Trypsin is a proteinase, meaning it breaks proteins into components such as amino acids or dipeptides (smaller proteins). It works with two other enzymes that are present in the stomach. At low pH such as in the stomach where Hydrochloric acid is present (HCl (aq), pH approx = 2) Trypsin only contributes to minor digestive powers. It works at highest efficiency at pH of 8, in the small intestine. Pancreas produces an inactive form of Trypsin that is introduced into the small intestine.
Trypsin is only effective against proteins that have carboxyl groups (COOH), the carboxyl groups is recognized by Trypsin's active sites. Once Tryspin latches onto the protein, it cleaves off the peptide bond connecting two amino acids. Since Trypsin has such a picky taste for proteins with certain chemical restrictions (requirements for activation) it provides ordered and clean cleavage of their substrates.
(Hope that helped
)
Linear Mode
