Nutrients in food cannot be absorbed by the body straight away. They need to be broken down into smaller parts by various enzymes. In the case of proteins, specific enzymes aid in breaking them into amino acids which are then utilized by the body. These enzymes are of two types, namely chymotrypsin and trypsin.
Chymotrypsin vs Trypsin
The main difference between chymotrypsin and trypsin is that chymotrypsin only works with specific aromatic amino acids which include tyrosine, tryptophan, and phenylalanine whereas trypsin only works with basic amino acids which include arginine and lysine. Each of these amino acids is selected by the enzymes according to their structure and size.
Chymotrypsin is an enzyme that essentially aids the digestion process by breaking down proteins. It is secreted from the pancreas as a constituent of pancreatic juice. The enzyme is activated by its precursor which is called chymotrypsinogen. This is an inactive enzyme that only functions in the presence of Trypsin.
Meanwhile, trypsin is another kind of digestive enzyme that works with different amino acids. It is produced by the pancreas as well. However, most of its work is carried out in the small intestine. Its precursor is an inactive enzyme called trypsinogen. The inactive enzyme functions only in the presence of enterokinase.
Comparison Table Between Chymotrypsin and Trypsin
| Parameters of Comparison | Chymotrypsin | Trypsin |
| Discovery | It was discovered in the 1900s. | It was discovered in 1876. |
| Meaning | It is a digestive enzyme that works on breaking down aromatic amino acids. | It is a digestive enzyme that works on breaking down basic amino acids. |
| Precursor | Its precursor is an inactive enzyme called chymotrypsinogen. | Its precursor is an inactive enzyme called trypsinogen. |
| Activation | Its precursor is activated with the help of Trypsin. | Its precursor is activated with the help of enterokinase. |
| Amino Acids | It selects amino acids including tyrosine, tryptophan, and phenylalanine. | It selects amino acids including arginine and lysine. |
| Uses | It can be used for peptide mapping, peptide synthesis, analysis, and even fingerprinting. | It can be used for tissue dissociation, mitochondrial isolation, and cell harvesting. |
| Inhibitors | Its inhibitors include benzamidine, aprotinin, DFP, EDTA, Ag+, etc. | Its inhibitors include boronic acids, peptidyl aldehydes, coumarin derivatives, etc. |
What is Chymotrypsin?
Chymotrypsin is a digestive enzyme that was first discovered in the 1900s. It is part of the serine protease family and falls under the category of endopeptidases. The enzyme has a molecular mass of 25.6 kDa. Its precursor is called chymotrypsinogen. This is an inactive enzyme that activates with the help of trypsin. When this happens, chymotrypsin is formed and released from the pancreas as a constituent of pancreatic juice.
Every enzyme has an active site inside it that is built for particular structures and sizes to fit inside. This means that the enzyme needs to select specific kinds of amino acids that can fit inside them. In the case of chymotrypsin, only aromatic amino acids are selected. These include tyrosine, tryptophan, and phenylalanine. Once they enter the enzymes active site, their peptide bonds are broken so that they can be digested.
These enzymes serve a variety of purposes in medical and Vito studies. They are used for peptide mapping, peptide synthesis, analysis, and even fingerprinting. There are certain inhibitors as well that bind with chymotrypsin so as to decrease its activity. These include benzamidine, aprotinin, DFP, EDTA, Ag+, etc. They are often found in supplements that are prescribed to people with dysfunctional chymotrypsin enzymes.
What is Trypsin?
Trypsin is another digestive enzyme, but it was discovered way before in the year 1876. It belongs to the serine proteases family as well but falls under the category of globular proteins. The molecular mass of trypsin is 23.3 kDa. Its function is to break peptide bonds in amino acids.
The enzyme is released from the pancreas from its precursor called trypsinogen. This inactive enzyme comes in contact with enterokinase for activation. Once this happens, it is carried to the small intestine where most of its functioning takes place. The enzyme only selects particular basic amino acids into its active site. These include arginine and lysine.
There are various uses for trypsin in tissue dissociation, mitochondrial isolation, and cell harvesting. It has several inhibitors as well which include boronic acids, peptidyl aldehydes, coumarin derivatives, etc. These are found in various supplements that have numerous medical uses.
Trypsin is of two main types. These include alpha-trypsin and beta-trypsin. Each of them has a different structure and functions at a different thermal stability threshold. However, both of their active sites contain Aspartic acid, Histidine and Serine, which aid in the entire process of breaking amino acids. They do so by cleaving the c-terminal end which has carbon on it.
Main Differences Between Chymotrypsin and Trypsin
- Chymotrypsin was discovered in the 1900s whereas trypsin was discovered in 1876.
- Chymotrypsin is a digestive enzyme that works on breaking down aromatic amino acids whereas trypsin is a digestive enzyme that works on breaking down basic amino acids.
- Chymotrypsin selects amino acids including tyrosine, tryptophan, and phenylalanine whereas trypsin selects amino acids including arginine and lysine.
- The precursor of chymotrypsin is an inactive enzyme called chymotrypsinogen whereas that of trypsin is an inactive enzyme called trypsinogen.
- The precursor of chymotrypsin is activated with the help of Trypsin whereas that of trypsin is activated with the help of enterokinase.
- Chymotrypsin can be used for peptide mapping, peptide synthesis, analysis, and even fingerprinting whereas trypsin can be used for tissue dissociation, mitochondrial isolation, and cell harvesting.
- Chymotrypsin inhibitors include benzamidine, aprotinin, DFP, EDTA, Ag+, etc. whereas trypsin inhibitors include boronic acids, peptidyl aldehydes, coumarin derivatives, etc.
Conclusion
Understanding what chymotrypsin and trypsin are, can be difficult for people who do not regularly delve into scientific study. However, knowing the differences between them may help clear the matter. The most notable distinguishing factor between the two is that chymotrypsin works on aromatic amino acids only whereas trypsin works with basic amino acids.
Another notable difference is that they both have different precursors that are activated only by specific enzymes. However, the inactive enzyme for chymotrypsin is activated by trypsin. Lastly, both enzymes have different structures and masses. They are used for different purposes in various medical studies and processes.
References
- https://www.sciencedirect.com/science/article/pii/0022283672900289
- https://www.sciencedirect.com/science/article/pii/0014579395014845