What’s the chymotrypsin?
Chymotrypsin is an enzyme that plays a role in digestion in the human body. As an enzyme, it has the task of breaking down proteins from food and breaking them down into small components – so-called oligopeptides – which can then be absorbed in the intestines. Chymotrypsin is produced in the pancreas and, along with other digestive enzymes such as trypsin, pepsin or carboxypeptidases, plays an important role in the absorption of proteins.
Function of the chymotrypsin
Chymotrypsin is an enzyme from the pancreas, which is responsible for breaking down and splitting proteins ingested with food. In this process, the proteins are split into so-called oligopeptides (composition of less than 10 amino acids) so that they can then be more easily absorbed through the mucous membrane in the small intestine and can be brought into circulation. This enables the body to absorb important components from protein-containing foods such as nuts, wholemeal bread, poultry or fish.
This in turn is important so that the body can build its own proteins from them. These include hormones and antibodies for the immune system, but also proteins for blood clotting, muscle building, hair and nails. Chymotrypsin is an endopeptidase.
Endopeptidases are enzymes that are responsible for splitting bonds between the individual amino acids, the peptide bonds. This enables proteins from food to be broken down into peptide fragments. These are then further split by other peptidases into the individual amino acids.
As an endopeptidase, chymotrypsin belongs to the group of serine proteases. This means that the amino acid serine is located in what is known as the active centre, i.e. the main work site of the enzyme. This amino acid has a specific group (hydroxy group) that is important for the cleavage of a peptide bond.
The proteins that chymotrypsin breaks down are always cleaved at certain positions in the sequence of amino acids. These are the so-called aromatic amino acids phenylalanine, tryptophan and tyrosine. In medicine, the splitting function of chymotrypsin also plays a role in the breakdown of immune complexes that could damage the body.
In addition, chymotrypsin can also help relieve inflammation or pain of the musculoskeletal system. It reduces classic signs of inflammation, such as swelling or local redness of the skin. Occasionally, it is also used as a mucolytic agent for pneumonia or asthma.
What forms of chymotrypsin are there?
Chymotrypsin is ultimately a family of different forms. They all have in common that they are serine proteases from the pancreas. First of all, a distinction must be made between the inactive and the active form.
In the pancreas, an inactive precursor (a so-called zymogen) of chymotrypsin is first produced, which is called chymotrypsinogen. If this is released from the pancreas and reaches the small intestine, it can be split by trypsin, another enzyme from the pancreas, and converted into the active chymotrypsin. In this process the chymotrypsinogen is broken down into three parts.
Furthermore, chymotrypsin A, B1, B2 and C can be differentiated. The most relevant forms for the human body are chymotrypsin B1 and chymotrypsin B2. The form chymotrypsin C was discovered in the pancreas of pigs lacking the B-form.
The various forms of chymotrypsin are all serine proteases, with the amino acid serine in the active centre (where the main activity of the enzyme takes place). The differences between the forms are in the structure, the sites where the proteins are cleaved (cleavage or substrate specificity), and the activity. The precursor chymotrypsinogen is inactive and not able to cleave proteins at their peptide bonds.
The chymotrypsin itself, however, is active and able to function due to cleavage by trypsin. All forms cleave proteins at the amino acids tyrosine and tryptophane. In addition, chymotrypsin B also cleaves other bonds that are found, for example, in the molecule glucagon.
