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Genetics and Breeding of Soybeans Lacking the Kunitz Trypsin Inhibitor

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Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 199))

Abstract

The major trypsin inhibitor present in soybean [Glycine max (L.) Merrill] seed is the Kunitz trypsin inhibitor or soybean trypsin inhibitor A2 (SBTI-A2). Four forms of SBTI-A2 have been identified in the U.S. soybean germplasm collection. Three of the forms designated Ti a, Ti b, and Ti c are electrophoretically distinguishable from one another by their different Rf values of 0.79, 0.75, and 0.83, respectively. The three forms are inherited as codominant alleles in a multiple allelic series at a single locus. The fourth form which is the absence of SBTI-A2 is found in P.I. 157440 and P.I. 196168. The allele lacking SBTI-A2 is designated ti and is inherited as a simple recessive to the other three SBTI-A2 forms. Ti a is the most common SBTI-A2 allele in the germplasm collection. Ti b primarily is found in Japan and Korea. Ti c is associated with the Tohoku District, Japan. P.I. 157440 and P.I. 196168 are from Korea. Linkage studies revealed that the Ti and Ap loci are linked by 16.2 ± 1.5 map units. Three isolines of soybeans lacking the Kunitz trypsin inhibitor, derived by backcrossing P.I. 157440 to three commercial cultivars (Ti a Ti a), were released to the research community. Results of preliminary feeding trials, with chicks and young pigs, revealed that gain/feed was significantly higher in lines lacking the Kunitz trypsin inhibitor than cultivars containing the inhibitor. However, the gain/feed was lower in both feeds than commercially processed soybean meal.

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References

  • Anon. (1985). Release of five soybean isolines with Kunitz trypsin inhibitor variants L82-2024, L82-2051, L81-4590, L81-4871, and L83-4387. USDA-ARS and University of Illinois, Agricultural Experiment Station.

    Google Scholar 

  • Bajjalieh, N., Orf, J.H., Hymowitz, T. and Jensen, A.H. (1980). Response of young chicks to raw, defatted, Kunitz trypsin inhibitor variant soybeans as sources of dietary protein. Poultry Sci., 59:328–332.

    Article  CAS  Google Scholar 

  • Bidlingmeyer, U.D., Leary, T.R. and Laskowski, M.Jr. (1972). Identity of the tryptic and α-chymotryptic reactive sites on soybean trypsin inhibitor (Kunitz). Biochemistry, 11:3303–3310.

    Article  CAS  Google Scholar 

  • Booth, A.W., Robbins, A.J. and Rebelin, W.E. (1960). Effect of raw soybean meal and amino acids on pancreatic hypertrophy in rats. Proc. Soc. Exp. Biol. Med., 104:681–683.

    CAS  Google Scholar 

  • Borchers, R., Anderson, C.W., Mussehl, F.E. and Moehl, A. (1948) Trypsin inhibitors. VIII. Growth inhibiting properties of a soybean trypsin inhibitor. Arch. Biochem., 19:317–322.

    CAS  Google Scholar 

  • Bowman, D.E. (1944). Fractions derived from soybeans and navy beans which retard the tryptic digestion of casein. Proc. Soc. Exp. Biol. Med., 57:139–140.

    CAS  Google Scholar 

  • Bray, D.J. (1964). Pancreatic hypertrophy in layering pullets induced by unheated soybean meal. Poult. Sci., 43:382–384.

    Article  Google Scholar 

  • 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. Amer. J. Physiol., 155:33–41.

    CAS  Google Scholar 

  • Clark, R.W., Mies, D.W. and Hymowitz, T. (1970). Distribution of a trypsin inhibitor variant in seed proteins of soybean varieties. Crop Sci., 10:486–487.

    Article  Google Scholar 

  • Hildebrand, D.F., Orf, J.H. and Hymowitz, T.(1980). Inheritance of an acid phosphatase and its linkage with the Kunitz trypsin inhibitor in seed protein of soybeans. Crop Sci., 20:83–85.

    Article  CAS  Google Scholar 

  • Hymowitz, T. (1973). Electrophoretic analysis of SBTI-a2 in the USDA soybean germplasm collection. Crop Sci., 13:420–421.

    Article  Google Scholar 

  • Hymowitz, T. (1980). Chemical germplasm investigations in soybeans: The flotsam hypothesis. Recent Adv. Phytochemistry, 14:157–179.

    CAS  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 

  • Hymowitz, T., Mies, D.W. and Klebek, C.J. (1971). Frequency of a trypsin inhibitor variant in seed protein of four soybean populations. East Afr. Agric. For. J., 37:63–72.

    Google Scholar 

  • Hymowitz, T., Orf, J.H., Kaizuma, N. and Skorupska, H. (1978). Screening the USDA soybean germplasm collection for Kunitz trypsin inhibitor variants. Soybean Genet. Newsl., 5:19–22.

    Google Scholar 

  • Kakade, M.L., Hoffa, D.E. and I.E. Liener. (1973). Contribution of trypsin inhibitors to the deleterious effects of unheated soybeans fed to rats. J. Nutr., 103:1772–1778.

    CAS  Google Scholar 

  • Koide, T. and Ikenada, T. (1973). Studies on soybean trypsin inhibitors:3. Amino-acid sequence of the carboxyl-terminal region and the complete amino-acid seuquence of soybean trypsin inhibitor (Kunitz). Eur. J. Biochem., 32:417–431.

    Article  CAS  Google Scholar 

  • Kunitz, M.(1945). Crystallization of a soybean trypsin inhibitor from soybean. Science, 101:668–669.

    Google Scholar 

  • Liener, I.E. and Kakade, M.L.(1980). Protease inhibitors. In “Toxic Constituents of Plant Foodstuffs”, I.E. Liener, Ed., Academic Press, New York, pp. 7–71.

    Google Scholar 

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

    Article  CAS  Google Scholar 

  • Orf, J.H. (1976). Electrophoretic studies on seed proteins of Glycine max (L.) Merrill. M.S. Thesis, Graduate College, University of Illinois at Urbana-Champaign, Urbana, Illinois.

    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. (1978). Soybean linkage tests between two seed proteins and other characteristics. Soybean Genet. Newsl., 5:22–24.

    Google Scholar 

  • Orf, J.H. and Hymowitz, T. (1979a). Genetics of the Kunitz trypsin inhibitor: An antinutritional factor in soybeans. J. Amer. Oil Chemists’ Soc., 56:722–726.

    Article  CAS  Google Scholar 

  • Orf, J.H. and Hymowitz, T. (1979b). Inheritance of the absence of the Kunitz trypsin inhibitor in seed protein of soybeans. Crop Sci., 19:107–109.

    Article  CAS  Google Scholar 

  • Orf, J.H. and Hymowitz, T. (1979c). Soybean linkage tests between Ti and Le seed proteins. Soybean Genet. Newsl., 6:32.

    Google Scholar 

  • Osborne, T.B. and Mendel, L.B. (1917). The use of soybean as feed. J. Biol. Chem., 32, 369–377.

    CAS  Google Scholar 

  • Rackis, J.J. (1965). Physiological properties of soybean trypsin inhibitors and their relationship to pancreatic phypertrophy and growth inhibition of rats. Fed. Proc., 29:1488–1493.

    Google Scholar 

  • Rackis, J.J. (1972). Biologically active components. In “Soybeans: Chemistry and Technology. Volume 1. Proteins”, A.K. Smith and S.J. Circle, Eds., The AVI Publ. Co., Westport, Connecticut, pp. 158–202.

    Google Scholar 

  • Rackis, J.J., Sasame, H.A., Mann, R.K., Anderson, R.L. and Smith, A.K.(1962). Soybean trypsin inhibitors: isolation, purification and physical properties. Arch. Biochem. Biophys., 98:471–478.

    Article  CAS  Google Scholar 

  • Rackis, J.J., and Anderson, R.L. (1964). Isolation of four soybean trypsin inhibitors by DEAE-cellulose chromatography. Biochem. Biophys. Res. Commun., 15:230–235.

    Article  CAS  Google Scholar 

  • Singh, L.C., Wilson, C. and Hadley, H.H. (1969). Genetic differences in soybean trypsin inhibitors separated by disc electrophoresis. Crop Sci., 9:489–491.

    Article  CAS  Google Scholar 

  • Skorupska, H. and Hymowitz T. (1977). On the frequency distribution of alleles of two seed proteins in European soybean [Glycine max (L.) Merrill] germplasm: Implications on the origin of European soybean germplasm. Genet. Polonica, 18:217–224.

    Google Scholar 

  • Yamamoto, M. and Ikenaka, T. (1967). Studies on soybean trypsin inhibitors. I. Purification and characterization of two soybean trypsin inhibitors. J. Biochem. (Tokyo),62:141–149.

    CAS  Google Scholar 

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© 1986 Plenum Press, New York

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Hymowitz, T. (1986). Genetics and Breeding of Soybeans Lacking the Kunitz Trypsin Inhibitor. In: Friedman, M. (eds) Nutritional and Toxicological Significance of Enzyme Inhibitors in Foods. Advances in Experimental Medicine and Biology, vol 199. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-0022-0_18

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  • DOI: https://doi.org/10.1007/978-1-4757-0022-0_18

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4757-0024-4

  • Online ISBN: 978-1-4757-0022-0

  • eBook Packages: Springer Book Archive

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