Trypsin USP33

1.USP standard Trypsin 2.Bovine or Porcine pancrease 3.Pharmaceutical raw material 4.White crystallized powder

Trypsin USP33

CAS 9002-07-7                                 

Source Porcine (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 ultra-filtration.

Specification

Items	Specification	Method
Appearance	White crystallized powder	USP33
solubility	500,000 USP Trypsin Unites, is soluble in 10mL of water and in 10 mL of saline TS	USP33
Loss on drying	≤ 5.0%	USP33
Residue on Ignition	≤2.5%	USP33
Microbial limits
Pseudomonas aeruginosa	Absent	USP33
Salmonella	Absent	USP33
Staphylococcus aureus	Absent	USP33
Limit chymotrypsin	NMT 50USP Chymotrypsin Units/2500USP Trypsin Units (NMT approximately 5% of Chymotrypsin)	USP33
Assay	NLT 2500 USP Trypsin Units/mg (calculated on the dried basis) and 90.0%-110.0% of the labeled potency.	USP33

Storage

 Sealed, Dark, at temperature 2-8°C

Trypsin USP33