Trypsinogen to trypsin is conveed by

Trypsin, a proteinase, is secreted as an inactive zymogen form trypsinogen, which is activated to form active Trypsin, which has strong proteolytic activity and an inactive hexapeptide which is produced and liberated during the process of activation. Activation is brought about by * A glycoprotein enzyme called as enterokinase of the intestinal juice at a pH of 5.5 * Also by trypsin itself once it is formed, autocatalytically, at a pH of 7.9. *C a++ also is required for the activation. In the process of activation, the "active site" of the enzyme trypsin, which is histidylserine residue is unmasked. Hence trypsin belongs to the group of serine proteases. Trypsin acts in an alkaline medium pH 8 to 9 (optimum pH-7.9) and has low Michaelis constant.Ref: Textbook of medical biochemistry, MN Chatterji, 8th edition, page no: 464