Native Porcine Trypsin, from porcine pancreas 

Bacterial Contaminants:

E. coli - negative

Salmonella sp. - negative

Aerobic Plate Count - ≤ 10,000 CFU/g

Trypsin is a serine protease found in the digestive system of many vertebrates, where it hydrolyzes proteins. It is produced in the pancreas as the inactive proenzyme, Trypsinogen. Trypsin is one of the three principal digestive proteinases, the other two being Pepsin and Chymotrypsin. In the digestive process, Trypsin acts with the other proteinases to break down dietary protein molecules to their component peptides and amino acids. Trypsin continues the process of digestion (begun in the stomach) in the small intestine where a slightly alkaline environment (about pH 8) promotes its maximal enzymatic activity. It cleaves peptide chains mainly at the Carboxyl end of the amino acids Lysine or Arginine, except when followed by a Proline.