Trypsin

Trypsin is a protease extracted from porcine pancreas by multiple crystallization and further prepared by chromatography and ultrafiltration technology. It consists 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 Information:

Product name: Trypsin

Main component: Trypsin

Product specification: 2500 USPU/mg (can be customized)

Product properties: Light yellow crystal powder

Storage: Room temperature, dry, and protected from light

Shelf life: 12 months

Applications:

Food Processing

In food processing, trypsin can make full use of the protein cleavage specificity for protein processing. It can also be used to achieve higher protein hydrolysis with other cut-site proteases.

Cell Culture

Trypsin can be used for cell culture in bioengineering by selectively hydrolyzing the proteins between cells, allowing for cell separation and cultivation for various bioengineering experiments.