Trypsin

Enzyme trypsin is one of the digestive enzymes responsible for absorption and štiepenie cleavage of proteins of the small intestine. Trypsin is excreted from the pancreas as inactive trypsinogen, which is only activated in the intestine enterokinase intestinal juice. It cleaves specifically those proteins that are digested by gastric pepsin, the polypeptides and dipeptides. Recent studies suggest that activated trypsin induces inhibition of stimulated pancreatic secretion in the upper small intestine.

In absorbed form, it is antitumor and anti-inflammatory substance. It can dissolve the protein layer that is on the surface of damaged cells in the human body, which after losing the protein layer become more accessible to immune cells.

It helps in digestion and cleansing the cardiovascular system and the whole organism. It has significant antioxidant effects.

Fig.1: crystal structure of trypsin (source: http://en.wikipedia.org/wiki/Trypsin)

Chymotrypsin has similar properties as trypsin. It differs from trypsin that it cleaves the peptide bond in place of phenylalanine, tryptophan or tyrosine. In contrast, trypsin cleaves the peptide bond based on the carboxyl groups of amino acids arginine and lysine.