Trypsin is an enzyme that is produced in the pancreas and is of great importance for the digestion of humans. It activates other digestive enzymes from the pancreas in the gut, which in turn further break down proteins that are ingested with food. These can then be taken up in the further course of the passage through the intestine. Thus, trypsin as an activator for various digestive enzymes is important for the absorption of proteins.
Trypsin is produced in the pancreas and is an enzyme responsible for activating other digestive enzymes from the pancreas. These are mainly chymotrypsin, elastase and carboxypeptidase. Thus, trypsin triggers an activation cascade, which is crucial for the digestion of proteins from food. In case of a deficiency it comes therefore to serious disturbances in the body and above all in the large intestine to the putrefaction.
The enzymes that activate trypsin can, in turn, break down proteins from food and break them down into so-called oligopeptides. These can then be absorbed more easily in the small intestine and transported via the circulation to various locations in the body. Above all, the body needs the protein components to make its own proteins. These are used, for example, for the body structure in the form of skin, connective tissue, muscle or bone. But also as hormones, antibodies for the immune system or for oxygen transport, the body needs proteins.
As an enzyme, trypsin has specific properties in terms of the way it cleaves proteins. It is a so-called endopeptidase, meaning that it binds peptide bonds, that is, the bonds between individual amino acids (which make up a peptide or protein) within the protein.
In addition to the main task of digestion, trypsin can also reduce pain that occurs, 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 happens because trypsin activates other enzymes, such as plasmin, which in turn dissolve fibrin and thus dissolve the cohesive network of platelets
Trypsin is an enzyme that tends to cleave other proteins. Therefore it is important that this function does not already come into force at the place of manufacture, ie the pancreas. To prevent this, trypsin is produced in an inactive precursor. This precursor is also called a proenzyme and in the case of trypsin is the trypsinogen.
During ingestion, the inactive precursor trypsinogen is released from the pancreas and activated in the small intestine. This is done by another enzyme called entereopeptidase. In the process, parts of the trypsinogen are split off, resulting in the active form trypsin.
In the diagnosis of some diseases, such as cystic fibrosis, it is important to measure trypsin levels in the human body. For this purpose, the amount of trypsinogen in the body can be determined, because this is directly related to the amount of available trypsin.
Antitrypsin is a so-called protease inhibitor. This means that antitrypsin is able to prevent trypsin from fulfilling its mission and splitting proteins. This is especially important for the comminution of proteins in the blood.
Antitrypsin is usually referred to as alpha-1-antitrypsin, since it is detectable in a detection method (protein electrophoresis) in the so-called alpha-1 fraction. It is produced largely in the liver and is important to prevent excessive inflammation in the body by inhibiting various enzymes, such as trypsin, plasmin, or thrombin. In the case of a deficiency, serious impairment of the liver but also of the lungs occurs.
Trypsin inhibitors are peptides that prevent trypsin from exerting or limiting its action in the gut. This trypsin is blocked and can not fulfill its role as an activator of other digestive enzymes in the gut.
Trypsin inhibitors are found in various foods. One known representative is soybeans which contain crude inhibitors of trypsin inhibitors. Consumption of raw soybeans may therefore interfere with protein digestion in the intestine. To prevent this, the soybeans should be boiled before consumption as this will inactivate the trypsin inhibitors. For soybean meal, it should be ensured that it has undergone a roasting process, as it also eliminates the trypsinin inhibitors. Otherwise, digestive problems could occur.
To determine the trypsin value, a blood sample is needed. From this, the amount of trypsin present in a medical laboratory can be determined.
The value is between 10 and 57 μg per liter of blood in a healthy person.
In general, the trypsin value is determined if it is suspected that an acute inflammation of the pancreas, so a pancreatitis, could be present. For this, however, other parameters should be determined, such as the elastase value.
If the level of trypsin in the blood is increased, this means that either an excessive amount of the digestive enzyme is released from the pancreas or too little trypsin is excreted from the body after it has performed its function.
Excessive secretion of trypsin can be caused by acute inflammation of the pancreas, pancreatitis. But it can also be a boost of chronic, so longer existing, pancreatitis. Furthermore, a tumor of the pancreas or a cystic pancreatic fibrosis in the context of cystic fibrosis may be considered as possible causes. If one of these diseases is suspected, further parameters of the pancreas should be evaluated for clarification.
Another possible cause of the increase in trypsin is renal insufficiency. This disease should be clarified further in case of suspicion.
Since trypsin is a crucial component of the activation cascade for digestive enzymes in the gut, deficiency leads to inadequate digestion and uptake of proteins from the diet.
The lack of absorption of dietary protein leads to the loss of weight and deficiency symptoms due to missing proteins in the human body. In addition, there is a so-called intestinal decay with an accumulation of nitrogen-containing compounds. This can also be recognized by meat fibers in the stool.
Trypsin, like most other digestive enzymes, can only work 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 can no longer be effective enough and, as a consequence, the absorption of proteins from the diet can be disrupted.
Trypsin, like many other digestive enzymes, is produced in the pancreas, more specifically, 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 in an active form, which in turn can then activate other digestive enzymes.