Protease Inhibitors in Plant Foods: Content and Inactivation

  • J. J. Rackis
  • W. J. Wolf
  • E. C. Baker

Abstract

To understand the present widespread interest in protease inhibitors (PI), one must look back to the vast amount of research that has been conducted for over 50 years. Intensive investigations, like wave motions on the water, followed a highly cyclical pathway depending upon the interest and support for research in various disciplines. Nutritionists were concerned with the potential adverse effects of the inhibitors of trypsin and chymotrypsin in the intestinal tract of man and animals (Liener and Kakade, 1980; Liener, 1981; Rackis and Gumbmann, 1981); biochemists recognized that the peculiar properties of PI’s may yield fundamental information concerning protein-protein interactions especially the mechanism of proteolytic hydrolysis (Richardson, 1981; Ryan, 1979); medical scientists envisioned an important role for PI’s in the treatment of various metabolic disorders (Katunuma et al., 1983; Vogel et al., 1968; Weyer, 1968), and biologists foresaw an important physiological role of PI’s to regulate plant growth, protein synthesis and resistance to microbial and insect pests (Richardson, 1977, 1981; Ryan, 1973, 1979).

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Al-Bakir, A. Y., Sachde, A. G., and Naoum, I. E., 1982, Occurrence and stability of trypsin inhibitors in Iraqi local legumes, J. Agric. Food Chem., 30:1184.Google Scholar
  2. Albrecht, W. J., Mustakas, G. C., and McGhee, J. E., 1966, Rate studies on atmospheric steaming and immersion cooking of soybeans, Cereal Chem., 43:400.Google Scholar
  3. American Association of Cereal Chemists, 1983, Determination of trypsin inhibitor activity of soy products, Method 71–10, in: “Approved Methods of the American Association of Cereal Chemists”, St. Paul, MN.Google Scholar
  4. American Oil Chemists’ Society, 1976, Trypsin inhibitor activity, Method Ba 12–75, in: “Official and Tentative Methods” Champaign, IL.Google Scholar
  5. American Oil Chemists Society, 1979, Proceedings—World Conference on Vegetable Food Proteins, Amsterdam, Netherlands, November, 1978. J. Am. Oil Chem. Soc., 56:99.Google Scholar
  6. American Oil Chemists’ Society, 1981, Proceedings of the World Conference on Soya Processing and Utilization, Acapulco, Mexico, November, 1980, J. Am. Oil Chem. Soc., 58:121.Google Scholar
  7. Baker, E. C., and Mustakas, G. C., 1973, Heat inactivation of trypsin inhibitor, lipoxygenase and urease in soybeans: Effect of acid and base additives, J. Am. Oil Chem. Soc., 50:137.Google Scholar
  8. Baker, E. C., Mustakas, G. C., and Warner, K. A., 1979, Extraction of defatted soybean flours and flakes with aqueous alcohols: Evaluation of flavor and selected properties, J. Agric. Food Chem., 27:969.Google Scholar
  9. Baker E. C, and Sullivan, D. A., 1983, Development of a pilot-plant process for the extraction of soy flakes with aqueous isopropyl alcohol, J. Am. Oil Chem. Soc., 60:1271.Google Scholar
  10. Bates, R. P., Knapp, F. W., and Araujo, P. E., 1977, Protein quality of green-mature, dry mature and sprouted soybeans, J. Food Sci., 42:271.Google Scholar
  11. Besrat, A., 1981, Protein quality of Faffa, the Ethiopian infant formula as affected by pulse substitution, J. Food Biochem., 5:233.Google Scholar
  12. Birk, Y., 1961, Purification and some properties of a highly active inhibitor of trypsin and α-chymotrypsin from soybeans, Biochem. Biophys., Acta 54:378.Google Scholar
  13. Birk, Y., Gertler, A., and Khalef, S., 1963, A pure trypsin inhibitor from soya beans, Biochem. J., 87:281.Google Scholar
  14. Birk, Y., and Waldman, M., 1965, Amylolytic-, trypsin-inhibiting- and urease-activity in three varieties of soybeans and in soybean plant, Qual. Plant. Mater. Veg., 12:199.Google Scholar
  15. Boisen, S., 1983, Protease inhibitors in cereals. Occurrence, properties, physiological role, and nutritional significance, Acta Agric. Scand., 33:369.Google Scholar
  16. Boisen S., and Djurtoft, R., 1981, Trypsin inhibitor from rye endosperm: Purification and properties, Cereal Chem., 58:194.Google Scholar
  17. Buera, M. P., Pilosof, A. M. R., and Bartholomai, G. B., 1984, Kinetics of trypsin inhibitory activity loss in heated flour from bean, Phaseolus vulgaris, J. Food Sci., 49:124.Google Scholar
  18. Buera, M. P., Pollio, M. L., Pilosof, A. M., and Bartholomai, G. B., 1983, Cinetica de la perdida de solubilidad y de lisina disponible en harinas de porotos trantadas termicamente, Rev. Agroquim. Tecnol. Aliment., 23:262.Google Scholar
  19. Campos F. A. P., and Richardson, M., 1983, The complete amino acid sequence of the bifunctional α-amylase/trypsin inhibitor from seeds of ragi (Indian finger millet, Eleusine coracana Gaertn.) FEBS Lett., 152:300Google Scholar
  20. Carasco J. F., and Xavier-Filho, J., 1981, Sequential expression of trypsin inhibitors in developing fruit of cowpea (Vigna unguiculata (L.) Walp) Ann. Bot., 47:259.Google Scholar
  21. Carvalho, C. C. C, Jansen, G. R., and Harper, J. M., 1977, Protein quality evaluation of an instant bean powder produced by dry heat processing, J. Food Sci., 42:553.Google Scholar
  22. Chang, C.-R., and Tsen, C. C., 1979, Note on trypsin inhibitor activity in the acetate extract of cereal samples, Cereal Chem., 56:493.Google Scholar
  23. Chang, C.-R., and Tsen, C. C., 1981, Characterization and heat stability of trypsin inhibitors from rye, triticale, and wheat samples, Cereal Chem., 58:211.Google Scholar
  24. Charpentier, B. A., and Lemmel, D. E., 1984, A rapid automated procedure for the determination of trypsin inhibitor activity in soy products and common foodstuffs. J. Agric Food Chem., 32:908.Google Scholar
  25. Chen, I., and Mitchell, H. L., 1973, Trypsin inhibitors in plants, Phytochemistry, 12:327.Google Scholar
  26. Chernick, S. S., Lepkovsky, S., and Chaikoff, I. L., 1948, A dietary factor regulating the enzyme content of the pancreas: Changes induced in size and proteolytic activity of the chick pancreas by the ingestion of raw soybean meal, Am. J. Physiol., 155:33.Google Scholar
  27. Collins, J. L., and Beaty, B. F., 1980, Heat inactivation of trypsin inhibitor in fresh green soybeans and physiological responses of rats fed the beans, J. Food Sci., 45:542.Google Scholar
  28. Collins, J. L., and Sanders, G. G., 1976, Changes in trypsin inhibitor activity in some soybean varieties during maturation and germination, J. Food Sci., 41:168.Google Scholar
  29. Cuevas, R., and Cheryan, M.,1983, Inhibidores de tripsina en alimentos a base de soya: Revision critica de la cinetica de destruccion termica, y los metodos de analisis. Arch. Latinoam. Nutr., 33:902.Google Scholar
  30. del Rosario, R. R., Lozano, Y., Pamorasamit, S., and Noel, M. G., 1980, The trypsin inhibitor activity of legume seeds, Philipp. Agric., 63:339.Google Scholar
  31. de Lumen, B. O., and Belo, P. S., Jr., 1981, Inhibitors of trypsin and chymotrypsin in winged beans (Psophocarpus tetragonolobus) tubers, J. Agric. Food Chem., 29:884.Google Scholar
  32. del Valle, F. R., Escobedo, M., Munoz, M. J., Ortega, R., and Bourges, H., 1983, Chemical and nutritional studies on mesquite beans (Prosopis juliflora), J. Food Sci., 48:914.Google Scholar
  33. del Valle, F. R., Villaneuva, H., Reyes-Govea, J., Escobedo, M., Bourges, H., Ponce, J., and Munoz, M. J., 1981, Development, evaluation and industrial production of a powdered soy-oats infant formula using a low-cost extruder, J. Food Sci., 46:192.Google Scholar
  34. Deshpande, S. S., Sathe, S. K., Salunkhe D. K., and Cornforth, D. P., 1982, Effects of dehulling on phytic acid, polyphenols, and enzyme inhibitors of dry beans (Phaseolus vulgaris L.), J. Food Sci., 47:184Google Scholar
  35. Doell, B. H., Ebden, C. J., and Smith, C. A., 1981, Trypsin inhibitor activity of conventional foods which are part of the British diet and some soya products, Qual. Plant. Plant Foods Hum. Nutr., 31:139.Google Scholar
  36. Egberg, D. C, Potter, R. H., and Honold, G. R., 1975, The semiautomated determination of trypsin inhibitors in textured soy protein, J. Agri. Food Chem., 23:603.Google Scholar
  37. Ekpenyong, T. E., and Borchers, R. L., 1981, Some toxic factors in winged bean seeds. 1. Antitrypsin, hemagglutinating and urease activities, Nutr. Rep. Int., 23:865.Google Scholar
  38. Eldridge, A. C, Warner, K., and Wolf, W. J., 1977, Alcohol treatment of soybeans and soybean protein products, Cereal Chem., 54:1229.Google Scholar
  39. Ellenrieder, G., Geronazzo, H., and de Bojarski, A. B., 1980, Thermal inactivation of trypsin inhibitors in aqueous extracts of soybeans, peanuts, and kidney beans: Presence of substances that accelerate inactivation, Cereal Chem. 57:25.Google Scholar
  40. Erlanger, B. F., Kokowsky, N., and Cohen, W., 1961, The preparation and properties of two new chromogenic substrates of trypsin, Arch. Biochem. Biophys. 95:271.Google Scholar
  41. Foard, D. E., Murdock, L. L., and Dunn, P. E., 1983, Engineering of crop plants with resistance to herbivores and pathogens: An approach using primary gene products, in: “Plant Molecular Biology”, Proceedings of the ARCO Solar-UCLA Symposium, R. B. ed., Goldberg, Keystone, Colorado, April 16–22, 1983, Alan R. Liss, Inc., New York.Google Scholar
  42. Foster, J. A., Rich, C. B., Berglund, N., Huber, S., Mecham, R., and Lange, G., 1979, The anti-proteolytic behavior of lathrogens, Biochem. Biophys. Acta., 587:477.Google Scholar
  43. Freed, R. C., and Ryan, D. S., 1978A, Changes in Kunitz trypsin inhibitor during germination of soybeans: An immunoelectrophoresis assay system, J. Food Sci.,43:1316.Google Scholar
  44. Freed, R. C., and Ryan, D. S., 1978B, Note on modification of the Kunitz soybean trypsin inhibitor during seed germination, Cereal Chem. 55:534.Google Scholar
  45. Freed, R. C., and Ryan, D. S., 1980, Isolation and characterization of genetic variants of the Kunitz soybean trypsin inhibitor, Biochim. Biophys. Acta, 624:562.Google Scholar
  46. Friedman, M., Grosjean, O.-K. K., and Zahnley, J. C., 1982A, Inactivation of soya bean trypsin inhibitors by thiols, J. Sci. Food Agric., 33:165.Google Scholar
  47. Friedman, M., Grosjean, O.-K. K., and Zahnley, J. C., 1982B, Cooperative effects of heat and thiols in inactivating trypsin inhibitors from legumes in solution and in the solid state, Nutr. Rep.Int., 25:743.Google Scholar
  48. Friedman, M., Grosjean, O.-K. K., and Zahnley, J. C, 1982C, Effect of disulfide bond modification on the structure and activities of enzyme inhibitors, in: “Food Protein Deterioration: Mechanisms and Functionality” ACS Symp. Series, Vol. 206, American Chemical Society, J. P. Cherry, ed. Washington, D.C.Google Scholar
  49. Friedman, M., Gumbmann, M. R., and Grosjean, O.-K. K., 1984, Nutritional improvement of soy flour, J. Nutr., 114:2241.Google Scholar
  50. Fritz, H., Trautschold, I., and Werle, E., 1974, Protease inhibitors, in: “Methods of Enzymatic Analysis,” Vol. 2, H. U. Bergmeyer, ed., Academic Press, New York.Google Scholar
  51. Fritz H., and Tschesche, H., 1971, “Proceedings of the International Research Conference on Proteinase Inhibitors,” Walter de Gruyter, Berlin.Google Scholar
  52. Fritz, H., Tschesche, H., Greene, L. J., and Truscheit, E., 1974, “Proteinase Inhibitors,” Proc 2nd Int. Res. Conf. Springer-Verlag, New York.Google Scholar
  53. Green, G. M., and Lyman, R. L., 1972, Feedback regulation of pancreatic enzyme secretion as a mechanism for trypsin inhibitor-induced hypersecretion in rats, Proc. Soc. Exp. Biol. Med., 140:6.Google Scholar
  54. Griffiths, D. W., 1979, The inhibition of digestive enzymes by extracts of field bean (Vicia faba), J. Sci. Food Agric., 30:458.Google Scholar
  55. Gupta, A. K., and Deodhar, A. D., 1975, Variation in trypsin inhibitor activity in soybean (Glycine max), Indian J. Nutr. Diet., 12:81Google Scholar
  56. Hackler, L. R., Van Buren, J. P., Steinkraus, K. H., El Rawi, I., and Hand, D. B., 1965, Effect of heat treatment on nutritive value of soymilk protein fed to weanling rats, J. Food Sci., 30:723.Google Scholar
  57. Hafez, Y. S., 1983, Nutrient composition of different varieties and strains of soybean, Nutr. Rep. Int., 28:1197.Google Scholar
  58. Hafez, Y. S., Singh, G., McLellan, M. E., and Monroe-Lord, L., 1983, Effects of microwave heating on nutritional quality of soybeans, Nutr. Rep. Int., 28:413.Google Scholar
  59. Haider, F. G., 1981, Inactivation studies on the trypsin inhibitor activity of green gram cultivars, Nutr. Rep. Int., 23:1167.Google Scholar
  60. Hamerstrand, G. E., Black, L. T., and Glover, J. D., 1981, Trypsin inhibitors in soy products: Modification of the standard analytical procedure, Cereal Chem., 58:42.Google Scholar
  61. Hamid, M. A. K., Bhartia, P., and Mostowy, N. J., 1975, Microwave bean roaster, J. Microwave Power, 10:109.Google Scholar
  62. Harper, J., and del Valle, F. R., 1979, Mexican soy plant, Chilton’s Food Eng.Int., 4:(6)22.Google Scholar
  63. Harper, J. M., and Jansen, G. R., 1981, “Nutritious Foods Produced by Low-Cost Technology,” LEG Report 10, Colorado State University, Fort Collins, CO.Google Scholar
  64. Hass, G. M., Hermodson, M. A., Ryan, C. A., and Gentry, L., 1982, Primary structures of two low molecular weight proteinase inhibitors from potatoes, Biochemistry, 21:752.Google Scholar
  65. Hass, G. M., Nau, H., Biemann, K., Grahn, D. T., Ericsson, L. H. and Neurath, H., 1975, The amino acid sequence of a carboxypeptidase inhibitor from potatoes, Biochemistry, 14:1334.Google Scholar
  66. Hildebrand, D. F., Hettiarachchy, N. S., Hymowitz, T., and Erdman, J. W., Jr., 1981, Electrophoretic separation and properties of winged bean seed trypsin inhibitor, J. Sci. Food Agric., 32:443.Google Scholar
  67. Hill, B. S., Synder, H. E., and Wiese, K. L., 1982, Use of the pH stat to evaluate trypsin inhibitor and tryptic proteolysis of soy flours, J. Food Sci., 47:2018.Google Scholar
  68. Hove, E. I., and King, S., 1979, Trypsin inhibitor contents of lupin seeds and other grain legumes, N. Z. J. Agric. Res., 22:41.Google Scholar
  69. Huang, D. Y., Swanson, B. G., Ryan, C. A., 1981, Stability of proteinase inhibitors in potato tubers during cooking, J. Food Sci., 46:287.Google Scholar
  70. Ida, E. I., da Silva, R. S. F., Fabre-Sanches, S., Perre da Silva, M. A., and Reddy, K. V., 1983, Trypsin inhibitor inactivation during hydrothermal processing: A mathematical model, Lebensm. Wiss. Technol., 16:81.Google Scholar
  71. Ikeda, K., and Kusano, T., 1983, In-vitro inhibition of digestive enzymes by indigestible polysaccharides, Cereal Chem., 60:260.Google Scholar
  72. Jaffe, W. G., and Vega Lette, C. L., 1968, Heat-labile growth-inhibiting factors in beans (Phaseolus vulgaris), J. Nutr., 94:203.Google Scholar
  73. Jansen, G. R., Harper, J. M. and O’Deen, L. A., 1978, Nutritional evaluation of full-fat soy flour produced by dry heat roasting, J. Food Sci., 43:1350.Google Scholar
  74. Jones, G., Moore, S., and Stein, W. H., 1963, Properties of chromatogra-phically purified trypsin inhibitors from lima beans, Biochemistry, 2:66.Google Scholar
  75. Joubert, F. J., 1982, Proteinase inhibitors from Erythrina lysistemon seed, Phytochemistry, 21:1213.Google Scholar
  76. Kadam, S. S., and Salunkhe, D. K., 1984, Winged bean in human nutrition, CRC Grit. Rev. Food Sci. Nutr., 21:1.Google Scholar
  77. Kakade, M. L., Rackis, J. J., McGhee, J. E., and Puski, G., 1974, Determination of trypsin inhibitor activity of soy products: A collaborative analysis of an improved procedure, Cereal Chem., 51:376.Google Scholar
  78. Kakade, M. L., Simons, N., and Liener, I. E., 1969, An evaluation of natural vs. synthetic substrates for measuring the antitryptic activity of soybean samples, Cereal Chem., 46:518.Google Scholar
  79. Kakade, M. L., Simons, N. R., Liener, I. E., and Lambert, J. W., 1972, Biochemical and nutritional assesment of different varieties of soybeans, J. Agric. Food Chem., 20:87.Google Scholar
  80. Kamalakannan, V., and Motlag, D. B., 1982, Effect of Rhizopus oligosporus (NRRL 2710) fermentation on the trypsin inhibitors of black gram (Vigna mungo), Can. J. Microbiol., 28:54.Google Scholar
  81. Kao, C., and Robinson, R. J., 1978, Nutritional aspects of fermented foods from chickpea, horsebean, and soybean, Cereal Chem., 55:512.Google Scholar
  82. Kapoor, A. C., and Gupta, Y. P., 1978, Trypsin inhibitor activity in soybean seed as influenced by stage of its development and different treatments, and the distribution in its anatomical parts, Indian J. Nutr. Diet., 15:429.Google Scholar
  83. Kas, J., Fukal, L., Kasafirek, E., Cap, M., and Solc, J., 1983, Assay of trypsin inhibitor and its application to thermally treated horse bean (Vicia faba), Sb. Vys. Sk. Chem. Technol. Praze, Potraviny E56:177.Google Scholar
  84. Katunuma, N., Umezawa, H., and Holzer, H., 1983, “Proteinase Inhibitors: Medical and Biological Aspects”, Japan. Sci. Soc. Press, Tokyo.Google Scholar
  85. Khor, H.-T., Tan, N.-H., and Wong, K.-C., 1982, The protein, trypsin inhibitor and lipid of the winged bean [Psophocarpus tetragonolobus (L) DC] seeds, J. Sci. Food Agric., 33:996.Google Scholar
  86. Klose, A. A., Hill, B., and Fevold, H. L., 1948, Food value of soybean protein as related to processing, Food Technol., 2:201.Google Scholar
  87. Koide, T., and Ikenaka, T., 1973, Studies on soybean trypsin inhibitors. 3. Amino-acid sequence of the carboxyl-terminal region and the complete amino-acid sequence of soybean trypsin inhibitor (Kunitz), Eur. J. Biochem., 32:417.Google Scholar
  88. Kouzeh-Kanani, M., Van Zuilichem, D. J., Roosen, J. P., Pilnik, W., Van Delden, J. R., and Stolp, W., 1983, Infrared processing of soybeans, Qual. Plant. Plant Foods Hum. Nutr., 33:139Google Scholar
  89. Kozlowska, H., Elkowicz, K., and Rutkowski, A., 1980, Thermal inactivation of trypsin inhibitors of soybean preparations added to meat, Meat Sci., 4:95.Google Scholar
  90. Krahn, J., and Stevens, F. C., 1970, Lima bean trypsin inhibitor. Limited proteolysis by trypsin and chymotrypsin, Biochemistry, 9:2646.Google Scholar
  91. Krahn, J., and Stevens, F. C., 1973, Peptide-bond hydrolysis equilibria in the antitrypsin site of lima bean protease inhibitor, Biochemistry, 12:1330.Google Scholar
  92. Kunitz, M., 1945, Crystallization of a trypsin inhibitor from soybeans, Science, 101:668.Google Scholar
  93. Kunitz, M., 1946, Crystalline soybean trypsin inhibitor, J. Gen. Physiol., 29:149.Google Scholar
  94. Kunitz, M., 1947, Isolation of a crystalline protein compound of trypsin and of soybean trypsin-inhibitor, J. Gen. Physiol., 30:311.Google Scholar
  95. Kute, L. S., Kadam, S. S., and Salunkhe, D. K., 1984, Changes in sugars, starch and trypsin inhibitor activity in winged bean (Psophocarpus tetragonolobus L.DC) during seed development, J. Food Sci., 49:314.Google Scholar
  96. Labuza, T. P., 1973, Effects of dehydration and storage, Food Technol., 27:(1)20.Google Scholar
  97. Lehnhardt, W. F., and Dills, H. G., 1984, Unpublished method, A. E. Staley Manufacturing Co., Decatur, IL.Google Scholar
  98. Levison, D. A., Morgan, R. G. H., Brimacombe, J. S., Hopwood, D., Coghill, G., and Wormsley, K. G., 1979, Carcinogenic effects of di(2-hydroxy-propyl) nitrosamine (DHPN) in male Wistar rats: Promotion of pancreatic cancer by a raw soya flour diet, Scand. J. Gastroenterol., 14:217.Google Scholar
  99. Liener, I. E., 1972, Nutritional value of food protein products, in: “Soybeans: Chemistry and technology,” Vol I, Proteins, A. K. Smith and S. J. Circle, eds. Avi Publishing, Westport CT.Google Scholar
  100. Liener, I. E., 1975, Effects of anti-nutritional and toxic factors on the quality and utilization of legume proteins, in: “Protein nutritional quality of foods and feeds,” Part 2, Quality Factors-Plant Breeding, Composition, Processing, and Antinutrients, M. Friedman, ed., Marcel Dekker, Inc., New York.Google Scholar
  101. Liener, I. E., 1976, Legume toxins in relation to protein digestibility — A review, J. Food Sci., 41:1076.Google Scholar
  102. Liener, I. E., 1981, Factors affecting the nutritional quality of soya products, J. Am. Oil Chem. Soc., 58:406.Google Scholar
  103. Liener, I. E., 1983, Naturally occurring toxicants in foods and their significance in the human diet, Arch. Toxicol. Suppl., 6:153.Google Scholar
  104. Liener, I. E., and Kakade, M. L., 1980, Protease inhibitors, in: “Toxic constituents of Plant Foodstuffs,” 2nd ed., I. E. Liener, ed., Academic Press, New York.Google Scholar
  105. Lorensen, E., Prevosto, R., and Wilson, K. A., 1981, The appearance of new active forms of trypsin inhibitor in germinating mung bean (Vigna radiata) seeds, Plant Physiol., 68:88.Google Scholar
  106. Madar, Z., Gertler, A., and Birk, Y., 1979, The fate of the Bowman-Birk trypsin inhibitor from soybeans in the digestive tract of chicks, Comp. Biochem. Physiol. A, 62A:1057.Google Scholar
  107. McNaughton, J. L., and Reece, F. N., 1980, Effect of moisture content and cooking time on soybean meal urease index, trypsin inhibitor content, and broiler growth, Poult. Sci., 59:2300.Google Scholar
  108. McGuinness, E. E., Hopwood, D., and Wormsley, K. G., 1982, Further studies of the effects of raw soya flour on the rat pancreas, Scand. J. Gastroenterol., 17:273.Google Scholar
  109. McGuinness, E. E., Morgan, R. G. H., and Wormsley, K. G., 1984, Effects of soybean flour on the pancreas of rats, EHP, Environ. Health Perspect., 56:205.Google Scholar
  110. Mahoney, W. C., Hermodson, M. A., Jones, B., Powers, D. D., Corfman, R. S., and Reeck, G. R., 1984, Amino acid sequence and secondary structural analysis of the corn inhibitor of trypsin and activated Hageman factor, J. Biol. Chem., 259:8412.Google Scholar
  111. Melville, J. C, and Ryan, C. A., 1972, Chymotrypsin inhibitor I from potatoes. Large scale preparation and characterization of its subunit components, J. Biol. Chem., 247:3445.Google Scholar
  112. Millar, D. B. S., Willick, G. E., Steiner, R. F., and Frattali, V., 1969, Soybean inhibitors. IV. The reversible self-association of a soybean proteinase inhibitor, J. Biol. Chem., 244:281.Google Scholar
  113. Morgan, R. G. H., Levison, D. A., Hopwood, D., Sanders, J. H. B., and Wormsley, K. G., 1977, Potentiation of the action of azaserine on the rat pancreas by raw soya flour, Cancer Lett., 3:87.Google Scholar
  114. Mustakas, G. C., Albrecht, W. J., Bookwalter, G. M., McGhee, J. E., Kwolek, W. F., and Griffin, E. L., Jr., 1970, Extruder-processing to improve nutritional quality, flavor, and keeping quality of full-fat soy flour, Food Technol., 24:1290.Google Scholar
  115. Mustakas, G. C., Moulton, K. J., Baker, E. C., and Kwolek, W. F., 1981, Critical processing factors in desolventizing-toasting soybean meal for feed, J. Am. Oil Chem. Soc., 58:300.Google Scholar
  116. Nielsen, S. S. and Liener, I. E., 1984, Degradation of the major storage protein of Phaseolus vulgaris during germination, Plant Physiol., 74:494.Google Scholar
  117. Nordal, J. and Fossum, K., 1974, The heat stability of some trypsin inhibitors in meat products, with special reference to added soybean protein, Z. Lebensm. Unters.-Forsch., 154:144.Google Scholar
  118. Norioka, S. and Ikenaka, T., 1983, Amino acid sequence of a trypsin-chymotrypsin inhibitor, B-III, of peanut (Arachis hypogaea), J. Biochem., 93:479.Google Scholar
  119. Noor, M. I., Bressani, R., and Elias, L. G., 1980, Changes in chemical and selected biochemical components, protein quality, and digestibility of mung bean (Vigna radiata) during germination and cooking, Qual. Plant. Plant Foods Hum. Nutr., 30:135.Google Scholar
  120. Odani, S., and Ikenaka, T., 1972, Studies on soybean trypsin inhibitors. IV. Complete amino acid sequence and the anti-proteinase sites of Bowman-Birk soybean proteinase inhibitor, J. Biochem., 71:839.Google Scholar
  121. Odani, S., and Ikenaka, T., 1973A, Studies on soybean trypsin inhibitors. VIII. Disulfide bridges in soybean Bowman-Birk proteinase inhibitor, J. Biochem., 74:697.Google Scholar
  122. Odani, S., and Ikenaka, T., 1973B, Scission of soybean Bowman-Birk proteinase inhibitor into two small fragments having either trypsin or chymotrypsin inhibitory activity, J. Biochem., 74:857.Google Scholar
  123. Odani, S., and Ikenaka, T., 1977, Studies on soybean trypsin inhibitors. XI. Complete amino acid sequence of a soybean trypsin-chymo-trypsin-elastase inhibitor, C-II, J. Biochem., 82:1523.Google Scholar
  124. Odani, S., and Ikenaka, T., 1978, Studies on soybean trypsin inhibitors. XII. Linear sequences of two soybean double-headed trypsin inhibitors, D-II and E-I, J. Biochem., 83:737.Google Scholar
  125. Odani, S., Koide, T., and Ono, T., 1983, The complete amino acid sequence of barley trypsin inhibitor, J. Biol. Chem., 258:7998.Google Scholar
  126. Ologhobo, A. D., and Fetuga, B. L., 1983, Trypsin inhibitor activity in some limabean (Phaseolus lunatus) varieties as affected by different processing methods, Nutr. Rep. Int., 27:41.Google Scholar
  127. Osborne, T. B., and Mendel, L. B., 1917, The use of soy bean as food, J. Biol. Chem., 32:369.Google Scholar
  128. Ozawa, K., and Laskowski, M. Jr., 1966, The reactive site of trypsin inhibitors, J. Biol. Chem., 241:3955.Google Scholar
  129. Pearce, G., McGinnis, J., and Ryan, C. A., 1983, Effects of feeding a carboxypeptidase inhibitor from potatoes to newly hatched chicks, Proc. Soc. Exp. Biol. Med., 173:447.Google Scholar
  130. Phillips, R. D., Chhinnan, M. S., and Mendoza, L. G., 1983, Effect of temperature and moisture content on the kinetics of trypsin inhibitor activity, protein in vitro digestibility and nitrogen solubility of cowpea flour, J. Food Sci., 48:1863.Google Scholar
  131. Possompes, B., Choi-Schin, I. S., and Besancon, P., 1979, Digestive transit in rats receiving an alkali-treated casein, Ann. Biol. Anim. Biochim. Biophys., 19(3B):907.Google Scholar
  132. Pour-El, A., Nelson, S. O., Peck, E. E., Tjhio, B., and Stetson, L. E., 1981, Biological properties of VHF- and microwave-heated soybeans, J. Food Sci., 46:880.Google Scholar
  133. Price, M. L., and Butler, L. G., 1980, Tannins and nutrition, Station Bulletin no. 272, March, 1980, Agricultural Experiment Station, Purdue University, West Lafayette, IN.Google Scholar
  134. Rackis, J. J., 1965, Physiological properties of soybean trypsin inhibitors and their relationship to pancreatic hypertrophy and growth inhibition of rats, Fed. Proc., 24:1488.Google Scholar
  135. Rackis, J. J., 1966, Soybean trypsin inhibitors: Their inactivation during meal processing, Food Technol., 20:1482.Google Scholar
  136. Rackis, J. J., 1972, Biologically active components, in: “Soybeans: Chemistry and Technology,” Vol. I, Proteins, A. K. Smith and S. J. Circle, eds., Avi Publishing, Westport, CT.Google Scholar
  137. Rackis, J. J., 1974, Biological and physiological factors in soybeans, J. Am. Oil Chem. Soc., 51:161A.Google Scholar
  138. Rackis, J. J., 1978, Biochemical changes in soybeans: Maturation, post-harvest storage and processing, and germination, in: “Postharvest Biology and Biotechnology,” H. O. Hultin and M. Milner, eds., Food and Nutrition Press, Westport, CT.Google Scholar
  139. Rackis, J. J., 1981, Comparison of the food value of immature, mature, and germinated soybeans, in: “Quality of selected fruits and vegetables of North America,” R. Teranishi and H. Barrera-Benitez, eds., ACS Symposium series 170, American Chemical Society, Washington, D.C.Google Scholar
  140. Rackis, J. J., and Gumbmann, M. R., 1981, Protease inhibitors: Physiological properties and nutritional significance, in: “Antinutrients and Natural Toxicants in Foods,” R. L. Ory, ed., Food and Nutrition Press, Inc., Westport, CT.Google Scholar
  141. Rackis, J. J., Gumbmann, M. R., and Liener, I. E., 1985, The USDA trypsin inhibitor study. I. Background, objectives, and procedural details, Qual. Plant. Plant Foods Hum. Nutr. 35: 213.Google Scholar
  142. Rackis, J. J., McGhee, J. E., and Booth, A. N., 1975A, Biological threshold levels of soybean trypsin inhibitors by rat bioassay, Cereal Chem., 52:85.Google Scholar
  143. Rackis, J. J., McGhee, J. E., Gumbmann, H. R., and Booth, A. N., 1979, Effects of soy proteins containing trypsin inhibitors in long term feeding studies in rats, J. Am. Oil Chem. Soc., 56:162.Google Scholar
  144. Rackis, J. J., McGhee, J. E., Honig, D. H., and Booth, A. N., 1975B, Processing soybeans into foods: Selected aspects of nutrition and flavor, J. Am. Oil Chem. Soc., 52:249A.Google Scholar
  145. Rackis, J. J., McGhee, J. E., Leiner, I. E., Kakade, M. L., and Puski, G., 1974, Problems encountered in measuring trypsin inhibitor activity of soy flour. Report of a collaborative analysis, Cereal Sci. Today, 19:513.Google Scholar
  146. Raghavan, G. S. V., and Harper, J. M., 1974, High temperature drying using a heated bed of granular salt, Trans. ASAE, 17:108.Google Scholar
  147. Read, J. W., and Haas, L. W., 1938, Studies on the baking quality of flour as affected by certain enzyme actions. V. Further studies concerning potassium bromate and enzyme activity, Cereal Chem., 15:59.Google Scholar
  148. Richardson, M., 1974, Chymotryptic inhibitor I from potatoes. The amino acid sequence of subunit A, Biochem. J., 137:101.Google Scholar
  149. Richardson, M., 1977, The proteinase inhibitors of plants and microorganisms, Phytochemistry, 16:159.Google Scholar
  150. Richardson, M., 1979, The complete amino acid sequence and the trypsin reactive (inhibitory) site of the major proteinase inhibitor from the fruits of aubergine (Solanum melongena L.), FEBS Lett., 104:322.Google Scholar
  151. Richardson, M., 1981. Protein inhibitors of enzymes, Food Chem., 6:235.Google Scholar
  152. Richardson, M., and Cossins, L., 1974, Chymotryptic inhibitor I from potatoes: The amino acid sequences of subunits B, C and D, FEBS Lett., 45:11.Google Scholar
  153. Rockland, L. B., and Nishi, S. K., 1979, Tropical grain legumes, in: “Tropical Foods: Chemistry and Nutrition,” Vol. 2, G. E. Inglett and G. Charalambous, eds., Academic Press, New York.Google Scholar
  154. Rockland, L. B., and Radke, T. M., 1981, Legume protein quality, Food Technol., 36:(3)79.Google Scholar
  155. Roy, D. N., and Bhat, R. V., 1974, Trypsin inhibitor content in some varieties of soyabean (Glycine max L.) and sunflower seeds (Helian-thus annus L.), J. Sci. Food Agric., 25:765.Google Scholar
  156. Ryan, C. A., 1973, Proteolytic enzymes and their inhibitors in plants, Ann. Rev. Plant Physiol., 24:173.Google Scholar
  157. Ryan, C. A., 1979, Proteinase inhibitors, in: “Herbivores: Their Interaction With Secondary Plant Metabolites,” G. A. Rosenthal and D. H. Janzen, eds., Academic Press, New York.Google Scholar
  158. Ryan, C. A., Huisman, O. C., and Van Denburgh, R. W., 1968, Transitory aspects of a single protein in tissues of Solanum tuberosum and its coincidence with the establishment of new growth, Plant Physiol., 43;589.Google Scholar
  159. Ryan, C. A., Kuo, T., Pearce, G., and Kunkel, R., 1976, Variability in the concentration of three heat stable proteinase inhibitor proteins in potato tubers, Amer. Potato J., 53:443.Google Scholar
  160. Ryan, C. A., and Pearce, G., 1978, Proteinase inhibitor proteins as genetic markers for identifying high protein potato clones, Am. Potato J., 55:351.Google Scholar
  161. Sanderson, J. E., Freed, R. C., and Ryan, D. S., 1982, Thermal denaturation of genetic variants of the Kunitz soybean trypsin inhibitor, Biochim. Biophys. Acta, 701:237.Google Scholar
  162. Sarett, H. P., 1976, Soy-based infant formulas, in: “World Soybean Research,” L. D. Hill, ed., The Interstate Printers and Publishers, Danville, IL.Google Scholar
  163. Sathe, S. K., Deshpande, S. S., and Salunkhe, D. K., 1984A, Dry beans of Phaseolus. A Review. Part I. Chemical composition: Proteins, CRC Grit. Rev. Food Sci. Nutr., 20:1.Google Scholar
  164. Sathe, S. K., Deshpande, S. S., and Salunkhe, D. K., 1984B, Dry beans of Phaseolus. A Review. Part 2. Chemical composition: Carbohydrates, fiber, minerals, vitamins and lipids, CRC Crit. Rev. Food Sci. Nutr., 21:41.Google Scholar
  165. Sathe, S. K., and Salunkhe, D. K., 1981, Studies on trypsin and chymotrypsin inhibitory activities, hemagglutinating activity, and sugars in the Great Northern beans (Phaseolus vulgaris L.), J. Food Sci., 46:626.Google Scholar
  166. Senti, F. R., 1982, Annotated bibliographies on pancreatic changes in experimental animals fed soybeans, processed soybean products, soybean trypsin inhibitor, or cholecystokinin-pancreozymin, and anti-nutritional factors in processed soybean products, Report prepared for Bureau of Foods, Food and Drug Administration, Washington, D.C.Google Scholar
  167. Sessa, D. J., 1984, Are toasted soybean flour proteins responsible for trypsin inhibitor activity?, J. Am. Oil Chem. Soc., 61:Abstract no. 226, 691.Google Scholar
  168. Sgarbieri, V. C., and Whitaker, J. R., 1982, Physical, chemical, and nutritional properties of common bean (Phaseolus) proteins, Adv. Food Res., 28:93.Google Scholar
  169. Sharma, Y. K., Gupta, A. K., Gangrade, G. A., and Deodhar, A. D., 1975, Trypsin inhibitor activity in soybean at different stages of development, Indian J. Entomol., 36:62.Google Scholar
  170. Smith, O. B., 1976, Extrusion cooking, in: “New Protein Foods,” Vol. 2, Technology, Part B, A. M. Altschul, ed., Academic Press, New York.Google Scholar
  171. Smith, A. K., and Circle, S. J., 1972, “Soybeans: Chemistry and Technology,” Vol. 1, Proteins, Avi Publishing Co., Westport,CT.Google Scholar
  172. Smith, C, Van Megen, W., Twaalhoven, L., and Hitchcock, C., 1980, The determination of trypsin inhibitor levels in foodstuffs, J. Sci. Food Agric., 31:341.Google Scholar
  173. Soni, G. L., Singh, T. P., and Singh, R., 1978, Comparative studies on the effects of certain treatments on the antitryptic activity of the common Indian pulses, Ind. J. Nutr. Diet., 15:341.Google Scholar
  174. Sri Kantha, S. S., and Erdman, J. W., Jr., 1984, The winged bean as an oil and protein source. A review, J. Am. Oil Chem. Soc., 61:515.Google Scholar
  175. Stinson, C. T., and Snyder, H. E., 1980, Evaluation of heated soy flours by measurement of tryptic hydrolysis using a pH stat, J. Food Sci., 45:936.Google Scholar
  176. Sweet, R. M., Wright, H. T., Janin, J., Chothia, C. H., and Blow, D. M.,1974, Crystal structure of the complex of porcine trypsin with soybean trypsin inhibitor (Kunitz) at 2.6-A resolution, Biochemistry, 13:4212.Google Scholar
  177. Tan, C. G. L., and Stevens, F. C., 1971, Amino acid sequence of lima bean protease inhibitor component IV. 2. Isolation and sequence determination of the chymotryptic peptides and the complete amino acid sequence, Eur. J. Biochem., 18:515.Google Scholar
  178. Tan, N.-H., Rahim, Z. Hj A., Khor, H.-T., and Wong, K.-C, 1984, Chymotrypsin inhibitor activity in winged beans (Psophocarpus tetragonolobus), J. Agric. Food Chem., 32:163.Google Scholar
  179. Tan, N.-H., and Wong, K.-C, 1982, Thermal stability of trypsin inhibitor activity in winged bean (Psophocarpus tetragonolobus), J. Agric. Food Chem., 30:1140.Google Scholar
  180. Tan-Wilson, A. L., Rightmire, B. R., and Wilson, K. A., 1982, Different rates of metabolism of soybean proteinase inhibitors during germination, Plant Physiol., 70:493.Google Scholar
  181. Thorn, K. A., Tinsley, A. M., Weber, C. W., and Berry, J. W., 1983, Anti-nutritional factors in legumes of the Sonoran Desert, Ecol. Food Nutr., 13:251.Google Scholar
  182. Troll, W., and Yavelow, J., 1983, Protease inhibitors as anticarcinogens, in: “Diet, Nutrition and Cancer: From Basic Research to Policy Implications,” Proc. Workship Cornell Univ., Ithaca, N.Y., D. A. Roe, ed., Alan R. Liss, New York.Google Scholar
  183. Tsukamoto, I., Miyoshi, M., and Hamaguchi, Y., 1983, Heat inactivation of trypsin inhibitor in Kintoki bean (Phaseolus vulgaris), Cereal Chem., 60:194.Google Scholar
  184. Umezawa, H,, and Aoyagi, T., 1983, Trends in research of low molecular weight protease inhibitors of microbial origin, in: “Proteinase Inhibitors: Medical and Biological Aspects,” N. Katunuma, H. Umezawa, and H. Holzer, eds., Japan Sci. Soc. Press, Tokyo.Google Scholar
  185. Valdebouze, P., 1977, Trypsin inhibitor and hemagglutinating activities in seeds of some legume species, in: “Protein Quality from Leguminous Crops,” Office for Official Publication of the European Communities, Cmmission of the European Communities; Luxembourg.Google Scholar
  186. Valdebouze, P., Bergeron, E., Gaborit, T., and Delort-Laval, J., 1980, Content and distribution of trypsin inhibitors and hemagglutinins in some legume seeds, Can. J. Plant Sci., 60:695.Google Scholar
  187. Vimont-Rispoli, S., Possompes, B., and Besancon, P., 1980, Formation of trypsin inhibitors during alkaline treatments of protein, C. R. Seances Acad, Sci. Ser. D., 291:945.Google Scholar
  188. Vogel, R., Trautschold, I., and Werle, E., 1968, “Natural Proteinase Inhibitors,” Academic Press, New York.Google Scholar
  189. Wang, H. L., 1983, Oriental soybean foods, in: “CRC Handbook of Processing and Utilization in Agriculture,” Vol. II, Part 2, Plant products, I. A. Wolff, ed., CRC Press, Boca Raton, FL.Google Scholar
  190. Wang, H. L., Vespa, J. B., and Hesseltine, C W., 1972, Release of bound trypsin inhibitors in soybeans by Rhizopus oligosporus, J. Nutr., 102:1495.Google Scholar
  191. Wang, H. L., Swain, E. W., Wallen, L. L., and Hesseltine, C. W., 1975, Free fatty acids identified as antitryptic factor in soybeans fermented by Rhizopus oligosporus, J. Nutr., 105:1351.Google Scholar
  192. Weyer, E. M., 1968, Chemistry, pharmacology, and clinical applications of proteinase inhibitors,” Ann. N.Y. Acad. Sci., 146:361.Google Scholar
  193. Wilcke, H. L., Hopkins, D. T., and Waggle, D. H., 1979, “Soy Protein and Human Nutrition,” Academic Press, New York.Google Scholar
  194. Wilson, K. A., 1980, The release of proteinase inhibitors from legume seeds during germination, Phytochemistry, 19:2517.Google Scholar
  195. Wilson, K. A., and Chen, J. C, 1983, Amino acid sequence of mung bean trypsin inhibitor and its modified forms appearing during germination, Plant Physiol., 71:341.Google Scholar
  196. Wilson, K. A., Rightmire, B. R., and Tan-Wilson, A. L., 1985, Involvement of carboxypeptidase in the degradation of the mung bean (Vigna radiata) trypsin inhibitor during germination and early seedling growth, Qual. Plant. Plant Foods Hum. Nutr., In press.Google Scholar
  197. Yoskikawa, M., Kiyohara, T., Iwasaki, T., and Yoshida, I., 1979, Modification of proteinase inhibitor II in adzuki beans during germination, Agric. Biol. Chem., 43:1989.Google Scholar

Copyright information

© Plenum Press, New York 1986

Authors and Affiliations

  • J. J. Rackis
    • 1
  • W. J. Wolf
    • 1
  • E. C. Baker
    • 1
  1. 1.Northern Regional Research CenterUSDAPeoriaUSA

Personalised recommendations