from leather, as well as to retrieve silver from the abandoned photographic film by digesting the gelatin layer that stores the silver.
Historically, it has also been used as medicine in the form of laxatives when combined with Senna. The first Pepsin syrup was sold in the 1800s. It is also used in Dr Pepper's pepsin Bitters.
It is used in medical research.
As can be seen, pepsin is a complicated enzyme with several uses in our digestive system. It is crucial for the healthy functioning of our digestive systems. Pepsin has a complicated structure and it has been classified into several subcategories. One must note that the role of pepsin is not only limited to digesting proteins in our food. The latest research shows that the functions of Pepsin are far more elaborate than was previously thought. Research shows that it also aids in the proper functioning of our immune system by digestive Nuclein acids. These acids are essential components of DNA and RNA.
Therefore it is essential to understand the working of the enzyme Pepsin as it is a fascinating enzyme with several crucial functions required for human life.
1. What is pepsin made of?
Pepsin is the mature active form of pepsinogen, which is an inactive protein. Pepsinogen is synthesized and secreted by chief cells (C) in the stomach, which combines with hydrochloric acid secreted by parietal cells to form pepsin (P). Pepsin is produced when pepsinogen reacts with hydrochloric acid. Pepsin is an endopeptidase enzyme that degrades proteins into peptides. It is formed in the chief cells of the stomach lining and is one of the most important digestive enzymes in humans and many other animals' digestive systems, where it aids in the digestion of proteins.
2. What is the source of pepsin and how is it prepared?
The mucous membrane of the ox (Bos taurus), sheep (Ovis aries), or hog (Sus scrofa) stomach is used to make pepsin. There are different methods to prepare pepsin which is mentioned as Pepsin is made by combining hydrochloric acid with minced stomach linings. This solution is clarified, partly evaporated, dialyzed, condensed, and either poured on glass plates to dry (scale pepsin) or carefully evaporated in a vacuum (spongy pepsin). Scale pepsin is made by digesting the mucous lining with about 0.2 per cent HCl (or water acidulated with other acids to the same degree of acidity) at about 100°C until the membrane is fully or nearly completely dissolved. Check out the Vedantu website or download the app for an easy explanation.
3. Why is pepsin important for our bodies?
Pepsin is an essential digestive enzyme in our bodies. Among the other two main proteases, it is the first enzyme to attack the protein that enters our bodies. Pepsin is essential for our digestive system and in turn our bodies as it helps break down proteins like eggs, meat, dairy, nuts, and seeds. The protein which is converted to peptides by pepsin is then absorbed in the small intestine. Without Pepsin, breaking down proteins is not done in our bodies. This is why people who do not have a lot of pepsin need to take supplements to ensure the proper digestion of proteins in their bodies.
4. What are some other benefits of pepsin?
Pepsin has several other benefits in addition to breaking down proteins in our food to amino acids and peptides. It also kills bad bacteria in the stomach. Another important function of Pepsin is to separate Vitamin B12 from the proteins that we eat and help it get properly utilized by our digestive system. Vitamin B12 is an essential vitamin for our bodies. Without Pepsin it won't be assimilated into our bodies. Recent studies have shown that Pepsin is also responsible for digesting nucleic acids which are components of DNA and RNA. It is therefore extremely beneficial in the growth and even the workings of our immune system.
5. Why is pepsin used by bodybuilders?
Bodybuilders take more protein than others to build lean muscle in their bodies. These bodybuilders want to absorb more protein into their bodies and get rid of excess fat. With this purpose in mind, they end up taking Pepsin supplements to ensure better assimilation of protein into their bodies. However, it must be noted that as of now there is no clinical data to show that Pepsin supplements aid in muscle building. But people with digestive problems, report positive results after taking such supplements.