What is Trypsin?- Its role and uses

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What is Trypsin?

Trypsin is an enzyme found in the digestive system of human beings and animals. Trypsin is a serine protease that hydrolyzes proteins and helps in the digestion process.

What is Trypsinogen?

Trypsinogen is the proenzyme form of trypsin. It is secreted by the exocrine part of the pancreas.
It is converted into trypsin in the small intestine. When cholecystokinin stimulates the pancreas trypsin is secreted via the pancreatic duct into the duodenum, the first part of the small intestine. The enzyme enteropeptidase in the small intestine activates the inactive zymogen trypsinogen into active form trypsin by protease activity.

Function of Trypsin

In the first part of the small intestine, trypsin hydrolyzes the peptide bond mainly at the carboxyl part of the aminoacids. These amino acids are further hydrolyzed. The products are easily absorbed through the blood vessels into the blood.

Effect of pH on Trypsin

Pepsin which is also a protease works only in acidic pH of the stomach. its optimum pH is around 1.5. Likewise, Trypsin works in the alkaline nature of the small intestine, its optimal level of pH is about 8.

What does Trypsin do?

The protein cutting machinery consists of a collection of enzymes that contains serine protease for the protein cutting reactions. Trypsin, chymotrypsin, and elastase are collectively called protein scissors. They cleave the protein bonds and release the amino acids. Each one of these enzymes cut the proteins at specific places of amino acid. Namely the trypsin cleaves at the end of lysine and arginine. Chymotrypsin cuts near the large amino acids and phenylalanine. Elastase cleaves at small amino acids like alanine.

Trypsin inhibitors

Trypsin inhibitors in the pancreas provide defense against inappropriate activation of the trypsin which may cause high damage. Inhibitors of trypsin are serine protease inhibitors. It controls the catalytic activity of the trypsin by controlling the activation of the biological activity of trypsin, Trypsin inhibitors bind with the trypsin and so competes with the protein so that the protein cannot bind to trypsin. Trypsinogen ensures the protein part of the pancreas and the muscles are not damaged or broken down. These inhibitors are anti-nutritional factors as it interferes with the digestion. The natural sources of trypsin are soybeans, cereals, grain, legumes, etc. trypsin inhibitors provide protection for the accidental activation of trypsinogen and Chymotrypsinogen.

Examples of trypsin inhibitors: BPTI and SPINK1 in the pancreas and the α1-antitrypsin in the serum are the defense mechanism of inappropriate activation.

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Trypsin Digestion

There is a large set of processes that are required for structural biology and chemistry. If the protein sequence is unknown, we get the sequence via mass spectrometry (MS). The mass spectrometry is the most advanced and advantageous technique to find the protein structure and sequence of an unknown protein. Before getting the protein structure and the components of the protein there are several steps, one such is trypsin digestion (tryptic digestion). In mass spectrometry, one of the important steps is to chop up the proteins into small fragments when we have an unknown protein.

For breaking the proteins into fragments we require this step called the tryptic digestion. For digestion, we require the enzyme called trypsin. Proteins contain many bonds. It has a combination of amino acids. This enzyme trypsin cleaves the aminoacids from the backbone of the bonds that is the peptide bond. The trypsin enzyme attacks at the peptide bond. The peptide bond is formed by the carboxyl group of one amino acid and the amine group of the neighboring amino acid. this C-N bond is cleaved by many proteases like trypsin, pepsin, etc.

Uses in MS

In mass spectrometry (MS) we choose trypsin. Here is why we choose trypsin. First, we take the protein sequence and lyse it and we can run the gel electrophoresis to understand the molecular weight of the protein. Then we can isolate the fragment which carries the protein and we elude the protein out using gel elution . after eluding out we do the in-gel digestion. In the in-gel digestion, we take the gel of its own and apply the trypsin in that place. It cleaves the peptide bond and we get fragments of the peptide. After that, we take this peptide and load it into the Mass spec Analyser. and we can find the components and the different types of amino acids making the protein. we can look into the protein databases and look for the structural similarities.

Substrate specificity of trypsin

The specialty of the trypsin digestion is that it cleaves especially at two different amino acid sequences. It can only cleave after lysine and arginine. So that at the C terminal of all the fragments we get either lysine or arginine. There is an exception in the trypsin digestion if we have proline next to arginine or lysine the digestion does not take place. it creates a steric hindrance for digestion. this is the only exception in the trypsin digestion. And as of chymotrypsin, the end will have glutamic acid.

In case, if we use both trypsin and chymotrypsin all together in a single protein. It ensures that we get too different types of the fragment. After finding the sequence of all the fragment cleaved by different proteases again with mass spectrometry. we feed all the data into software and this software overlap and arrange the sequences in the way we get suitable overlaps using these overlapping sequences we can reconstruct the whole protein sequence and from this, we can create the protein structure using 2D and 3D with the help of specific software.

Therefore, trypsin digestion plays a very important role in finding the unknown protein and protein sequences.

Trypsin is prepared from the pancreas of the livestock. The people who lack the enzymes of digestion is prescribed with trypsin supplementations. It used in the treatment of osteoarthritis and others In combination with bromelain and rutin. It helps in skin healing and removes dead skin cells in wounds and ulcers. Trypsin allows healthy skin cells to grow. reduces swelling and inflammation in combination with other enzymes.

Other uses of trypsin:

• Respiratory infections caused by the workout.
• Diabetes mellitus.
• Enhancing digestion.
• Urinary tract infections like infections of the kidney, bladder, or urethra
• Multiple sclerosis (MS).
• Intestinal and rectal cancer.
• Sored muscle caused by exercise.
• Osteoarthritis.
• Damage to the skin provoked by radiation therapy or known as radiation dermatitis
• Sprains.
• Postsurgery swellings.
• Injury healing.
• Other conditions.

Note that there are no sufficient shreds of evidence for these uses.

Side effects of using trypsin

Firstly, when used on the skin

Some of the most common side effects, whenever you use any medicine to heal the wound, is the effects of pain and burning. Other than this the trypsin is possibly safe.

Secondly, when took orally

There is no adverse reaction of a drug with trypsin and other combination of the enzymes in almost all of the clinical studies. However, it is also no known whether it is safe to take it separately.

Precautions of taking trypsin

Avoid using it during pregnancy and breastfeeding. During these situations, the effects of trypsin are not known completely yet.

The dosage form of Trypsin

One should keep the appropriate dosage form of trypsin. We should take into consideration the patient’s well-being, age, and several conditions. However, consult with your doctor before using trypsin supplementations.

Reference: https://en.wikipedia.org/wiki/Trypsin

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