Trypsin: Definition, Function, Inhibitors, Values, Clinical Uses, Side Effects and Interactions

It belongs to the so-called endopeptidases and is secreted by the pancreas to aid in the digestion of food.

Trypsin splits protein molecules at specific sites within the protein chain.

Because trypsin is highly proteolytic, the pancreas secretes an inactive form of this enzyme ( trypsinogen ) in the small intestine, where enterokinase cleaves the N-terminal hexapeptide and activates the enzyme.

Like most other digestive enzymes, trypsin can only function properly at a certain pH.

The optimal pH range for trypsin is between 7 and 8, which corresponds to the pH range in a healthy person in the small intestine.

If this range changes, trypsin may no longer be compelling enough, and, consequently, protein absorption from the diet may be impaired.

Trypsin is most effective on partially digested proteins. It also digests some proteins, such as protamines and histones, which cannot be digested by pepsin.


The products of trypsin digestion are amino acids and various polypeptides.

A rare inherited trypsinogen deficiency has been reported resulting in significant impairment of protein digestion.

Symptoms include severe growth inhibition, hypoproteinemia, edema, and diarrhea.

Evaluation of pancreatic enzymes in such cases reveals a complete absence of trypsinogen. In addition, elevated serum levels of trypsin are found in individuals with cystic fibrosis.

Trypsin is a serine protease that selectively cleaves after the peptide bonds of the intestinal region after the amino acids lysine and arginine and modified cysteine.

Unlike most enzymes, proteinases are not specialized for specific proteins but rather for certain structural features of proteins.

This is especially important for the digestive process, as the small intestine would otherwise need its digestive enzyme for each type of protein.

Furthermore, endopeptidases are an essential tool in the chemical analytical sequencing of proteins.

Cut (denatured) proteins are easily hydrolyzed; they combine with water at the free ends to bind water molecules.

This increases the surface area of ​​the food eaten and speeds up the digestive process in a self-reinforcing mechanism.

A similar function and effect have released pepsin from the stomach wall.

The pancreas secretes the proteases trypsin, chymotrypsin, and carboxypeptidases as inactive zymogen precursors.

The intestinal enteropeptidase enzyme, bound to the intestinal epithelium, controls the conversion of the precursor trypsinogen to trypsin.

Trypsin becomes activated (positive feedback) and, in turn, converts chymotrypsinogen, proelastase, procoxypeptidase, and other inactive enzymes to their active forms (chymotrypsin, elastase, and carboxypeptidase).

Therefore, trypsin triggers an activation cascade, which is crucial for the digestion of food proteins. In case of deficiency, severe disorders occur in the body, especially in the large intestine, in putrefaction.

Trypsin function

Trypsin is an enzyme that acts to degrade proteins. It is often called a proteolytic enzyme or proteinase.

Trypsin is one of the three principal digestive proteinases, the other two being pepsin and chymotrypsin.

In the digestive process, trypsin works with the other proteinases to break down dietary protein molecules into their component peptides and amino acids.

Trypsin is an enzyme produced in the pancreas and is of great importance for the digestion of humans.

It activates other digestive enzymes of the pancreas in the intestine, which break down proteins eaten with food.

These can be retaken in the subsequent course of passage through the intestine. Therefore, trypsin as an activator of various digestive enzymes is essential for protein absorption.

Trypsin continues the digestion process (which begins in the stomach) in the small intestine, where a slightly alkaline environment (approximately pH 8) promotes its maximum enzyme activity.

Trypsin, produced inactively by the pancreas, is remarkably similar in chemical composition and structure to the other major pancreatic protease, chymotrypsin.

Both enzymes also appear to have similar mechanisms of action; Histidine and serine residues are found at the active sites.

The main difference between the two molecules appears to be in their specificity; each is active only against peptide bonds in protein molecules that have carboxyl groups donated by specific amino acids.

For trypsin, these amino acids are arginine and lysine; for chymotrypsin, they are tyrosine, phenylalanine, tryptophan, methionine, and leucine.

Trypsin is the most discriminating of all proteolytic enzymes regarding the restricted number of chemical bonds it will attack.

Chemists interested in determining the amino acid sequence of proteins have used this fact well.

Trypsin is widely used as a reagent for such molecules’ orderly and unambiguous cleavage.

The enzymes that activate trypsin can, in turn, break down proteins in food and break them down into so-called oligopeptides.

These can be more easily absorbed in the small intestine and transported through the circulation to various bodily places.

The body needs protein components to make its proteins.

These are used, for example, for the body’s structure in the form of skin, connective tissue, muscle, or bone. But also like hormones, antibodies for the immune system, or oxygen transport, the body needs proteins.

Trypsin dissolves adherent cells from the bottom of culture dishes or separate compartments in cell culture laboratories.

As long as cells are not trypsinized for too long, they will not be damaged, and only extracellular proteins will divide.

In addition to the main task of digestion, trypsin can also reduce pain, for example, in the context of arthritis.

Furthermore, it plays a role in the degradation of various complexes in autoimmune diseases and can prevent excessive platelet aggregation. The latter occurs because trypsin activates other enzymes, such as plasmin, which dissolves fibrin and the cohesive platelet network.


Trypsin is an enzyme that tends to cleave other proteins. Therefore, this function mustn’t take effect at the place of manufacture, that is, in the pancreas.

To avoid this, trypsin is produced in an inactive precursor. This precursor is also called a proenzyme, and in the case of trypsin, it is trypsinogen.

During ingestion, the inactive precursor trypsinogen is released from the pancreas and becomes activated in the small intestine.

This is done by another enzyme called entereopeptidase. In the process, parts of the trypsinogen are separated, resulting in the active form of trypsin.

In diagnosing some diseases, such as cystic fibrosis, measuring trypsin levels in the human body is essential.

For this purpose, the amount of trypsinogen in the body can be determined, as this is directly related to the amount of trypsin available.


Antitrypsin is a protease inhibitor. This means that antitrypsin can prevent trypsin from doing its job and breaking down proteins.

Antitrypsin is generally known as alpha-1-antitrypsin, as it is detectable in a detection method (protein electrophoresis) in the so-called alpha-1 fraction.

It is produced mainly in the liver and is essential to avoid excessive inflammation in the body by inhibiting various enzymes, such as trypsin and plasmin.

In the case of a deficiency, there is severe deterioration of the liver and lungs.

Trypsin inhibitors

Trypsin inhibitors are peptides that prevent or can restrict trypsin from developing its effect in the intestine.

If trypsin is blocked, it cannot fulfill its function as an activator of other digestive enzymes in the intestine.

Trypsin inhibitors are found in various foods.

A well-known representative is soybeans, which contain crude inhibitors of trypsin inhibitors.

Raw soybeans can therefore be used to disturb the digestion of proteins when they reach the intestine.

To avoid this, soybeans should be boiled before consumption, which will inactivate the trypsin inhibitors.

For soy flour, you must ensure that it has undergone a roasting process as it removes trypsin inhibitors. Otherwise, digestive problems could occur.

Trypsin laboratory values

To determine the trypsin value, a blood sample is needed. The amount of trypsin present can be determined by laboratory analysis.

N-benzoyl-D can detect trypsin activity, L-arginine-p-nitroaniline, it is cleaved by arginine trypsin, and p-nitroaniline is formed.

The concentration of p-nitroaniline can be detected spectroscopically at a wavelength of 410 nm.

The value is between 10 and 57 μg per liter of blood in a healthy person.

In general, the trypsin value is determined if an acute inflammation of the pancreas is suspected – pancreatitis.

However, other parameters must be determined, such as the elastase value.

high trypsin

If the value of trypsin in the blood increases, there is already an excessive amount of the digestive enzyme in the pancreas.

Excessive trypsin secretion can be caused by acute pancreas inflammation or pancreatitis. But it can also be an impulse from chronic pancreatitis, which has been around for longer.

Also, a pancreas tumor or cystic fibrosis tumor can be considered a possible cause.

If one of these diseases is suspected, other parameters of the pancreas should be evaluated to clarify them.

Another possible cause of increased trypsin is kidney failure.

Low trypsin

Since trypsin is a crucial component of the digestive enzyme activation cascade in the gut, deficiency leads to poor digestion and absorption of protein from the diet.

Lack of protein absorption in the diet leads to weight loss and deficiency symptoms due to a lack of protein in the human body.

Also, there is a so-called intestinal breakdown with a build-up of nitrogen-containing compounds. The meat fibers can also recognize this in the stool.

Trypsin preparation

Like many other digestive enzymes, trypsin is produced in the pancreas, specifically in the exocrine part of the pancreas.

There, it is first released as a proenzyme trypsinogen and then converted in the small intestine by the enzyme entereopeptidase into an active form, which in turn can activate other digestive enzymes.

Trypsin is an enzyme whose commercial preparations are derived from animal sources such as the ox pancreas.


Trypsin is used orally as a digestive enzyme supplement with amylase, lipase, and other proteases.

It is also used with bromelain and other compounds to treat osteoarthritis.

Trypsin is also topically used to clean wounds and ulcers and remove necrotic tissue debris.

Prescription aerosol products with trypsin, balsam of Peru, and castor oil are used topically for enzymatic debridement and promote the healing of necrotic wounds and ulcers of the oral mucosa.

These compounds are Proteinase, Proteolytic Enzyme, Trypsin, Trypsin, Trypsin.

Side effects

Trypsin has proven very safe when used topically by medical professionals for wound debridement.

There is insufficient information on the safety of trypsin for its other uses.

There is also no information on side effects during pregnancy or lactation, so its use should be under the strict supervision of a doctor.

Topically, possible side effects associated with trypsin include transient burning and localized pain.


There are no known drug interactions, nor are there any known supplement, herb, or food interactions for trypsin.


The correct dosage of any supplement requires a thorough analysis of many factors, including your age, gender, health conditions, DNA, and lifestyle.

Oral use

For osteoarthritis, a combined enzyme product (Phlogenzym) containing rutin 100 mg, trypsin 48 mg, and bromelain 90 mg has been administered as two tablets daily.

Topical use

Wound debridement products (Dermuspray, Granulderm, Granules, and GranuMed) containing trypsin, balsam of Peru, and castor oil are FDA-approved as prescription drugs.