Skip to main content

Abstract

Trypsin inhibitors (TIs) constitute at least 6% of the protein of soybeans (Ryan, 1973). In addition to their beneficial effects elaborated upon in this volume, high levels of protease inhibitors have both antinutritional and toxicological effects (reviewed by Gallaher and Schneeman, 1984; Rackis and Gumbmann, 1981). In the rat, dietary protease inhibitors can induce the development of pancreatic acinar cell adenoma, but the mechanistic basis, involving cholecystokinin, appears not to operate in other species, including humans (see Chapter 18). Accurate measurement of specific protease inhibitors will be important to define the human dietary exposure to protease inhibitors in epidemiological studies. Such studies should elucidate the role of protease inhibitors in preventing breast, colon, and prostatic cancer, as well as their potential contribution to human pancreatic cancer (see Chapters 1 and 18).

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 39.99
Price excludes VAT (USA)
  • Available as EPUB and PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 54.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  • Birk, Y., 1985, The Bowman-Birk inhibitor, Int. J. Peptide Protein Res. 25:113–131.

    Article  CAS  Google Scholar 

  • Brandon, D. L., and Bates, A. H., 1988, Definition of functional and antibody-binding sites on Kunitz soybean trypsin inhibitor isoforms using monoclonal antibodies, J. Agric. Food Chem. 36:1336–1341.

    Article  CAS  Google Scholar 

  • Brandon, D. L., Bates, A. H., Friedman, M., and Corse, J. W., 1986a, Monitoring nutritional and toxicological changes in processed foods using monoclonal antibodies, in: Food Processing, Online International, New York, pp. 27–37.

    Google Scholar 

  • Brandon, D. L., Haque, S., and Friedman, M., 1986b, Antigenicity of native and modified Kunitz soybean trypsin inhibitors, in: Nutritional and Toxicological Significance of Enzyme Inhibitors in Foods (M. Friedman, ed.), Plenum Press, New York, pp. 449–467.

    Chapter  Google Scholar 

  • Brandon, D. L., Bates, A. H., and Friedman, M., 1987a, Immunoassays for measuring beneficial and adverse changes in food proteins, in: Biotech USA 1987, Online International, New York, pp. 308–317.

    Google Scholar 

  • Brandon, D. L., Haque, S., and Friedman, M., 1987b, Interaction of monoclonal antibodies with soybean trypsin inhibitors, J. Agric. Food Chem. 35:195–200.

    Article  CAS  Google Scholar 

  • Brandon, D. L., Bates, A. H., and Friedman, M., 1988, Enzyme-linked immunoassay of soybean Kunitz trypsin inhibitor using monoclonal antibodies, J. Food Sci. 53:97–101.

    Article  Google Scholar 

  • Brandort, D. L., Bates, A. H., and Friedman, M., 1989, Monoclonal antibody-based enzyme immunoassay of the Bowman-Birk protease inhibitor of soybeans, J. Agric. Food Chem. 37:1192–1196.

    Article  Google Scholar 

  • Brandon, D. L., Bates, A. H., and Friedman, M., 1990, Monoclonal antibodies to soybean Kunitz trypsin inhibitor and immunoassay methods, U.S. Patent No. 4, 959, 310.

    Google Scholar 

  • Brandon, D. L., Bates, A. H., and Friedman, M., 1991a, ELISA analysis of soybean trypsin inhibitors in processed foods, in: Nutritional and Toxicological Consequences of Food Processing (M. Friedman, ed.), Plenum Press, New York, pp. 321–337.

    Google Scholar 

  • Brandon, D. L., Bates, A. H., and Friedman, M., 1991b, High affinity monoclonal antibodies to Bowman-Birk inhibitor and immunoassay methods, U.S. Patent No. 5, 053, 327.

    Google Scholar 

  • Catsimpoolas, N., and Leuthner, E., 1969, Immunochemical methods for detection and quantitation of Kunitz soybean trypsin inhibitor, Anal. Biochem. 31:437–447.

    Article  PubMed  CAS  Google Scholar 

  • Catsimpoolas, N., Rogers, D. A., and Meyer, E. W., 1969, Immunochemical and disc electrophoresis study of soybean trypsin inhibitor SBTIA-2, Cereal Chem. 46:136–144.

    CAS  Google Scholar 

  • Dierks, S. E., Butler, J. E., and Richerson, H. B., 1986, Altered recognition of surface adsorbed compared to antigen-bound antibodies in the ELISA, Mol. Immunol. 23:403–411.

    Article  PubMed  CAS  Google Scholar 

  • DiPietro, C. M., 1987, Heat stability and occurrence of the Kunitz and Bowman-Birk soybean protease inhibitors in soybean products: Quantitation with enzymatic and immunochemical techniques, Dissertation, University of Minnesota.

    Google Scholar 

  • DiPietro, C. M., and Liener, I. E., 1989, Heat inactivation of the Kunitz and Bowman-Birk soybean protease inhibitors, J. Agric. Food Chem. 37:39–44.

    Article  CAS  Google Scholar 

  • Domagalski, J. M., Kollipara, K. P., Bates, A. H., Brandon, D. L., Friedman, M., and Hymowitz, T., 1992, Nulls for the major soybean Bowman-Birk protease inhibitor in the genus Glycine, Crop Sci. 32:1502–1505.

    Article  CAS  Google Scholar 

  • Finney, D. J., 1964, Statistical Method in Biological Assay, Hafner, New York.

    Google Scholar 

  • Freed, R. C., and Ryan, D. S., 1978a, Changes in Kunitz trypsin inhibitors during germination of soybeans: An immunoelectrophoresis assay system, J. Food Sci. 43:1316–1319.

    Article  Google Scholar 

  • Freed, R. C., and Ryan, D. S., 1978b, Note on modification of the Kunitz soybean trypsin inhibitor during seed germination, Cereal Chem. 55:534–538.

    CAS  Google Scholar 

  • Freed, R. C., and Ryan, D. S., 1980, Isolation and characterization of genetic variants of the Kunitz soybean trypsin inhibitor, Biochim. Biophys. Acta 624:562–572.

    Article  PubMed  CAS  Google Scholar 

  • Friedman, M., and Gumbmann, M. R., 1986, Nutritional improvement of legumes through disulfide interchange, in: Nutritional and Toxicological Significance of Enzyme Inhibitors in Foods (M. Friedman, ed.), Plenum Press, New York, pp. 357–389.

    Chapter  Google Scholar 

  • Friedman, M., Grosjean, O. K., and Zahnley, J. C., 1982, Inactivation of soya bean trypsin inhibitor by thiols, J. Sci. Food Agric. 33:165–172.

    Article  PubMed  CAS  Google Scholar 

  • Friedman, M., Levin, C. E., and Noma, A. T., 1984, Factors governing lysinoalanine formation in soy proteins, J. Food Sci. 49:1282–1288.

    Article  CAS  Google Scholar 

  • Friedman, M., Gumbmann, M. R., and Brandon, D. L., 1988, Nutritional, toxicological, and immunological consequences of food processing, Front. Gastrointest. Res. 14:79–90.

    CAS  Google Scholar 

  • Friedman, M., Gumbmann, M. R., Brandon, D. L., and Bates, A. H., 1989, Inactivation and analysis of soybean inhibitors of digestive enzymes, in: Food Proteins (J. E. Kinsella and W. G. Soucie, eds.), American Oil Chemists’ Society, Champaign, 111., pp. 296–328.

    Google Scholar 

  • Friedman, M., Brandon, D. L., Bates, A. H., and Hymowitz, T., 1991, Comparison of a commercial soybean cultivar and an isoline lacking the Kunitz trypsin inhibitor: Composition, nutritional value, and effects of heating, J. Agric. Food Chem. 39:327–335.

    Article  CAS  Google Scholar 

  • Gallaher, D., and Schneeman, B. O., 1984, Nutritional and metabolic response to plant inhibitors of digestive enzymes, in: Nutritional and Toxicological Aspects of Food Safety (M. Friedman, ed.), Plenum Press, New York, pp. 299–320.

    Chapter  Google Scholar 

  • Gould, D. H., and MacGregor, J. T., 1977, Biological effects of alkali-treated protein and lysinoalanine: An overview, in: Protein Crosslinking: Nutritional and Medical Consequences (M. Friedman, ed.), Plenum Press, New York, pp. 29–48.

    Google Scholar 

  • Guesdon, J. L., Ternynck, T., and Avrameas, S., 1979, The use of avidin-biotin interaction in immunoenzymatic techniques, J. Histochem. Cytochem. 27:1131–1139.

    Article  PubMed  CAS  Google Scholar 

  • Haiti, P. N., Tan-Wilson, A. L., and Wilson, K. A., 1986, Proteolysis of Kunitz soybean trypsin inhibitor during germination, Phytochemistry 25:23–26.

    Google Scholar 

  • Hathcock, J. N., 1991, Residue trypsin inhibitor: Data needs for risk assessment, in: Nutritional and Toxicological Consequences of Food Processing (M. Friedman, ed.), Plenum Press, New York, pp. 273–279.

    Google Scholar 

  • Horisberger, M., and Tacchini-Vonlanthen, M, 1983a, Ultrastructural localization of Kunitz inhibitors on thin sections of Glycine max (soybean) cv. Maple Arrow by the gold method, Histochemistry 77:37–50.

    Article  PubMed  CAS  Google Scholar 

  • Horisberger, M., and Tacchini-Vonlanthen, M., 1983b, Ultrastructural localization of Bowman-Birk inhibitor on thin sections of Glycine max (soybean) cv. Maple Arrow by the gold method, Histochemistry 77:313–321.

    Article  PubMed  CAS  Google Scholar 

  • Hwang, D. L. R., Lin, K. T. D., Yang, W. K., and Foard, D. E., 1977, Purification, partial characterization, and immunological relationships of multiple low molecular weight protease inhibitors of soybean, Biochim. Biophys. Acta 495:369–382.

    Article  PubMed  CAS  Google Scholar 

  • Hymowitz, T., 1986, Genetics and breeding of soybeans lacking the Kunitz trypsin inhibitor, in: Nutritional and Toxicological Significance of Enzyme Inhibitors in Foods (M. Friedman, ed.), Plenum Press, New York, pp. 291–298.

    Chapter  Google Scholar 

  • Hymowitz, T., and Hadley, H. H., 1972, Inheritance of a trypsin inhibitor variant in seed protein of soybeans, Crop Sci. 12:197–198.

    Article  CAS  Google Scholar 

  • Kim, S., Hara, S., Hase, S., Ikenaka, T., Toda, H., Kitamura, K., and Kaizuma, N., 1985, Comparative study on amino acid sequences of Kunitz-type soybean trypsin inhibitors, Tia, Tib, and Tic, J. Biochem. 98:435–448.

    PubMed  CAS  Google Scholar 

  • Koide, T., and Ikenaka, T., 1973a, Studies on soybean trypsin inhibitors. 1. Fragmentation of soybean trypsin inhibitor (Kunitz) by limited proteolysis and by chemical cleavage, Eur. J. Biochem. 32:401–407.

    Article  PubMed  CAS  Google Scholar 

  • Koide, T., and Ikenaka, T., 1973b, 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. 32:417–431.

    Article  PubMed  CAS  Google Scholar 

  • Koide, T., Tsunasawa, S., and Ikenaka, T., 1973, Studies on soybean trypsin inhibitors. 2. Aminoacid sequence around the reactive site of soybean trypsin inhibitor (Kunitz), Eur. J. Biochem. 32:408–416.

    Article  PubMed  CAS  Google Scholar 

  • Kunitz, M., 1947, Crystalline soybean trypsin inhibitor. II. General properties, J. Exp. Med. 30:291–310.

    CAS  Google Scholar 

  • Lehnhardt, W. L., and Dills, H. G., 1984, Analysis of trypsin inhibitors in soy products, J. Am. Oil Chem. Soc. 61:691.

    Google Scholar 

  • Liener, E. I., and Tomlinson, S., 1981, Heat inactivation of protease inhibitors in a soybean line lacking Kunitz trypsin inhibitor, J. Food Sci. 46:1354–1356.

    Article  CAS  Google Scholar 

  • Moroz, L. A., and Yang, W. H., 1980, A specific allergen in food anaphylaxis, N. Engl. J. Med. 302:1126–1128.

    Article  PubMed  CAS  Google Scholar 

  • Nakane, P. K., and Kawaoi, A., 1974, Peroxidase-labeled antibody. A new method of conjugation, J. Histochem. Cytochem. 22:1084–1091.

    Article  PubMed  CAS  Google Scholar 

  • Obara, T., and Watanabe, Y., 1971, Heterogeneity of soybean trypsin inhibitors. II. Heat inactivation, Cereal Chem. 48:523–527.

    CAS  Google Scholar 

  • Offir, E., Trop, M., and Birk, Y., 1971, Studies on the antigenicity of trypsin inhibitors from soybeans and lima beans, Isr. J. Chem. 9:17BC–18BC.

    Google Scholar 

  • Orf, J. H., and Hymowitz, T., 1977, Inheritance of a second trypsin inhibitor variant in seed protein of soybeans, Crop Sci. 17:811–813.

    Article  CAS  Google Scholar 

  • Orf, J. H., and Hymowitz, T., 1979, Genetics of the Kunitz trypsin inhibitor: An antinutritional factor in soybeans, J. Am. Oil Chem. Soc. 56:722–726.

    Article  CAS  Google Scholar 

  • Orf, J. H., Mies, D. W., and Hymowitz, T., 1977, Qualitative changes of the Kunitz trypsin inhibitor in soybean seeds during germination as detected by electrophoresis, Bot. Gaz. 138:255–260.

    Article  CAS  Google Scholar 

  • Oste, R. E., Brandon, D. L., Bates, A. H., and Friedman, M., 1990, Effects of nonenzymatic browning reactions of the Kunitz soybean trypsin inhibitor on its interaction with monoclonal antibodies, J. Agric. Food Chem. 38:258–261.

    Article  CAS  Google Scholar 

  • Prischmann, J. A., and Hymowitz, T., 1988, Inheritance of double nulls for protein components of soybean seeds, Crop Sci. 28:1010–1012.

    Article  Google Scholar 

  • 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, Westport, CT, pp. 203–237.

    Google Scholar 

  • Rackis, J. J., Wolf, W. J., and Baker, E. C., 1986, Protease inhibitors in plant foods: Content and inactivation, in: Nutritional and Toxicological Significance of Enzyme Inhibitors in Foods (M. Friedman, ed.), Plenum Press, New York, pp. 299–347.

    Chapter  Google Scholar 

  • Rossebo, L., and Nordal, J., 1972, A serological method for the detection of trypsin inhibitor in commercial soy proteins and its use in detecting soy protein addition to raw meat, Z. Lebenst. Unters. Forsch. 147:335–338.

    Article  Google Scholar 

  • Ryan, C. A., 1973, Proteolytic enzymes and their inhibitors in plants, Annu. Rev. Plant Physiol. 24:173–196.

    Article  CAS  Google Scholar 

  • Singh, R. J., Kollipara, K. P., and Hymowitz, T., 1990, Backcross-derived progeny from soybean and Glycine tomentella Hayata intersubgeneric hybrids, Crop Sci. 30:871–874.

    Article  Google Scholar 

  • Smirnoff, P., Khalef, S., and Birk, Y, 1976, A trypsin and chymotrypsin inhibitor from chick peas Cicer arietinum, Biochem. J. 157:745–751.

    PubMed  CAS  Google Scholar 

  • Smith, G. A., and Friedman, M., 1984, Effect of carbohydrates and heat on the amino acid composition and chemically available lysine content of casein, J. Food Sci. 49:817–820, 843.

    Article  CAS  Google Scholar 

  • Tan-Wilson, A. L., Rightmire, B. R., and Wilson, K. A., 1982, Different rates of metabolism of soybean proteinase inhibitors during germination, Plant Physiol. 70:493–497.

    Article  PubMed  CAS  Google Scholar 

  • Tan-Wilson, A. L., Cosgriff, S. E., Duggan, M. C., Obach, R. S., and Wilson, K., 1985, Bowman-Birk proteinase isoinhibitor complements of soybean strains, J. Agric. Food Chem. 33:389–393.

    Article  CAS  Google Scholar 

  • Tan-Wilson, A. L., Chen, J. C., Duggan, M. C., Chapman, C., Obach, R. S., and Wilson, K. A., 1987, Soybean Bowman-Birk trypsin isoinhibitors: Classification and report of a glycine-rich trypsin inhibitor class, J. Agric. Food Chem. 35:974–980.

    Article  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Editor information

Editors and Affiliations

Rights and permissions

Reprints and permissions

Copyright information

© 1993 Springer Science+Business Media New York

About this chapter

Cite this chapter

Brandon, D.L., Bates, A.H., Friedman, M. (1993). Antigenicity of Soybean Protease Inhibitors. In: Troll, W., Kennedy, A.R. (eds) Protease Inhibitors as Cancer Chemopreventive Agents. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-2882-1_6

Download citation

  • DOI: https://doi.org/10.1007/978-1-4615-2882-1_6

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4613-6249-4

  • Online ISBN: 978-1-4615-2882-1

  • eBook Packages: Springer Book Archive

Publish with us

Policies and ethics