Pepsin

Pepsin is a protein that breaks down ingested proteins into smaller peptides to facilitate digestion. Pepsin is produced in the stomach and helps the body to absorb the proteins from the ingested foods. It is an endopeptidase that is produced in an inactive state and later hydrochloric acid (HCl) activates it inside the stomach. After pepsin has broken the ingested proteins into simpler or smaller proteins, other proteins in the intestine break them down further into smaller parts. Incidentally, pepsin is the first enzyme that was identified by scientists.

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A German physician Theodor Schwann discovered pepsin way back in 1836. However, this enzyme was not crystallized till nearly a century later - i.e. 1929. Finally, a biochemist named John Northrop crystallized pepsin.

The word pepsin has been derived from the Greek term denoting digestion, because this enzyme helps to digest the proteins present in the ingested foods. Precisely speaking, pepsin is basically a protease that has its origin in pepsinogen, which is released by the chief cells into the gastric juice that only occurs in the stomach. Pepsin is present in the stomach of all mammals and it has a crucial role in the initial stage of digestion, when the ingested food is broken down into simpler substances. During this course, pepsin helps to degrade proteins into peptides to facilitate the digestive process.

Normally pepsin is always found in the stomach only. However, when this enzyme is present in the mouth, throat, esophagus or the lungs it is said that pepsin has been refluxed.

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Ideally, pepsin works best when the environment is acidic (pH2). It is the active state of pepsinogen. Since pepsin is a very potent enzyme that easily digests all types of protein, it has the ability to even digest the stomach lining. This is because the lining of the stomach also comprises protein. Therefore, pepsin is released in an inactive form and it is only activated when it is needed. Moreover, the lining of the stomach is protected due to mucus, which forms a covering inside the stomach wall. It is worth mentioning here that protein is basically a polymer comprising sub units of amino acid and, hence, it can digest all types of proteins present in the ingested foods. For instance, it breaks down ingested meat into small particles of peptides and protease.

What are proteins? They are molecules made up of long amino acid chains. These amino acid chains are bound by peptide bonds. It an amino acid chain is a small one it is called peptide, while the longer chains are known as polypeptides. The linings of the intestines absorb the amino acids as well as small peptides and utilize them a fuel for the body. Alternatively, they can also be utilized as the building blocks of creating new proteins.

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Enzymes work as catalysts to make the reactions happen faster. Protease is also an enzyme that works to break down proteins into simpler substances more quickly. Pepsin too is a digestive protease that begins the breaking down process of proteins in the stomach.

Together with trypsin and chymotrypsin present in the small intestine, pepsin breaks down proteins present in the ingested foods. All these enzymes have specific responsibilities and work on specific targets and they only target proteins present in particular amino acids - for example, phenylalanine, tryptophan or tyrosine in the instance of pepsin.

However, it is important to protect the tissues that surround the stomach from damage and, hence, digestive protease is generated as zymogen - its inactive form.

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The zymogen or inactive form of protein is known as pepsinogen, which has an additional 44 amino acids bound to the molecule. Pepsinogen continues to be inactive till it is released into the gastric juices in the stomach, where it comes in contact with hydrochloric acid (HCl). In fact, pepsin and hydrochloric acid (HCl) are released separated into the stomach fluids and they remain separate until they also become constituents of the gastric juices in the stomach.

Production of gastric juice in the stomach is promoted by the smell or taste of food, which kindles gastrin production. As the name suggests, gastrin is a hormone found in the stomach. Hydrochloric acid (HCl) works to bring down the pH of the contents in the stomach dramatically to roughly about pH 1-3. When the environment becomes acidic, pepsinogen spreads out and separates its additional 44 amino acids. At this juncture, the enzyme is activated and it starts digesting the ingested proteins. At the same time, it also splits the remaining pepsinogen molecules and makes them active.

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Moreover, such an acidic environment also denatures the proteins and alters their three-dimensional structure, thereby helping the enzyme. This enables the digestive enzyme to access more peptides of the proteins and helps pepsin to further break them down in simpler substances. In this way, pepsin helps the body to digest the ingested proteins.

After the ingested foods are broken down into smaller substances in the stomach, they move into the small intestine. These partially cleaved products of pepsin are called polypeptides and still very large for the intestinal cells to absorb. Hence, these particles are broken down further by trypsin, chymotrypsin and other specific enzymes and turned into peptides. After the polypeptides are degraded into smaller peptides and amino acids, they are easily taken up by the cells in the intestine. Subsequently, these are utilized by the body as nutrients.

Pepsin is also produced from other sources and marketed commercially. This type of commercial pepsin is obtained from hog stomachs' glandular layers. It forms a constituent of rennet (a set of complex proteins produced in the ruminant animals' stomachs) and utilized to curdle milk in the process of cheese manufacture. Pepsin has various applications in the food industry. It is used to impart whipping quality and also modify soy protein as well as gelatine. In addition, pepsin is also used for modifying vegetable proteins for making non-dairy snacks and also to modify cereals cooked in advance into instantaneous hot cereals. Pepsin is also used to make vegetable and animal protein hydrolysates for preparing flavoring beverages and foods.

Aside from its applications in foods and beverages, pepsin has some industrial uses too. The leather industry uses pepsin to get rid of hair as well as residual tissue from animal hides. It is also used to recover silver from useless photographic films. Pepsin digests the gelatine layer that binds the silver on the photographic films. Historically, pepsin was used as an additive in the Beeman's chewing gum.

Health benefits and uses

Aside from its primary function of breaking down proteins into simpler substances, pepsin also has many other roles, which includes helping the body to absorb the nutrients present in the ingested food as well as eliminating microbes that are detrimental for our health. Digestive enzymes mainly work as catalysts in the various chemical reactions that take place in our body. All digestive enzymes actually transform the bigger molecules into smaller and simpler particles that can be absorbed by our body more easily and use them as fuel for survival and also to thrive.

People can take pepsin enzymes as they provide us with several benefits. Some of the benefits of taking pepsin enzymes are discussed briefly below.

Primarily pepsin helps the body to break down larger molecules of food, especially proteins, into simpler substances so that they are easy to absorb and use as nutrients. It also helps to cure leaky gut or indigestion by removing the stress from the digestive tract. At the same time, this hormone deals with pancreatitis that hinder the pancreas' ability to produce proper amounts of enzymes so that they are able to break down ingested foods effectively.

Pepsin also aids in producing antibodies as well as digest IgG. At the same time, it triggers production and secretion of bile. It works to detoxify the liver and helps to ease the symptoms related to heartburn, acid reflux and other problems such as irritable bowel syndrome. Moreover, pepsin improves the body's ability to absorb nutrients, thereby preventing nutritional deficiency, especially deficiency of iron, calcium and vitamin B12 in the body.

Among its other functions, pepsin naturally works to neutralize enzyme inhibitors in various foods like nuts, peanuts, seeds, potatoes, wheat germ, beans and egg whites. This hormone is also utilized for dealing with an assortment of health issues, including dyspepsia (which is discomfort or recurrent pain in the upper abdominal region), nausea, indigestion related to treatment of various forms of cancer, diarrhea and even vomiting caused by morning sickness in pregnant women.

While pepsin is a vital enzyme that offers numerous health benefits, dysfunction of pepsin may lead to more than a few digestive problems. Some of them are discussed briefly below.

Pepsin dysfunction often results in gastroesophageal reflux disease (also known as GERD) and laryngopharyngeal influx (also known as extraesophageal influx). These conditions occur when pepsin, acid as well as other substances in the stomach move up into the esophagus. In fact, pepsin can stay behind in the larynx after one has endured gastric reflux. When an individual is said to have laryngopharyngeal reflux, it denotes that pepsin as well as stomach acid have move up into the larynx.

Both GERD as well as laryngopharyngeal reflux events can result in uneasiness and they also have the potential to cause grave damages to the esophagus as well as the laryngeal mucosa. The common symptoms of these conditions include burning sensation in the chest, acid reflux, and chronic cough. In addition, one may also endure hoarseness and their vocal chords may contract voluntarily.

Moreover, pepsin enzymes possess the ability to stick to the laryngeal cells, thereby diminishing their ability to defence, and also wear away the membranes or tissues (known as endocytosis). When this occurs, it has the potential to enhance the chances of developing laryngeal and esophageal cancers.

To detect extraesophageal reflux, physicians examine the acidification by undertaking a pH rest and also by identifying the presence of pepsin in saliva as well as in exhaled breath. Studies hint that using proton pump inhibitors are not useful for many people who suffer from extraesophageal reflux.

While it is true that pepsin dysfunction is responsible for health problems like gastroesophageal reflux disease (GERD), but this condition may also occur when an individual's lower esophageal sphincter is feeble or it does not relax properly. Often, this happens due to obesity, hernias or even inflammation. Consequently, the contents of the stomach moves upwards into the esophagus. On many instances, one can get relief from GERD by taking healthy diet and making necessary changes in their lifestyle. These may prove to be helpful in reducing inflammation.

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