KOTASE combines primarily Bromelain, plant-proteolytic enzyme extracted from pineapple plant, Ananas comosus and Crystalline trypsin, animal-proteolytic enzyme extracted from mammalian pancreas.
KOTASE is green sugar coated tablet and has potent antiinflammatory, antiedemic activity after oral administration. Generally, inflammatory reaction occurs when abnormal change in body protein induces inflammatory polypeptide. Bromelain in KOTASE acts against inflammatory polypeptides such as bradykinin, kallidin etc. and crystalline trypsin acts against inflammatory polypeptides except kinis, therefore KOTASE actively breaks peptide bond, proteolytic action, it results effective antiinflammatory action.
Mechanism of action of Bromelain:
Bromelain increases blood fibrinolytic activity as well as inhibiting fibrinogen synthesis. It also directly degrades fibrin and fibrinogen. Kininogen and bradykinin serum and tissue levels are lowered by bromelain, and it also affects prostaglandin synthesis, which gives it its anti-inflammatory effects. Bromelain has been found to reduce the excretion of pro-inflammatory cytokines as well as chemokines in a study into its possible mechanism of action in ulcerative colitis, inflammatory bowel disease, and Crohn’s disease.
Mechanism of action of Trypsin:
The enzymatic mechanism is similar to that of other serine proteases. These enzymes contain a catalytic triad consisting of histidine-57, aspartate-102, and serine-195. These three residues form a charge relay that serves to make the active site serine nucleophilic. This is achieved by modifying the electrostatic environment of the serine.
The enzymatic reaction that trypsins catalyze is thermodynamically favorable but requires significant activation energy (it is “kinetically unfavorable”). In addition, trypsin contains an “oxyanion hole” formed by the backbone amide hydrogen atoms of Gly-193 and Ser-195, which serves to stabilize the developing negative charge on the carbonyl oxygen atom of the cleaved amides.