Human trypsin is more resistant to inhibition than is the trypsin of other mammalian species. The effect on human trypsin of soybean trypsin inhibition in soy protein does not appear to be a potential hazard to man. Therefore, the elimination of STI does not seem to be necessary for humans. In animal diets, however, pancreatic toxicity must be considered whenever soybean protein is utilized. Soybeans should be treated to increase their nutritional benefits and decrease any animal health risks (27-29). This will insure healthy control subjects in laboratory situations and avoid misinterpretation of pathologic data. The treatment suggested is heat (2,18,25,30-32) since heat will destroy most of the soybean trypsin inhibitors. Additional supplementation is required following heat treatment for amino acids (33,34) such as methionine, valine, and threonine; for choline (2,14,35); and for the minerals zinc (36) and calcium (11,34). Excessive heat must be avoided since it will decrease the nutritional value of soybean protein and increase lysinoalanine, a nephrotoxic substance (12). Finally, the use of STI as a promotor in the study of potential pancreatic carcinogens may prove beneficial for cancer research (24,25) and might be considered in the future.