is produced in the pancreas as the inactive proenzyme trypsinogen. Trypsin predominantly cleaves peptide chains at the carboxyl side of the amino acids lysine or arginine, except when either is followed by proline. It is used for numerous biotechnological processes. The process is commonly referred to as trypsin proteolysis or trypsinisation and proteins that have been digested/treated with trypsin are said to have been trypsinized.Trypsin is secreted into the duodenum, where it acts to hydrolyse peptides into their smaller building blocks, namely amino acids (these peptides are the result of the enzyme pepsin breaking down the proteins in the stomach). This is necessary for the uptake of protein in the food as though peptides are smaller than proteins, they are still too big to be absorbed through the lining of the ileum. Trypsin catalyses the hydrolysis of peptide bonds.