1. Protein Inhibitors of Serine Proteinases - Mechanism and Classification.- 2. The Biological Functions and Physiological Effects of Ingested Inhibitors of Digestive Reactions.- 3. Safety of Trypsin Inhibitors in the Diet: Effects on the Rat Pancreas of Long-Term Feeding of Soy Flour and Soy Protein Isolate.- 4. Dose Effects of Raw Soyabean Flour on Pancreatic Growth.- 5. Enhancement of Pancreatic Carcinogenesis of Raw Soy Protein Isolate Quantitative Rat Model and Nutritional Considerations.- 6. Pancreatic Carcinogenesis - The Potential of Cholecystokinin as a Cocarcinogen in the Hamster - Nitrosamine Model.- 7. Interaction of Dietary Protein and Trypsin Inhibitor on Plasma Cholecystokinin and Pancreatic Growth in Rats.- 8. Gastrin and Cholecystokinin Levels in Rats Fed Soya Bean Trypsin Inhibitor.- 9. Negative Feedback Inhibition of Pancreatic Exocrine Secretion in Humans.- 10. Protease Inhibitors: Their Role as Modifiers of Carcinogenic Processes.- 11. Nutritional and Metabolic Response to Plant Inhibitors of Digestive Enzymes.- 12. Among Speciesesponse to Dietary Trypsin Inhibitor: Variation Species.- 13. The Effect of the Long-Term Feeding of Raw Soyflour on the Pancreas of the Mouse and Hamster.- 14. Accentuated Response to Dietary Raw Soyflour by Meal-Feeding in Various Species.- 15. Effect of Long-Term Feeding of Soy-Based Diets on the Pancreas of Cebus Monkeys.- 16. Inhibition of Human Proteinases by Grain Legumes.- 17. Regulation of Proteinase Inhibitor Genes in Food Plants.- 18. Genetics and Breeding of Soybeans Lacking the Kunitz Trypsin Inhibitor.- 19. Protease Inhibitors in Plant Foods: Content and Inactivation.- 20. Preparation of Unheated Soy Protein Isolate with Low Trypsin Inhibitor Content.- 21. Nutritional Improvement of Legume Proteins Through Disulfide Interchange.- 22. Relevance of Multiple Soybean Trypsin Inhibitor Forms to Nutritional Quality.- 23. Antinutritional and Biochemical Properties of Winged Bean Trypsin Inhibitors.- 24. Protease Inhibitors of the Marama Bean.- 25. Trypsin/Chymotrypsin Inhibitors from Millets.- 26. Antigenicity of Native and Modified Kunitz Soybean Trypsin Inhibitors.- 27. Photoreactive, Active Derivatives of Trypsin- and Chymotrypsin-Inhibitors Fomr Soybeans and Chick Peas.- 28. Biochemical, Nutritional, and Toxicological Aspects of Alpha-Amylase Inhibitors from Plant Foods.- 29. The Inhibition of Digestive Enzymes by Polyphenolic Compounds.- 30. Effect of Severely Alkali-Treated Casein on Gastrointestinal Transit and Selected Intestinal Enzyme Activity.- 31. Inactivation of Metalloenzymes by Lysinoalanine, Phenylethylaminoalanine, Alkali-Treated Food Proteins, and Sulfur Amino Acids.
Soybean protei ns are wi de 1 y used inhuman foods ina vari ety of forms, including baby formulas, flour, soy protein concentrates, soy protein isolates, soy sauces, textured soy fibers, and tofu. The presence of inhibitors of digestive enzymes in soy proteins impairs nutritional quality and possible safety of this impportant legume. Normal processing conditions based on the use of heat do not completely inactivate these inhibitors, so that residual amounts of plant protease inhibitors are consumed by animals and man. Inhibitors of digestive enzymes are present not only in legumes, such as soybeans, lima beans, and kidney beans, but also in nearly all plant foods, including cereals and potatoes, albeit in much smaller amounts. The antinutritional effects of inhibitors of proteolytic enzymes have been widely studied and can be ameliorated by processing and/or sulfur amino acid fortification. A more urgent concern is reports that rats fed diets containing even low levels of soybean-derived inhibitors, which are found in foods such as soy-based baby formulas, may develop over their lifespan pancreatic lesions leading eventually to neoplasia or tumor formation. On the other hand, recent stUdies suggest that certain enzyme inhibitors from plant foods may prevent cancer formation in other tissues. A key question, therefore, is whether inhibitors from plant foods constitute a human health hazard.
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