Trypsin

Trypsin Source: Swine (Bovine) pancreas General description Trypsin is a kind of serine proteolytic enzyme, with molecular weight of 23300 dalton, and is a single peptide chain composed of 223 amino acid residues. With rigorous specificity, the trypsin specifically acts on the peptide linkage constituted by the basic amino acid arginine and leucine. Enzyme easily autolyzes by itself, and its activation also reduces or loses gradually. It is easily soluble in the water, but insoluble in trichloromethane, ethanol, and glycerin, and the optimum PH is 8.0 9.0. When the PH is 1.8, it is hardly deactivated when boiled for a short time; if the salt is added into the hot solution, the protein will precipitate, and the enzyme action of filtrate cannot be seen, and Ca2+ plays the role in protecting and activating the trypsin. The high purity Trypsin of Beijing Geyuantianrun Bio-tech Co., Ltd.. is purified by re-crystallization, and then by Ion Exchange Chromatography and ultra-filtration. Specification ItemsSpecificationMethod Appearance White or almost white lyophilized powderSolvent Transparentness ConfromsUSP32Loss on drying ≤ 5.0%USP32Residue on Ignition ≤2.5%USP32Microbial limits ConfromsUSP32Chymotrypsin ≤50 USP units/mg powderUSP32Assay Trypsin ≥ 2500USP units/mg powderUSP32 Storage Sealed, Dark, at temperature 2-8