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APIs Bovine trypsin (Trypsin, bovine pancreas) is a serine protease extracted from the pancreas of cattle, which is an animal extract. It is usually a white or off-white crystalline powder. This enzyme has a high degree of specificity and selective hydrolysis function, and can cut specific peptide bonds in protein molecules, especially the peptide bonds formed at the carboxyl end of lysine and arginine. Bovine trypsin has good solubility in water, but is insoluble in organic solvents such as ethanol, glycerol, chloroform and ether. As an important enzyme, bovine trypsin can be used as pharmaceutical raw materials in pharmaceutical chemicals due to its various biological activities.
Improved digestion ingredients: Bovine trypsin, as an endopeptidase, has a selective hydrolysis effect on arginine and lysine peptide chains, and can specifically catalyze the hydrolysis of peptide bonds formed by lysine and arginine carboxyl groups.
Protein research: In protein chemistry research, bovine trypsin can be used to hydrolyze proteins to help study protein structure and function.
Cell culture: Bovine trypsin is often used to dissociate tissues and monolayer cells because it can act on transmembrane proteins and proteins in the extracellular matrix, such as cadherins, integrins, etc.
Pharmaceutical raw materials: Bovine pancreatic protease is used in the production of insulin and inactivated vaccines, and is also used for tissue cell separation and culture.
Clinical surgery: In clinical surgery, bovine pancreatic protease is used to treat symptoms such as local abscesses, edema, hematomas caused by various inflammations, ulcers, gangrene, trauma, and atrophy, as well as snake bites.
Food additives: As a food processing aid, bovine pancreatic protease is used to cut macromolecular proteins and improve the texture and taste of food.
Pharmaceutical chemicals: In the field of biopharmaceuticals, bovine pancreatic protease was mainly used in the production of insulin in the early days, and was also used in other cell culture fields.
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