Anti-nutritional factors in Soy Myths and Facts

Many plants and animals that man uses for food contain as natural constituents chemical substances known to have toxic properties. By experimentation man has learned to avoid dangerous exposure to the natural chemical components of his foods. Although acute poisoning is usually avoided, the public health significance associated with naturally-occurring toxicants is usually in the realm of chronic toxicity. A number of possible cause and effect relationships of this kind exist, but usually they only point to the presence of a toxicant. This is true because the intake is too small to cause severe effects, and because chronic effects are difficult to identify. Recognition of factors in the environment that may affect public health is basic to the eventual control of those factors. Anti-enzymes or Inhibitors Seed proteins such as cereal grains, legumes, and oil seeds are important sources of dietary protein in many areas of the world but some of them contain enzyme inhibitors. Perhaps the best known and most extensively studied of these toxic factors in seeds used as food are the trypsin inhibitors. Trypsin is an enzyme involved in protein digestion and trypsin inhibitors can result in a decreased availability of protein. However, under conditions of controlled processing the antitryptic factor in the seeds can be partially or completely altered and the nutritional value improved. Trypsin inhibitors, which for the most part are completely destroyed by heat, have been reported in wheat flour, soybeans, lima beans, mung beans, peanuts, oats, buckwheat, barley, sweet potatoes, garden peas, corn and white potatoes. Chymotrypsin is another enzyme involved in protein digestion and a chymotrypsin inhibitor has been found in potatoes. Protease inhibitors are destroyed relatively easily by heat. There is a vast amount of literature on this topic. In general, the extent to which trypsin inhibitor activity is destroyed by heating is a function of temperature, duration of heating, particle size, and moisture conditions. At 100 degrees centigrade, nearly all of the trypsin inhibitor activity is destroyed after 10 minutes. Several methods inactivating the trypsin inhibitors are effective: boiling soybeans in water, dry roasting, dielectric heating, microwave irradiation, extrusion cooking, gamma irradiation, and infrared radiation. Especially Indian cooking methods trypsin inhibitor or anti-nutritional factors is not a concern. As far as soy is concerned, even though soy has a very high amount of these antinutritional factors, they are very heat sensitive compared to those found in any legumes or food commodities (see the table below). Trypsin inhibitor and hemagglutinin contents of raw, microwave-heated and conventionally-cooked legume seeds5
Legume seeds Trypsin inhibitors (TIU/mg sample) Raw Microwave heated Dry Wet Conventional cooking3 Raw C 8 O 12 Hemagglutinins Microwave heated Dry C 6 O 9 Wet C 4 O 7 0 0 2 0 3 Conventional cooking3 C 0 0 0 0 0 0 O 0 0 0 2 0 2

White 31.3a 10.2b 8.1c 1.4d bean Soybean 75.4a 22.5b 3.2c 1.2c 0 5 0 3 0 Green 2.5a 1.6b 0.8c 1.6b 0 0 0 0 0 pea Mature 3.5a 3.1a 1.8c 2.5b 0 3 0 2 0 pea Lentil 3.6a 0.4c 0.3c 2.4b 0 2 0 0 0 Chickpea 17.9a 3.6b 3.1b 3.1b 0 3 0 3 0 1 TIU= Trypsin inhibitor units. 2 Extract maximum dilution causing agglutination of cow (C) and human (O) erythrocytes. 3 Cooking in boiling water until softness. Values with different letter (a,b,c,d) within a row indicate significant differences (p < 0:05).

References 1. Committee on Nitrite and Alternative Curing Agents in Food, National Academy of Sciences, The Health Effects of Nitrates, Nitrite, and N-Nitroso Compounds. Washington, DC, 1981. 2. Dack, G. M. Food Poisoning, 3rd ed. The University of Chicago Press: Chicago, IL, 1956. 3. Liener, Irvin E., Ed. Toxic Constituents of Plant Foodstuffs, 2nd ed., Academic Press: New York, NY, 1980. 4. Liener, Irvin E. Implications of antinutritional components in soybean foods. Critical Reviews in Food Science and Nutrition, vol. 34, pages 31-67, 1994 5. Hernndez-Infante, M., Sousa, V., Montalvo, I. and Tena, E. 1998. Impact of microwave heating on hemagglutinins, trypsin inhibitors and protein quality of selected legume seeds. Plant Foods for Human Nutrition 52: 199208. 6. Rackis, J. J., Wolf, W. J. and Baker, E. C. Protease inhibitors in plant foods: Content and inactivation, In: Nutritional and Toxicological Significance of Enzyme Inhibitors in Foods, edited by M. Freidman, Plenum Press, New York, 1986~Committee on Food Protection, Food and Nutrition Board, National Research Council, National Academy of Sciences, Toxicants Occurring Naturally in Foods. Washington, DC, 1973.