Learn the Properties and Applications of Chymotrypsin
SummaryChymotrypsin is a typical serine protease. As an endopeptidase that catalyzes the hydrolysis of protein peptide bonds, its realization form is mainly for the cleavage of the peptide bond formed by the carboxyl end of the aromatic amino acid-tryptophan, phenylalanine or tyrosine. Chymotrypsin is a typical serine protease and is currently one of the digestive enzymes of most vertebral animals.
- Author Name: Iva Colter
Chymotrypsin is a typical serine protease. As an endopeptidase that catalyzes the hydrolysis of protein peptide bonds, its realization form is mainly for the cleavage of the peptide bond formed by the carboxyl end of the aromatic amino acid-tryptophan, phenylalanine or tyrosine. Chymotrypsin is a typical serine protease and is currently one of the digestive enzymes of most vertebral animals.
Similar to trypsin inhibitors, chymotrypsin inhibitors can also reduce the degradation of proteins in the intestinal tract, causing the production of amino acids and peptides to be affected, thereby affecting the normal metabolism of organisms. Potato tubers contain 0.6%-2.1% wet-based protein, of which protease inhibitors account for about half, and their molecular weight is between 5-25kDa. In potato tubers, the role of protease inhibitors is to act as storage proteins and regulate the activity of endogenous proteases.
The reason they are activated is also because the synthesis of chymotrypsinogen (the precursor of chymotrypsin) does not have the activity of normal enzymes. But after the pancreatic juice reaches the small intestine, it is cut into two parts by trypsin (the two parts are still linked by disulfide bonds). Subsequently, the cleaved chymotrypsinogen can cut a relatively short peptide segment from each other to form a protease with three polypeptide chains connected by disulfide bonds, which forms a chymotrypsin with intact activity. This activation method ensures that chymotrypsin can only obtain catalytic activity in a specific location in the body (small intestine), thereby avoiding damage to the body.
In animals, chymotrypsin can only play a role when it is used in the digestive system. It catalyzes a hydrolysis reaction to cut the corresponding peptide bonds and promote digestion in the body. And its normal catalytic reaction is divided into two stages, namely the rapid reaction at the beginning and the subsequent stable reaction. Because the reaction is mainly affected by the reaction substrate, the reaction rate will be different.
What are the applications of chymotrypsin?
- Chymotrypsin can cleave the peptide chains of protein macromolecules into smaller molecular weight peptides, or act on the peptide ends of protein molecules to separate amino acids. Through this action, fibrin and mucin can be hydrolyzed into polypeptides or amino acids in the sputum, making the viscous sputum liquefied and easy to cough out. It is effective for purulent or non-purulent sputum.
- Chymotrypsin can relax the ciliary ligament and dissolve the protein structure of certain tissues in the eye. Chymotrypsin also promotes the penetration of antibiotics and chemotherapeutic drugs into the lesions.
- Chymotrypsin can be used to treat acne. Chymotrypsin improves tissue permeability, inhibits inflammatory reactions, and dissolves exudates and necrotic tissues, which can improve acne symptoms.
- Chymotrypsin can also treat infertility. It has been found that there are many factors involved in the process of semen liquefaction, of which the most important factors are enzymes. α-chymotrypsin can significantly shorten the liquefaction time of semen and reduce its viscosity, but it has no obvious effect on sperm activity.