Trypsin inhibitors (TI) are substances which, when added to a mixture of a trypsin and a subtrate, bind to the enzyme and render it to decrease in the rate of substrate cleavage. These inhibitors are nonglycosylated, water-soluble (albumin) that account for about 0,2-2 % of the total soluble protein of the legume seeds. Two major families of trypsin inhibitors have been described in legumes: the Bowmen-Brix-type (BBI) and the Kunitz-type inhibitors (KTI). They are distinct families of proteins, as evidenced by their molecular weights, compositions, and amino acid sequences. Because of their unique pharmacological properties, these inhibitors hold considerable promise in clinical applications in their field of medicine. At least one inhibito...