Trypsin CAS NO.9002-07-7

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…

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, ether 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 Items Specification Method Appearance White or almose white lyophilized powder Solvent Transparentness Confroms USP30 Loss on drying ≤ 5.0% USP30 Residue on Ignition ≤2.5% USP30 Microbial limits Confroms USP30 Chymotrypsin ≤50 USP units/mg powder USP30 Assay Trypsin ≥ 2500USP units/mg powder USP30 Storage Sealed, Dark, at temperature 2-8℃1.USP and EP standard 2.sourcebovine or porcine 3.White crystalline powder, odorless 4.High purity reagents TrypsinCA9002-07-7Source Porcine (Bovine) pancreasGeneral descriptionTrypsin is a kind of serine protease that specifically hydrolyze peptide bond formed of carboxyl of basic amino acids Arginine and Leucine. The enzyme can easily be autolyzed. It is soluble in Water, insoluble in trichloromethane, ethanol, aether and glycerol. The optimum pH is 8.0. Calcium can delay the autolysis of Trypsin and promote the activity of pre-Trypsin.The high puri1.E1.Enterprise standard 2.Porcine or bovine pancreas3.Food&pharmaceutical grade 4.White crystallize powder or powder Trypsin-ChymotrypsinSource Swine (Bovine) pancreasGeneral descriptionTrypsin-Chymotrypsin is the co-crystal of Chymotrypsin and Trypsin so it has the properties of both. The activity of hydrolyzing casein is as much as Chymotrypsin. But the activity of its Chemotrypsin to hydrolyze N-Benzoyl-L-tyrosine ethyl ester(BTEE)is three times higher than Chemotrypsin.The activity of hydrolyze ester bond similar to that of Trypsin. It is stable when dry and easy to be inactivated in solutions. The optimum pH is 7.0-8.0.The high purity Trypsin-Chymotrypsin of Beijing Geyuantianrun Bio-tech Co., Ltd.. is purified by re-crystallization, and then by ultra-filtration.Specification ItemsSpecificationMethodAppearanceWhite crystallize powder or powderEnterprise standardsolubilitySolubleUSP33Loss on dryingNo more than5.0%USP33Residue on ignitionNo more than 2.5%USP33PH3.0—6.0EP6.0Microbial limits  Pseudomonas aeruginosaAbsentUSP33Salmonella AbsentUSP33Staphylococcus aureusAbsentUSP33E.ColiAbsentUSP33AssayTrypsin≥2400USP units/mg,Chymotrypsin≥400USP u/mgEnterprise standard Storage Sealed, Dark, at temperature 2-8°C