Introduction

Trypsin is a highly significant digestive enzyme in the human body. Its primary function consists of breaking down proteins into smaller components like amino acids in the small intestine.

It is one of the few enzymes secreted by the pancreas in an inactive form known as trypsinogen. Once it reaches the small intestine, it becomes active.

Among some of the most common enzymes, when mentioned with trypsin include chymotrypsin, which plays a role in protein digestion in the human body and also ensures the proper uptake of nutrition.

This article explores the function and activation of trypsin, and their clinical significance, particularly concerning the role it plays in the pancreas and digestive system, conditions that may arise with malfunction, and different uses of trypsin in medicine.

Role of Trypsin in Digestion

Trypsin is one of the digestive enzymes that actually cleaves large protein molecules into smaller peptides and eventually into amino acids.

The work of trypsin commences in the small intestine, where it acts on proteins that are partially digested beforehand by the enzyme pepsin in the stomach.

Trypsin is synthesized by the pancreas in an inactive precursor form called trypsinogen.

This mechanism ensures that the pancreas' proteins do not get digested by trypsin, which could damage tissue.

Once trypsinogen reaches the small intestine, the enzyme enteropeptidase, better known as enterokinase, decomposes trypsinogen into active trypsin.

Then trypsin activates other digestive enzymes like chymotrypsin and elastase, thus multiplying the process of protein digestion.

Activation of Trypsinogen

It is activated to become trypsin only when this enzyme has reached the small intestine; otherwise, it would damage the pancreas.

Trypsinogen, like all digestive enzymes, is secreted in an inactive state so that the pancreas is not lysed or digested by its own enzymes.

The small intestine may have trypsinogen, which is converted into trypsin by the action of enteropeptidase cleaving a particular peptide bond in trypsinogen.

This is an important step because trypsin not only degrades proteins into smaller peptides but also activates other enzymes from the proteolytic family, such as chymotrypsinogen, to further assist in digesting.

Trypsin and Chymotrypsin

Both trypsin and chymotrypsin are pancreatic secretions with important roles in protein digestion.

Trypsin acts on peptide bonds that have lysine and arginine. In its role, chymotrypsin acts on peptide bonds that contain the aromatic amino acids phenylalanine, tryptophan, and tyrosine.

These enzymes function simultaneously in the intestines to split proteins into smaller peptides that will later be split by other digestive enzymes to amino acids.

Since trypsin and chymotrypsin co-operate to digest proteins, amino acids can be appropriately broken down and absorbed by the body for utilization in myriad biological functions such as tissue repair, synthesis of enzymes, and energy metabolism.

The Pancreas and Enzyme Production

The pancreas is a large gland that produces trypsin and other enzymes found in the body digestive system.

It is positioned at the posterior side of the stomach and functions both exocrine and endocrine.

As an exocrine organ, the pancreas produces and secretes such digestive enzymes as trypsinogen, chymotrypsinogen, amylase, and lipase which are secreted to the small intestine through the pancreatic duct.

Apart from trypsinogen, the pancreas also produces bicarbonate, which neutralizes stomach acid when the latter enters the small intestine.

This creates an ideal pH environment for trypsin and other enzymes to function. The ability of the pancreas to regulate enzyme secretion is vital for digestion to occur properly in proteins, fats, and carbohydrates.

How Trypsin Works in Protein Digestion

Trypsin is an enzyme that hydrolyzes proteins by breaking specific peptide bonds.

Following activation in the small intestine, trypsin begins cleaving peptide bonds that include lysine and arginine. Their ultimate decomposition into smaller peptides then allows other enzymes to break them down to individual amino acids.

Proteins are large molecules that, if not for the action of enzymes like trypsin, they could not pass through and be absorbed by the small intestine.

The action of trypsin breaks proteins into smaller pieces in order that the amino acids needed for a myriad of biological processes can easily pass into the bloodstream for absorption.

Trypsin Inhibitors

Trypsin inhibitors are compounds that block the activity of trypsin, along with other proteolytic enzymes.

They occur naturally in foods such as soybeans and legumes and, through their impact on digestion, can be limiting or delay the digestive process wherein the activity of trypsin on proteins.

In such cases, if significant amounts of dietary trypsin inhibitors are present in the diet, the efficiency of the digestion and absorption of proteins is lowered, and the nutritional deficiency can be linked to this element.

This has given trypsin inhibitors relevance in medical science that could prevent the breakdown of proteins in certain pathological conditions.

For example, inflammation of the pancreas can be regarded as acute when the activation of trypsin takes place within the pancreas instead of the small intestine.

Since intracellular trypsin leads to inflammation of pancreatic tissue and associated tissues, the use of trypsin inhibitors would restrict damage to the tissues and lead to less inflammation.

Clinical Relevance of Trypsin

Malfunction or overactivation of the trypsin can lead to clinical conditions. One of the most difficult conditions linked with trypsin is acute pancreatitis.

It is an inflammatory disease in which autodigestion and marked inflammation of the pancreas take place because the trypsin inside the pancreatic tissue activates before its normal activation time in the small intestine.

Usually, trypsin is activated in the small intestine; however, in pancreatitis, it gets activated in the pancreas, where it digests itself and becomes highly inflamed.

Besides pancreatitis, elevated trypsin levels in the blood may be an indicator of damage or failure of the pancreas. Blood tests to measure the level of trypsin are often performed to confirm a diagnosis for pancreatic disorders.

Applications of Trypsin in Medicine and Research

Trypsin has been utilized highly in medical research and in different applications in clinics to facilitate protein and tissue degradation.

Amongst these applications is cell culture, which generally applies for the breaking loose of adherent cells from the surface of culture plates so cells can be collected for experimentation.

Apart from its application in researches, trypsin has been used for certain wound and burn treatments where dead tissue is removed and healing is promoted.

Trypsin being a proteolytic enzyme can be applied to remove necrotic tissue in wounds to assist with the regeneration of healthy tissue.

It is also used as an analytical agent in some diagnostic tests that may be associated with pancreatic functions. Since the pancreas secretes trypsin, activity or level of this enzyme can diagnose the state of the pancreas.

Trypsin and Other Digestive Enzymes

Trypsin itself is not one of the digestive protein breakdown enzymes alone.

Its function is supplementary to other digestive enzymes like chymotrypsin, carboxypeptidase, and elastase coming from the pancreas.

It breaks up various peptide bonds scattered within the proteins to guarantee the efficient proteolytic digestion.

Such cooperative action of trypsin and others with digestive enzymes illustrates how complex the digestive system is.

Each one has a specific role to play, and altogether they can break proteins into absorbable amino acids.

This is a multi-enzymatic process without which it is not possible to maintain appropriate nutrition and metabolic balance.

Regulation of Trypsin Activity

The action of trypsin is highly regulated so that it does not cause pathological effects within the pancreas and other tissues.

This is done by generating the zymogen, which is the inactive form of the enzyme, in this case, trypsinogen, so that the pancreatic proteins are not hydrolyzed before they reach the small intestine.

Upon entering the small intestine, this trypsinogen is activated by enteropeptidase, and the active trypsin activates other proteolytic enzymes.

This system of control is of extreme importance, preventing situations such as acute pancreatitis, in which tissue damage and inflammation result from an inappropriate early activation of trypsin inside the pancreas.

The proper balance between activation and inhibition of trypsin ensures proteins are broken down for use within the body but not tissues of the body are destroyed.

Conditions Resulting from Lack of Control over Trypsin

Besides acute pancreatitis, there are other conditions related to abnormal trypsin activity. The one example is genetic mutation of the PRSS1 gene that encodes for trypsinogen.

It causes hereditary pancreatitis and is characterized by recurrent inflammatory and damaging episodes in the pancreas due to an auto-digestive effect of uncontrolled activation of trypsinogen into trypsin within the pancreas.

This is another disorder of the malfunction of trypsin, which is cystic fibrosis. This is when thick mucus secretion blocks the pancreatic ducts, meaning such a patient cannot release digestive enzymes, like trypsin, into the small intestine.

Such a patient undergoes malabsorption and nutritional deficiency because the proteins are not well digested.

Conclusion

The enzyme that can participate in the process of breaking down proteins into smaller peptides and, finally, amino acids by the walls of the small intestine is trypsin.

It is synthesized by the pancreas as a zymogen called trypsinogen and activated in the small intestine.

Trypsin, along with chymotrypsin and other digestive enzymes, plays an important role in the digestion and absorption of dietary proteins.

Even though trypsin forms part of the digestive process, it is also pretty relevant in other areas- such as studies and clinical practice for being applied in cell culture or wound healing but malfunction on its part and that of its activity leads to conditions such as pancreatitis or cystic fibrosis which can be very deleterious to health.

An understanding of the role of trypsin and regulation of this process is fundamental for maintaining digestive health as well as for therapeutic strategy development in disorders involving this key enzyme.

* Medical Disclaimer - The following information is for educational purposes only. No information provided on this website, including text, graphic, and images, are intended as substitutes for professional medical advice. Please consult with your doctor about specific medical advice pertaining to your condition(s).