Trypsin is a protease extracted from porcine pancreas by multiple crystallization and further prepared by chromatography and ultrafiltration technology, consisting of 223 amino acid residues with a molecular weight of about 24,000, and is widely used in research and development, production and testing in biological and food industries.
Trypsin is a serine-type endonuclease with high specificity, which acts exclusively to cut off the carboxyl side of lysine and arginine residues in proteins. It can also restrict the precursors of other enzymes such as chymotrypsinogen, carboxypeptidase, phospholipase, etc. and act as an activator.
It is easily soluble in water and the aqueous solution is a clarified off-white liquid, insoluble in organic solvents such as ethanol, glycerol, chloroform and ether.
Product name: Trypsin main component: Trypsin
Product specification: 2500USPU/mg (can be customized) Product properties: light yellow crystal powder Storage: room temperature dry and protected from light Shelf life: 12 months
In food processing, it can make full use of the protein cleavage specificity of trypsin for protein processing; it can also be used to achieve higher protein hydrolysis with other cut site proteases.
Trypsin can also be used for cell culture in bioengineering by selectively hydrolyzing the proteins between cells so that the cells can be separated, and the separated cells can be cultured for various bioengineering experiments.