Abstract
The soybean is one of the most economical and valuable agricultural commodities because of its unique chemical composition. Among cereal and other legume species, it has the highest protein content (around 40%); other legumes have a protein content between 20% and 30%, whereas cereals have a protein content in the range of 8-15%. The soybean also contains about 20% oil, the second highest content among all food legumes. (The highest oil content is found in peanut, which is about 48% on dry matter basis. The third highest oil content is chickpea, which is about 5%. The remaining food legume species have oil contents in the range of 1-3.6%) (Salunkhe et al. 1983). Other valuable components found in soybeans include phospholipids, vitamins, and minerals. Furthermore, soybeans contain many minor substances, some of which, such as trypsin inhibitors, phytates, and oligosaccharides, are known to be biologically active. Others, such as isoflavones, are just being recognized for their powerful ability to prevent human cancers and other diseases (Messina et al. 1994, Chapter 10 of this book). In this chapter the chemical components of soybeans are discussed with respect to their occurrences, properties, nutritional value, physiological roles, and assay methodology.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
Similar content being viewed by others
References
AACC, 1983. American Association of Cereal Chemists, Approved Methods. Method 7110, approved Nov. 1973, St. Paul, MN.
Abbott, T.P., Nabetani, H., Sessa, D.J., and Wold, W.J. 1996. Effects of bound water on FTIR spectra of glycinin. J. Agric. Food Chem. 44:2220–2224.
Abdullah, A., Baldwin, R.E., and Minor, H. 1984. Germination effects on flatus-causing factors and antinutrients of mung beans and two strains of small-seeded soybeans. J. Food Prot. 47:441.
Adlercreutz, H., Mousave, Y., Clark, J., Höcherstedt, K., Hämäläinen, E., Wähälä, K., Mäkelä, T., and Hase, T. 1992. Dietary phytoestrogens and cancer: in vitro and in vivo studies. J. Steroid Biochem. Mol. Biol. 41:331–337.
Ahrens, E.H., Hirsch, J., Insull, W., Tsaltas, T.T., Blomstrand, R., and Peterson, M.L. 1957. The influence of dietary fats on serum lipid levels in man. Lancet 1:943–953.
Akiyama, T., Ishida, J., Nakagawa, S., Ogawara, H., Watanabe, S., Itoch, N., Shibuya, M., and Fukami, Y. 1987. Genistein, a specific inhibitor of tyrosine protein kinase. J. Biol. Chem. 262:5592–5595.
Anderson, J.T., Grande, F., and Keys, A. 1961. Hydrogenated fats in the diet and lipids in the serum of man. J. Nutr. 75:388.
Anderson, J.W., Johnstone, B.M., and Cook-Newell, M.L. 1995. Meta-analysis of the effects of soy protein intake on serum lipids. N. Engl. J. Med. 333:276.
Anderson, R.L. 1992. Effect of steaming on soybean proteins and trypsin inhibitors. J. Am. Oil Chem. Soc. 69:1170–1176.
Anonymous 1991. The trouble with margarine. Consumer Report. March, p. 196–197.
Anthony, M.S., Clarkson, T.B., Hughes, C.L., Jr., Morgan, T.M., and Burke, G.L. 1996. Soybean isoflavones improve cardiovascular risk factors without affecting the reproductive system of prepubertal Rhesus monkeys. J. Nutr. 126:43.
Applewhite, T.H. (Ed.) 1989. Proceedings of the World Congress: Vegetable Protein Utilization in Human Foods and Animal Feedstuffs. American Oil Chemists’ Society, Champaign, IL.
Arechavaleta-Medina, F. and Snyder, H.E. 1981. Water imbibition by normal and hard soybeans. J. Am. Oil Chem. Soc. 58:976.
Argos, P., Narayana, S.V.L., and Nielsen, N.C. 1985. Structural similarity between legumin and vicilin storage proteins from legumes. EMBO J. 4:1111–1117.
ASCN/AIN. 1996. Position paper on trans fatty acids, American Society for Clinical Nutrition/American Institute of Nutrition Task Force on Trans Fatty Acids. Am. J. Clin. Nutr. 63:663–670.
Aspinall, G.O. 1988. Chemistry of soybean carbohydrates. In Proceedings of Soybean Utilization Alternatives, L. McCann (Ed.), pp. 117–129. University of Minnesota, St. Paul, MN. Feb. 16–18.
Astwood, J.D. and Fuchs, R.L. 1996. Preventing food allergy: emerging technologies. Trends Food Sci. Technol. 7:219–226.
Axelrod, B., Cheesbrough, T.M., and Laakso, S. 1981. Lipoxygenase from soybeans. Ch. 53. In Methods in Enzymology, vol. 71, p.441. Academic Press, New York.
Badley, R.A., Atkinson, D., Hauser, H., Oldani, D., Green, J.P., and Stubbs, J.M. 1975. The structural, physical and chemical properties of soybean protein glycinin. Biochim. Biophys. Acta 412:214–228.
Baker, E.C. and Mustakas, G.C. 1973. Heat inactivation of trypsin inhibitor, lipoxygenase, and urase in soybeans: effect of acid and base additives. J. Am. Oil Chem. Soc. 50:137.
Barnes, S., Kirk, M., and Coward, L. 1994. Isoflavones and their conjugates in soy foods: extraction conditions and analysis by HPLC-mass spectrometry. J. Agric. Food Chem. 42:2466–2474.
Bartholomew, R.M. and Ryan, D.S. 1980. Lack of mutagenicity of some phytoestrogens in the Salmonella/mammalian microsome assay. Mutat. Res. 78:317–320.
Bates, R.P. and Matthews, R.F. 1975. Ascorbic acid and (3-carotene in soybeans as influenced by maturity, sprouting, processing and storage. Proc. Fla. State Hort. Soc. 88:266–271.
Bau, H.M. and Debry, G. 1979. Germinated soybean protein products: chemical and nutritional evaluation. J. Am. Oil Chem. Soc. 56:160.
Beleia, A., Thu Thao, L.T., and Ida, E.I. 1993. Lowering phytic phosphorus by hydration of soybeans. J. Food Sci. 58:375–388.
Ben-Aziz, A., Crossman, S., Ascarelli, I., and Budowski, P. 1970. Linoleate oxidation induced by lipoxygenase and heme proteins: a direct spectrophotometric assay. Anal. Biochem. 34:88–100.
Bernal-Lugo, I., Castillo, A., Diaz de Leon, F., Moreno, E., and Ramirez, J. 1991. Does phytic acid influence cooking rate in common beans? J. Food Biochem. 15:367–374.
Blatny, P., Kvasnicka, F., and Kenndler, E. 1995. Determination of phytic acid in cereal grains, legumes, and feeds by capillary isotachophoresis. J. Agric. Food Chem. 43:129–133.
Birk, Y. 1961. Purification and some properties of a highly active inhibitor of trypsin and a-chymotrypsin inhibitor from soya beans. Biochem. Biophys. Acta 54:378–381.
Bodwell, C.E., and Marable, N.L. 1981. Effectiveness of methods for evaluating the nutritional quality of soybean protein. J. Am. Oil Chem. Soc. 58:475–483.
Bonanome, A. and Grundy, S.M. 1988. Effect of dietary stearie acid on plasma cholesterol and lipoprotein levels. N. Engl. J. Med. 318:1244.
Borchers, R., Mange, L.D., Nelson, S.O., and Stetson, L.E. 1982. Rapid improvement in nutritional quality of soybeans by dielectric heating. J. Food Sci. 37:333.
Borhan, M. and Snyder, H.E. 1979. Lipoxygenase destruction in whole beans by combinations of heating and soaking in ethanol. J. Food Sci. 44:586.
Bowman, D.E. 1944. Fractions derived from soybeans and navy beans which retard tryptic digestions of casein. Proc. Soc. Exp. Biol. Med. 57:139–140.
Brown, B.D., Wei, L.S., Steinberg, M.P., and Villota, R. 1982. Minimizing protein insolubilization during thermal inactivation of lipoxygenase in soybean cotyledons. J. Am. Oil Chem. Soc. 59:88.
Burkitt, D.P. 1971. Epidemiology of cancer of the colon and rectum. Cancer 28:3.
Burkitt, D.P. and Trowell, H.C. (Ed.) 1975. Refined Carbohydrate Foods and Disease, Some Implications of Dietary fiber. Academic Press, London.
Burks, A. W., Williams, L.W., Helm, R.M., Thresher, W., Brooks, J.R., and Sampson, H.A. 1991. Ch. 22, Identification of soy protein allergens in patients with atopic dermatitis and positive soy challenges; determination of change in allergenicity after heating or enzymatic digestion. In Nutritional and Toxicological Consequences of Food Processing,M. Friedman (Ed.). pp. 295–307. Plenum Press, New York.
Calderon de la Barca, A.M., Vazquez-Moreno, L., and Robles-Burgueno, M.R. 1991. Active soybean lectin in foods: isolation and quantitation. Food Chem. 39:321.
Calloway, D.H., Hickey, C.A., and Murphy, E.L. 1971. Reduction of intestinal gas-forming properties of legumes by traditional and experimental food processing methods. J. Food Sci. 36:251.
Caragay, A.B. 1992. Cancer preventive foods and ingredients. Food Technol. 46(4):65.
Carroll, K.K. and Kurowska, E. M. 1995. Soy consumption and cholesterol reduction: review of animal and human studies. J. Nutr. (suppl.) 125 (3S):594S–597S.
Cassidy, A., Bingham, S., and Setchell, H.D.R. 1994. Biological effects of a diet of soy protein rich in isoflavones on the menstrual cycle of premenopausal women. Am J. Clin. Nutr. 60:333.
Catsimpoolas, N. 1969. Isolation of glycinin subunit by isoelectric focusing in ureamercaptoethanol. FEBS Lett. 4:259–261.
Catsimpoolas, N. and Ekenstam, C. 1969. Isolation of a, 13, and ti conglycinins. Arch. Biochem. Biophys. 129:490.
Catsimpoolas, N., Campbell, T.G., and Meyer, E.W. 1969. Association-dissociation phenomenon in glycinin. Arch. Biochem. Biophys. 131:577.
Cavins, J.F., Kwolek, W.E., Inglett, G.E., and Cowan, J.C. 1972. Amino acid analysis of soybean meal: interlaboratory study. J. Asso. Off. Anal. Chem. 55:686–691.
Chang, R., Schwimmer, S. and Burr, H.K. 1977. Phytate: removal from whole dry beans by enzymatic hydrolysis and diffusion. J. Food Sci. 42:1098–1101.
Chapkin, R.S. 1992. Reappraisal of the essential fatty acids. Ch. 18. In Fatty Acids and Their Health Implications, C.K. Chow (Ed.), pp. 429–435. Marcel Dekker, New York.
Che Man, Y.B., Wei, L.S., and Nelson, A.I. 1989. Acid inactivation of soybean lipoxygenase with retention of protein solubility. J. Food Sci. 54(4):963.
Chen, B.H-Y. and Mon, C.V. 1985. Solubility and forming properties of phytate-reduced soy protein isolate. J. Food Sci. 50:1139–1142.
Chen, L.H. and Pan, S.H. 1977. Decrease of phytates during germination of pea seeds (Pisum sativum). Nutr. Rep. Int. 16:125.
Chernick, S.S., Lepkovsky, S.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.
Cheryan, M. 1980. Phytic acid interactions in food systems. CRC Crit. Rev. Food Sci. Nutr. 13:297–335.
Chow, C.K. (Ed.). 1992. Fatty Acids and Their Health Implications. Marcel Dekker, New York.
Christopher, J.P. and Axelrod, B. 1971. On the different positional specificities of peroxidation of linoleate shown by two isozymes of soybean lipoxygenase. Biochem. Biophys. Res. Commun. 44:731–736.
Coates, J.B., Medeiros, J.S., Thanh, V.H., and Nielsen, N.C. 1985. Characterization of the subunits of β-conglycinin. Arch. Biochem. Biophys. 243:184–189.
Chu, Y.-H. and Lin, J.-Y. 1993. Factors affecting the content of tocopherol in soybean oil. J. Am. Oil Chem. Soc. 70:1263–1268.
Coon, C., Akavanichan, O., and Cheng, T. 1988. The effect of oligosaccharides on the nutritive value of soybean meal. In Proceedings of Soybean Utilization Alternatives, L. McCann (Ed.), p. 203–214. University of Minn. St. Paul, MN.
Cooper, J.B., Chen, J.A., van Holst, G.-J. and Varner, J.E. 1987. Hydroxyproline-rich glycoproteins of plant cell walls. TIBS 12:24–27.
Coward, L., Barnes, N.C., Setchell, K.D.R., and Barnes, S. 1993. Genistein, daidzein, and their β-glycoside conjugates: antitumor isoflavones in soybean foods from American and Asian diets. J. Agric. Food Chem. 41:1961–1967.
Cristofaro, E., Mottu, F., and Wuhrmann, J.J. 1974. Involvement of the raffinose family of oligosaccharides in flatulence. Ch. 20. In Sugar in Nutrition, H.L. Sipple and K.W. McNutt (Ed.). Academic Press, New York.
Cruz, R., Batistela, J.C., and Wosiaski, G. 1982. Microbial a-galactosidase for soymilk processing. J. Food Sci. 46:1196.
de Muelenaere, H.J.H. 1964. Effect of heat treatment on the hemagglutinating activity of legumes. Nature 201:1029.
Deshpande, S.S., Cheryan, M., and Salunkhe, D.K. 1984. Tannin analysis of food products. CRC Crit. Rev. Food Sci. Nutr. 24:401–449.
Desikachar, H.S.R. and De, S.S. 1947. Role of inhibitors in soybeans. Science 106:421.
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.
Donatucci, D.A. 1983. The role of lectins in the nutritional toxicity of raw legumes. Ph.D. dissertation, University of Minnesota, St. Paul, MN.
Dornbos, D.L. Jr. and Mullen, R.E. 1992. Soybean seed protein and oil contents and fatty acid composition adjustments by drought and temperature. J. Am. Oil Chem. Soc. 69(3):228–231.
Eggum, B.O., and Beames, R.M. 1983. The nutritive value of seed proteins. In Seed Proteins,Biochemistry, Genetics, Nutritive Value. E. Gottschalk and H.P. Muller (Ed.). pp. 499–531. Martinus Nijhof/Junk, Hague.
Eldridge, A. and Kwolek, W. 1983. Soybean isoflavones: effect of environment and variety on composition. J. Agric. Food Chem. 31:394–396.
Eldridge, A.C., Warner, K.. and Wolf, W.J. 1977. Alcohol treatment of soybeans and soybean protein products. Cereal Chem. 54:1229.
Enig, M.G., Atal, S., Keeney, M., and Sampugna, J. 1990. Isometric trans fatty acids in the U.S. diet. J. Am. Coll. Nutr. 9:471.
Erdman, J.W. Jr. 1979. Oilseed phytates: nutritional implications. J. Am. Oil Chem. Soc. 56:736–741.
Evans, C.D., McConnell, D.G., List, G.R., and Scholfield, C.R. 1969. Structure of unsaturated vegetable oil glycerides: direct calculation from fatty acid composition. J. Am. Oil Chem. Soc. 46:421.
FAO/WHO, 1985. Energy and Protein Requirements, FAO/WHO Nutrition Meetings, Report Series 724. Food and Agriculture Organization/World Health Organization, Geneva.
FAO/WHO, 1990. Protein Quality Evaluation. FAO/WHO Nutrition Meetings, Report Series 51. Food and Agriculture Organization/World Health Organization, Rome.
Fenner, G.P. 1996. Low-temperature treatment of soybean (Glycine max) isoflavonoid aglycon extracts improves gas chromatographic resolution. J. Agric. Food Chem. 44(12):3727–3729.
Fernando, S.M. and Murphy, P.A. 1990. HPLC determination of thiamin and riboflavin in soybeans and tofu. J. Agric. Food Chem. 38:163–167.
Fleury, Y., Welti, D.H., Phillippossian, G., and Magnolato, D. 1992. Soybean (malonyl) isoflavones characterization and antioxidant properties. In Phenolic Compounds in Food and Their Effects on Health, Vol. II, M.-T. Huang, C.-T. Ho, and C.Y. Lee, (Ed.), pp. 98–113. American Chemical Society, Washington, DC.
Fontes, E.P.B., Moreira, M.A., Davies, C.S., and Nielsen, N.C. 1984. Urea-elicited changes in relative electrophoretic mobility of certain glycinin and (3-conglycinin subunits. Plant Physiol. 76:840–843.
Frazier, P.J. 1979. Lipoxygenase action and lipid binding in breadmaking. Baker’s Dig. 53(6):8–14.
Friedman, M. and Gumbmann, M.R., 1986. Nutritional improvement of soy flour through inactivation of trypsin inhibitors by sodium sulfite. J. Food Sci. 51(5):1239–1241.
Friedman, M., Brandon, D.L., Bates, A.H., and Hymowitz, T. 1991. Comparison of commercial soybean cultivar and an isoline lacking the Kunitz trypsin inhibitor: composition, nutritional value, and effects of heating. J. Agric. Food Chem. 39:327.
Fujimaki, M., Arai, S., Kirigaya, N., and Sakurai, Y. 1965. Studies of flavor compounds in soybean. Part 1. aliphatic carbonyl compounds. Agric. Biol. Chem. 29:855–858.
Fukushima, D. 1968. Internal structure of 7S and 11S globulin molecules in soybean proteins. Cereal Chem. 45:203.
Fukutake, M., Takahashi, M., Ishida, K., Kawamura, H., Sugimura, T., and Wakabayashi, K. 1996. Quantification of genistein and genistin in soybeans and soybean products. Food Chem. Toxicol. 34(5):457–461.
Gauthier, S.F., Vachon, C., Jones, J.D., and Savoie, L. 1982. Assessment of protein digestibility by in vitro enzymatic hydrolysis with simultaneous dialysis. J. Nutr. 112:1718.
German, B., Damodaran, S., and Kinsella, J.E. 1982. Thermal dissociation behavior of soy proteins. J. Agric. Food Chem. 30:807–811.
Green, G.M., Olds, B.A., Mathews, G., and Lyman, R.L. 1973. Protein as a regulator of pancreatic enzyme secretion in the rat. Proc. Soc. Exp. Biol. Med. 142:1162–1167.
Green, G.M. and Lyman, R.L. 1972. Feedback regulation of pancreatic enzyme secretion in rats. Proc. Sci. Exp. Biol. Med. 140:6–12.
Gumbmann, M.R., Spangler, W.L., Dugan, G.M., and Rackis, J.J. 1986. Safety of trypsin inhibitors in the diet: effects on the rat pancreas of long-term feeding of soy flour and soy protein isolate. In Nutritional and Toxicological Significance of Enzyme Inhibitors in Foods, M. Friedman (Ed.), p. 33. Plenum Press, New York.
Guzman, G.J. and Murphy, P.A. 1986. Tocopherols of soybean seeds and soybean curd (tofu). J. Agric. Food Chem. 34:791–795.
Hajika, M., Igita, K., and Nakazawa, Y. 1991. A line lacking all the seed lipoxygenase isozymes in soybean [Glycine max (L.) Merrill] induced by gamma-ray irradiation. Japan. J. Breed. 41:507–509.
Hammerstrand, G.E., Black, L.T., and Glover, J.D. 1981. Trypsin inhibitors in soy products: modification of the standard analysis procedure. Cereal Chem. 58:42–45.
Hammond, E.G. and Glatz, B.A. 1989. Biotechnology applied to fats and oils. Ch. 6. In Developments in Food Biotechnology, R. King and P.S.J. Cheetham (Ed.), Vol. 2 pp. 173–217. John Wiley & Sons, New York.
Harada, K., Toyokawa, Y., and Kitamura, K. 1983. Genetic analysis of the most acidic lis globulin subunit and related characters in soybean seeds. Japan. J. Breed. 33:23–30.
Hashizume, K., Nakamura, N., and Watanabe, T. 1975. Influence of ionic strength on conformation changes of soybean proteins caused by heating, and relationship of its conformation changes to gel formation. Agric. Biol. Chem. 39:1339–1347.
Hefle, S.L. 1996. The Chemistry and Biology of Food Allergens. Food Technol. 50(3)86–92.
Hegsted, D.M., McGandy, R.B., Myers, M.L., and Stare, F.J. 1965. Quantitative effects of dietary fat on serum cholesterol in man. Am. J. Clin. Nutr. 17:281–295.
Hessing, M., Bleeker, H., van Biert, M., Vlooswijk, R.A.A., and van Oort, M.G. 1994. Antigenicity of legume proteins. Food Agric. Immunol. 6:315–320.
Hettiarachchy, N.S. and Ziegler, G.R. (Ed.) 1994. Protein Functionality in Food Systems. IFT Basic Symposium Series. Marcel Dekker, Inc. New York, NY.
Hildebrand, D.F. and Hymowitz, T. 1981. Two soybean genotypes lacking lipoxygenase-1. J. Am. Oil. Chem. Soc. 58:583–586.
Hildebrand, D.F., Hamilton-Kemp, T.R., Legg, C.S., and Bookjans, G. 1988. Plant lipoxygenases: occurrence, properties, and possible functions. Current Topics Plant Biochem. Physiol. 7:201–219.
Howard, P.A., Lehnhardt, W.F., and Orthoefer, F.T. 1983. 7S and 11S vegetable protein fraction and isolation. U.S. Patent 4,368,151, Jan.11.
Hsu, H.W., Vavak, D.L., Satterlee, L.D., and Miller, G.A. 1977. A multienzyme technique for estimating protein digestibility. J. Food Sci. 42:1269.
Huang, A.S., Hsieh, O.A.L., and Chang, S.S. 1981. Characterization of the nonvolatile minor constituents responsible for the objectionable taste of defatted soybean flour. J. Food. Sci. 47:19.
Hurburgh, C.R. Jr. 1994. Long-term soybean composition patterns and their effect on processing. J. Am. Oil Chem. Soc. 71(12):1425–1427.
Hutton, K. and Foxcroft, P.D. 1975. Effect of processing temperature on some indices of nutritional significance for micronized soya beans. Proc. Nutr. Soc. 34:49A.
Hymowitz, T., Collins, F.I., Panczner, J., and Walker, W.M. 1972. Relationship between the content of oil, protein, and sugar in soybean seed. Agron. J. 64:613–616.
Hwang, K.M., Murphreee, S.A., and Sartorelli, A.C. 1974. A quantitative spectrophotomet-ric method to measure plant lectin-induced cell agglutination. Cancer Res. 34:3396.
Ibrahim, N., Puri, R.K., Kapila, S., and Unklesbay, N. 1990. Plant sterols in soybean hulls. J. Food Sci. 55:271–272.
Ikeda, K., Matsuda, Y., Katsumaru, A., Teranishi, M., Yamanoto, T., and Kishida, M. 1995. Factors affecting protein digestibility in soybean foods. Cereal Chem. 72(4):401.
Jacks, T.J., Yatsu, L.Y., and Altschul, A.M. 1967. Isolation and characterization of peanut spherosome. Plant Physiol. 42:585–597.
Johnson, C.D., Berry, M.F., and Weaver, C.M. 1985. Soybean hulls as an iron source for bread enrichment. J. Food Sci. 50:1275–1277.
Jones, P.M.B. and Boulter, D. 1983. The cause of reduced cooking rate in Phaseolus vulgaris following adverse storage conditions. J. Food Sci. 48:623–627.
JSNFS, 1984. Rice, soybean, and fish—Scientific approach to staple foods. In Japanese Society of Nutrition and Food Science. M. Fujimaki, G. Inoue, and T. Tanaka, (Ed.), Kouseikan Publishing, Tokyo.
Kakade, M.I., Simons, N., and Liener, I.E. 1969. An evaluation of natural vs. synthetic substances for measuring the antitryptic activity of soybean samples. Cereal Chem. 46:518–526.
Kakade, M.L., Hoffa, D.E., and Liener, I.E. 1973. Contribution of trypsin inhibitors to the deleterious effects of unheated soybeans fed to rats. J. Nutr. 103:1172.
Kaul, R., Read, J., and Mattiasson, B. 1991. Screening for plant lectins by latex agglutination test. Phytochemistry 30:4005.
Kellor, R.L. 1974. Defatted soy flour and grits. J. Am. Oil Chem Soc. 51:77A–80A.
Kennedy, A.R. 1993. Overview: anticarcinogenic activity of protease inhibitors. In Protease Inhibitors as Cancer Chemopreventive Agents, W. Troll and A.R. Kennedy (Ed.), pp. 9–64. Plenum Publishing, New York.
Kennedy, A.R. 1994. Prevention of carcinogenesis by protease inhibitors. Cancer Res. (Suppl.) 54:1999s-2005s.
Keys, A., Anderson, J.T., and Grade, F. 1957. Prediction of serum-cholesterol responses of man to changes in fats in diet. Lancet 2:955–966.
Kikuchi, T.S., Ishii, S., Fukushima, D., and Yokotsuka, T. 1971. Food chemical studies on soybean polysaccharides. Part I. Chemical and physical properties of soybean cell wall polysaccharides and their changes during cooking. J. Agric. Chem. Soc. 45:228.
Kim, Y.A. and Barbeau, W.E. 1991. Evaluation of SDS-PAGE method for estimating protein digestibility. J. Food Sci. 56(4):1082–1086.
Kim, C.-S., Kamiya, S., Sato, T., Utsumi, S., and Kito, M. 1990. Improvement of nutritional value and functional properties of soybean glycinin by protein engineering. Protein Eng. 3:725–731.
Kinney, A.J. 1996. Soybean biotechnology: improving soybean seed quality by genetic engineering. Paper No. 21A, presented at 87th American Oil Chemists’ Society Annual Meeting & Expo, Indianapolis, IN. April 28-May 1.
Kitamura, K. 1984. Biochemical characterization of lipoxygenase lacking mutants, L-1-less, L-2-less, and L-3-less soybeans. Agric. Biol. Chem. 48:2339–2346.
Kitamura, K. 1995. Genetic improvement of nutritional and food processing quality in soybean. Jap. Agric. Res. Quart. 29:1–8.
Kitamura, K., Toyokawa, Y., and Harada, K. 1980. Polymorphism of glycinin in soybean seeds. Phytochemistry 19:1841–1843.
Kitamura, K., Davies, C.S., Katzuma, N., and Nielsen, N.C. 1983. Genetic analysis of a null-allele for lipoxygenase-3 in soybean seed. Crop. Sci. 23:924–927.
Klopfenstein, T. and Owen, F. 1988. Feeding soybean hulls to cattle. In Proceedings on Soybean Utilization Alternatives, L. McCann (Ed.), Feb. 16–18. University of Minnesota, St. Paul, MN.
Knuckles, B.E. and Betschart, A.A. 1987. Effect of phytate and other myo-inositol phosphate esters on amylase digestion of starch. J. Food Sci. 52:719.
Kobayashi, A., Tsuda, Y., Hirata, N., Kubota, K., and Kitamura, K. 1995. Aroma constituents of soybean IGlycine max (L.) Merrill] milk lacking lipoxygenase isozymes. J. Agric. Food Chem. 43:2449–2452.
Kohle, H. and Kauss, H. 1980. Improved analysis of hemagglutination assays for quantitation of lectin activity. Anal. Biochem. 103:227.
Kohyama, K. and Nishinari, K. 1993. Rheological studies on the gelation process of soybean 7S and 11S proteins in the presence of glucono-S-lactone. J. Agric. Food Chem. 41:8–14.
Koide, T., Tsunasawa, S., and Ikenaka, T. 1973. Studies on soybean trypsin inhibitors and amino acid sequence around the reactive site of soybean trypsin inhibitor (Kunitz). Eur. J. Biochem. 32:408–416.
Kon, S. and Sanshuck, D. 1981. Phytate content and its effect on cooking quality of beans. J. Food Sci. 44:1329–1335.
Kris-Etherton, P.M. and Nicolosi, R.J. 1995. Trans Fatty Acids and Coronary Heart Disease Risk. International Life Sciences Institute (ILSI) Press, Washington, D.C. pp. 1–24.
Krogdahl, A. and Holm, H. 1981. Soybean proteinase inhibitors and human proteolytic enzymes: selective inactivation of inhibitors by treatment with human gastric juice. J. Nutr. 111:2045.
Kudou, S., Fleury, Y., Welti, D., Magnolato, D., Uchida, T., Kitamura, K., and Okubo, K. 1991. Malonyl isoflavone glucosides in soybean seeds (Glycine max Merrill). Agric. Biol. Chem. 55:2227–2233.
Kunitz, M. 1945. Crystallization of a trypsin inhibitor from soybeans. Science 101:668–669.
Lalles, J.P., Dreau, D., Salmon, H., and Toullec, R. 1996. Identification of soyabean allergens and immune mechanisms of dietary sensitivities in preruminant calves. Res. Vet. Sci. 60:111–116.
Lalles, J.P. and Peltre, G. 1996. Biochemical features of grain legume allergens in humans and animals. Nutri. Rev. 54(4):101–107.
Lehnhardt, W.F., Gibson, P.W., and Orthoefer, F.T. 1983. Fraction and isolation of 7S and 11S protein from isoelectrically precipitated vegetable protein mixtures. U.S. patent 4,370,267, Jan. 25.
Lei, M.-G. and Reeck, G.R. 1987. Two-dimensional electrophoretic analysis of the proteins of isolated soybean bodies and of the glycosylation of soybean proteins. J. Agric. Food Chem. 35:296–300.
Levine, S.E., Weaver, C.M., and Kirleis, A.W. 1982. Accumulation of selected trace elements in hydroponically grown soybeans and distribution of the elements in processed soybean fractions. J. Food Sci. 47:1283.
Liener, I.E. 1953. Soyin, a toxic protein from the soybean. I. Inhibition of rat growth. J. Nutr. 49:527.
Liener, I.E. 1955. The photometric determination of the hemagglutinating activity of soyin and crude soybean extracts. Arch. Biochem. Biophys. 54:223.
Liener, I.E. 1994. Implications of antinutritional components in soybean foods. CRC Crit. Rev. Food Sci. Nutr. 34(1):31–67.
Liener, I.E., Deuel, H.J. Jr., and Frevold, H.L. 1949. The effect of supplemental methionine on the nutritive value of diets containing concentrates of the soybean trypsin inhibitor. J. Nutr. 39:325.
Liener, I.E., Goodale, R.L., Deshmukh, A., Satterberg, T.L., Ward, G., DiPietro, C.M., Bankey, P.E., and Borner, J.W. 1988. Effect of a trypsin inhibitor from soybeans (Bowman-Birk) on the secretory activity of the human pancreas. Gastroenterology 94:419–427.
Liener, I.E. and Kakade, M. 1980. Protease inhibitors. In Toxic Constituents of Plant Foodstuffs, I.E. Liener (Ed.), pp. 7–71. Academic Press, New York.
List, G.R., Evans, C.D., Warner, K., Beal, R.E., Kwolek, W.F., Black, L.T., and Moulton, K.J. 1977. Quality of oil from damaged soybeans. J. Am. Oil. Chem. Soc. 54:8.
Liu, K.S. 1986. Effects of processing and maturation on certain antinutritional factors in soybeans. M.S. thesis, Michigan State University, East Lansing, MI.
Liu, K.S. 1995. Cellular, biological and physicochemical basis for the hard-to-cook defect in legume seeds. CRC Crit. Rev. Food Sci. Nutr. 35(4):263–298.
Liu, K.S. and Markakis, P. 1987. Effect of maturity and processing on the trypsin inhibitor and oligosaccharides of soybeans. J. Food Sci. 52(1):222–223, 225.
Liu, K.S. and Markakis, P. 1989a. Trypsin inhibition assay as related to limited hydrolysis of inhibitors. Anal. Biochem. 178:159–165.
Liu, K.S. and Markakis, P. 1989b. An improved colorimetric method for determining antitryptic activity in soybean products. Cereal Chem. 66:415–422.
Liu, K.S. and Markakis, P. 1990. Effect of the reactant mixing sequence on the chymotrypsin inhibition assay. Analyst 115:1143–1145.
Liu, K.S. and Markakis, P. 1991. Aqueous ethanol extraction of soybean trypsin inhibitors and characterization of a calcium-sensitive fraction. J. Food Biochem. 15:159–168.
Liu, K.S., Markakis, P., and Smith, D. 1990. Trypsin inhibition by free fatty acids and stearoyl-CoA. J. Agric. Food Chem. 38:1475–1478.
Liu, K.S., Orthoefer, F., and Brown, E.A. 1995a. Association of seed size with genotypic variation in the chemical constituents of soybeans. J. Am. Oil Chem. Soc. 72(2):191.
Liu, K.S., Brown, E.A., and Orthoefer, F. 1995b. Fatty acid composition within each structural part and section of a soybean seed. J. Agric. Food Chem. 43:381–383.
Lolas, G.M., Palamidas, N.. and Markakis, P. 1976. The phytic acid-total phosphorus relationship in barley, oats, soybeans, and wheat. Cereal Chem. 53:876.
Lotan, R.H., Sieggelman, W., Lit, H., and Sharon, N. 1974. Subunit structure of soybean agglutinin. J. Biol. Chem. 249:1219.
Lott, J.N.A. and Buttrose, M.S. 1978. Globoids in protein bodies of legume seed cotyledons. Aust. J. Plant Physiol. 5:89–111.
Lykken, G.I., Hunt, J.R., Nielsen, E.J., and Dintzis, F.R. 1987. Availability of soybean hull iron fed to humans in a mixed Western meal. J. Food Sci. 52:1545–1548.
MacLeod, G. and Ames, J. 1988. Soy flavor and its improvement. CRC Crit. Rev. Food Sci. Nutr. 27(4):219–401.
McNiven, M.A., Grimmelt, B., MacLeod, J.A., and Voldeng, H. 1992. Biological characterization of a low trypsin inhibitor soybean. J. Food Sci. 57(6):1375–1377.
Maga, J.A. 1982. Phytate: its chemistry, occurrence, food interactions, nutritional significance, and methods of analysis. J. Agric. Food Chem. 30:1–9.
Magee, A.C. 1963. Biological responses of young rats fed diets containing genistin and genistein. J. Nutr. 80:151–156.
Mahalko, J.R., Sandstead, H.H., Johnson, L.K., Inman, L.F., Milne, D.B., Warner, R.C., and Haubnz, E.A. 1984. Effect of consuming fiber from corn bran, soy hulls, or apple powder on glucose tolerance and plasma lipids in type II diabetes. Am. J. Clin. Nutr. 39:25.
Makower, R.U. 1970. Extraction and determination of phytic acid in beans (Phaseolus vulgari.$). Cereal Chem. 47:288.
Marczy, J.S., Simon, M.L., Mozsik, L., and Szajani, B. 1995. Comparative study on the lipoxygenase activities of some soybean cultivars. J. Agric. Food Chem. 43(2):313.
Martin, M.J., Hulley, S.B., Browner, W.S., Kuller, L.H., and Wentworth, D. 1986. Serum cholesterol, blood pressure, and mortality: implications from a cohort of 361,662 men. Lancet 2:933–936.
Masai, T., Wada, K., Hayakawa, K., Yoshihara, I., and Mitsuoka, T. 1987. Effects of soybean oligosaccharides on human intestinal flora and metabolic activities. Japan J. Bacteriol. 42(1):313.
Mason, A.C., Weaver, C.M., Kimmel, S., and Brown, R.K. 1993. Effect of soybean phytate content on calcium bioavailability in mature and immature rats. J. Agric. Food Chem. 41:246–249.
Mattson, F.M. and Grundy, S.M. 1985. Comparison of effects of dietary saturated, monosaturated. and polyunsaturated fatty acids on plasma lipids and lipoproteins in man. J. Lipid Res. 26:194–202.
Mensink, R.P. and Katan, M.B. 1989. Effect of a diet enriched with monounsaturated or polyunsaturated fatty acids on levels of low-density and high-density lipoproteins in healthy women and men. New Engl. J. Med. 321:436–441.
Mensink, R.P. and Katan, M.B. 1990. Effect of dietary trans fatty acids on high-density and low density lipoprotein cholesterol levels in healthy subjects. N. Engl. J. Med. 323:439–445.
Messina, M. and Barnes, S. 1991. The role of soy products in reducing cancer risk. J. Natl. Cancer Inst. 83:541–546.
Messina, M., Messina, V., and Setchell, K.D.R. 1994. The Simple Soybean and Your Health. Avery Publishing Group, Garden City Park, New York.
Mittal, B.K. and Steinkraus, K.H. 1975. Utilization of oliogosaccharides by lactic acid bacteria during fermentation of soymilk. J. Food Sci. 40:114.
Montelongo, J-L., Chassy, B.M., and McCord, J.D. 1993. Lactobacillus salivarius for conversion of soy molasses into lactic acid. J. Food Sci. 58(4):863–866.
Moreira, M.A., Hermodson, M.A., Larkins, B.A., and Nielsen, N.C. 1979. Partial characterization of the acidic and basic polypeptides of glycinin. J. Biol. Chem. 254:9921–9926.
Moreira, M.A., Tavares, S.R., Ramos, V., and de Banos, E.G. 1993. Hexanal production and TBA number are reduced in soybean [Glycine max (L.) Men.] seeds lacking lipoxygenase isozymes 2 and 3. J. Agric. Food Chem. 41:103–106.
Morita, S., Fukase, M., Hoshino, K., Fukuda, Y., Yamaguchi, M., and Morita, Y. 1994. A serine protease in soybean seeds that acts specifically on the native a subunit of 13conglycinin. Plant Cell Physiol. 35(7): 1049–1056.
Morita, S., Fukase, M., Yamaguchi, M., Fukuda, Y., and Morita, Y. 1996. Purification, characterization, and crystallization of single molecular species of (3-conglycinin from soybean seeds. Biosci. Biotech. Biochem. 60(5): 866–873.
Moroz, L.A. and Yang, W.H. 1980. Kunitz soybean trypsin inhibitor. A specific allergen in food anaphylaxis. New Engl. J. Med. 15:1126–1128.
Murasawa, H., Sakamoto, A., Sasaki, H., and Harada, K. 1991. The effect of glycinin subunit on tofu-making. In Japan Part Proceedings of the International Conference on Soybean Processing and Utilization, K. Okubo (Ed.). pp. 53–57.
Murphy, P.A. 1985. Structural characteristics of soybean glycinin and 13-conglycinin. In World Soybean Research Conference III: Proceedings,R. Shibles (Ed.), pp. 143–151. Westview Press, Boulder, CO.
Murphy, P.A. and Resurrection, A.P. 1984. Varietal and environmental differences in soybean glycinin and 13-conglycinin concentration. J. Agric. Food Chem. 32:911.
Mustakas, G.C., Albrecht, W.J., McGhee, J.E., Black, L.T., Bookwalter, G.N., and Griffin, E.L. Jr. 1969. Lipoxidase deactivation to improve stability, odor and flavor of full-fat soy flours. J. Am. Oil Chem. Soc. 46:623.
Naim, M., Gestetner, B., Bondi, A., and Birk, Y. 1976. Antioxidative and antihemolytic activities of soybean isoflavones. J. Agric. Food Chem. 24:1174–1177.
Naismith, W.E.F. 1955. Ultracentrifuge studies on soya bean protein. Biochim. Biophys. Acta 16:203–210.
Nakamura, T., Utsumi, S., and Mori, T. 1986. Mechanism of heat-induced gelation and gel properties of soybean 7S globulin. Agric. Biol. Chem. 50:1287–1293.
Neff, W.E., Selke, E., Mounts, T.L., Rinsch, W., Frankel, E.N., and Zeitoun, M.A.M. 1992. Effect of triacylglycerol composition and structures on oxidative stability of oils from selected soybean germplasm. J. Am. Oil Chem. Soc. 69(2):111–118.
Nelson, T.S., Shieh, T.R., Wodzinski, R.L., and Ware, J.H. 1968. The availability of phytate phosphorus in soybean meal before and after treatment with a mold phytase. Poult. Sci. 47:1842.
Nelson, A.I., Steinberg, M.P., and Wei, L.S. 1976. Illinois process for separation of soymilk. J. Food Sci. 41:57–61.
Nielson, N.C. 1985a. Structure of soy proteins. Ch. 2. In New Protein Foods, Vol 5. Seed Storage Proteins, A.M. Altschul and H.L. Wilcke (Ed.), pp. 27–64. Academic Press, Orlando, FL.
Nielsen, N.C. 1985b. Structure and complexity of the 11S polypeptides in soybeans. J. Am. Oil Chem. Soc. 62(12):1680–1685.
Nishiba, Y., Furuta, S., Hajika, M., lgita, K., and Suda, I. 1995. Hexanal accumulation and DETBA value in homogenate of soybean seeds lacking two or three lipoxygenase isozymes. J. Agric. Food Chem. 43(3):738–741.
Nonaka, M., Toiguchi, S., Sakamoto, H., Kawajiri, H., Soeda, T., and Motoki, M. 1994. Changes caused by microbial transglutaminase on physical properties of thermally induced soy protein gels. Food Hydrocolloids, 8(1):1–8.
NRC-NAS. 1972. Nutritional Requirements of Laboratory Animals. No. 10. 2nd Rev. Ed.
Obata, A., Matsuura, M., and Kitamura, K. 1996. Degradation of sulfhydryl groups in soymilk by lipoxygenases during soybean grinding. Biosci. Biotech. Biochem. 60(8):1229–1232.
Odani, S. and Ikenaka, T. 1973. Studies on soybean trypsin inhibitors VIII. Disulfide bridges in soybean Bowman-Birk protease inhibitors. J. Biochem. (Tokyo) 74:697.
O’Dell, B.L. 1979. Effect of soy protein on trace mineral availability. In Soy Protein and Human Nutrition, H.L. Wilcke, D.R. Hopkins, and D.H. Waggle, (Ed.) Academic Press. New York.
O’Dell, B.L. and deBoland, A. 1976. Complexation of phytate with proteins and cations in corn germ and oilseed meals. J. Agric. Food Chem. 24:804.
Ogawa, T., Bando, N., Tsuji, H., Okajima, H., Nishikawa, K. and Sasaoka, K. 1991. Investigation of the IgE-binding proteins in soybeans by immunoblotting with the sera of the soybean-sensitive patients with atopic dermatitis. J. Nutrí. Sci. Vitaminol. 37:555–565.
Ogawa, T., Tsuji, H., Bando, N., Kitamura, K., Zhu, Y.L., Hirano, H., and Nishikawa, K. 1993. Identification of the soybean allergenic protein, Gly m Bd 30 K, with the soybean seed 34-kDa oil-body-associated protein. Biosci. Biotech. Biochem. 57:1030–1033.
Okubo, K., Iijima, M., Kobayashi, Y., Yoshikoshi, M., Uchida, T., and Kudou, S. 1992. Components responsible for the undesirable taste of soybean seeds. Biosci. Biotechnol. Biochem. 56:99–103.
Olson, A., Gray, G.M., and Chiu, M.-C. 1987. Chemistry and analysis of soluble dietary fiber. Food Technol., Feb. pp. 71–80.
Orf, J.H. 1988. Modifying soybean composition by plant breeding. In Proceedings: Soybean Utilization Alternatives, L. McCann (Ed.). p. 131. University of Minnesota, St. Paul, MN. Feb. 16–18.
Orf, J.H. and Hymowitz, T.H. 1979. Inheritance of the absence of the Kunitz inhibitor in seed protein of soybeans. Crop Sci. 19:107.
Osborne, T.B. and Mendel, L.B. 1917. The use of soybean as food. J. Biol. Chem. 32:369.
Ozawa, K. and Laskowski, M. Jr. 1966. The reactive site of trypsin inhibitor. J. Biol. Chem. 241:3955–3961.
Pallansch, M.J. and Liener, I.E. 1953. Soyin, a toxic protein from the soybean. II. Physical characterization. Arch. Biochem. Biophys. 45:366.
Park, D.K., Terao, J., and Matsushita, S. 1983. Influence of the positions of unsaturated acyl groups in glycerides on autoxidation. Agric. Biol. Chem. 47:2251–2255.
Perkins, E. G. 1995. Composition of soybeans and soy products. In Practical Handbook of Soybean Processing and Utilization, D.R. Erickson (Ed.), pp. 9–28. AOCS Press, Champaign, IL.
Pernollet, J-C. 1978. Protein bodies of seeds: ultrastructure, biochemistry, biosynthesis and degradation. Phytochemistry 17:1473–1480.
Pernollet, J-C. and Mosse, J. 1983. Structure and location of legume and cereal seed storage proteins. No. 20. In Seed Proteins, J. Daussant, J. Mosse, and J. Vaughan (Ed.), Annual Proceedings of the Phytochemical Society of Europe, pp. 155–190. Academic Press, London.
Peters, J. and Czakor, B. 1989. Effect of extrusion cooking on trypsin inhibitor activity. Nahrung 33:275.
Peterson, T.G. and Barnes, S. 1993. Genistein and biochanin A inhibit the growth of human prostate cancer cells, but not epidermal growth factor receptor tyrosine autophosphorylation. Prostate 22:335–345.
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. 46:880–885, 895.
Pratt, D.E. and Birac, P. M. 1979. Source of antioxidant activity of soybean and soy products. J. Food Sci. 44:1720–1722.
Prattley, C.A. and Stanley, D.W. 1983. Protein-phytate interactions in soybeans. I. Localization of phytate in protein bodies and globoids. J. Food Biochem. 6:243–253.
Pryde, E.H. 1980. Composition of soybean oil. Ch. 2. In Handbook of Soy Oil Processing and Utilization. S.R. Erickson, E.H. Pryde, O.L. Brekke, T.L. Mounts, and R.A. Falb, (Ed.), p. 13. American Oil Chemists’ Society, Champaign, IL.
Pull, S.P., Pueppke, S.G., Hymowitz, T., and Orf, H.H. 1978. Soybean lines lacking 120,000-Da seed lectin. Science 200:1277.
Rackis, J.J. 1974. Biological and physical factors in soybeans. J. Am. Oil Chem. Soc. 51:161A.
Rackis, J.J., Honig, D.H., Sessa, D.J., and Steggerda, F.R. 1970. Flavor and flatulence factors in soybean protein products. J. Agric. Food Chem. 18:977.
Read, R.J. and Jame, M.N.D. 1986. Introduction to the protease inhibitors: X-ray crystallography. In Protease Inhibitors, A.J. Barrett and G. Salvesen (Ed.). Elsevier, Amsterdam/ New York.
Reseland, J.E., Holm, H., Jacobsen, M.B., Jenssen, T.G., and Hanssen, L.E. 1996. Protein-ase inhibitors induce selective stimulation of human trypsin and chymotrypsin secretion. J. Nutr. 126(3):634–642.
Rios-Iriarte, B.J. and Barnes, R.H. 1966. The effect of overheating on certain nutritional properties of the protein of soybeans. Food Technol. 20:836.
Ritter, M.A., Mon, C.V., and Thomas, R.L. 1987. In vitro digestibility of phytate-reduced and phenolics-reduced soy protein isolates. J. Food Sci. 52(2):325–341.
Robinson, D.S., Wu, Z., Domoney, C., and Casey, R. 1995. Lipoxygenases and the quality of foods. Food Chem. 54:33–43.
Saio, K. 1976. Soybeans resistant to water absorption. Cereal Foods World. 21:168.
Saio, K. and Watanabe, T. 1966. Preliminary investigation on protein bodies of soybean seeds. Agric. Biol. Chem. 30:1133–1138.
Saio, K. and Watanabe, T. 1968. Observation of soybean foods under electron microscope. J. Jap. Soc. Food Sci. Technol. 15:290–296.
Saio, K., Kamiya, M., and Watanabe, T. 1969. Food processing characteristics of soybean 11S and 7S proteins. Part 1. Effect of difference of protein component among soybean varieties on formation of tofu-gel. Agric. Biol. Chem. 33:1301–1308.
Saio, K., Yamagishi, T. and Yamauchi, F. 1986. Quantitative analysis of soybean proteins by densitometry on gel electrophoresis. Cereal Chem. 63(6):493–496.
Salunkhe, D.K., Sathe, S.K., and Reddy, N.R. 1983. Legume lipids. In Chemistry and Biochemistry of Legumes, S.K. Arora (Ed.) Edward Arnold Pub. Ltd., London.
Samoto, M., Akasaka, T., Mori, H., Manabe, M., Ookura, T., and Kawamura, Y. 1994. A simple and efficient procedure for removing the 34 KD allergenic soybean protein, Gly m I, from defatted soy milk. Biosci. Biotech. Biochem. 58(11):2123–2125.
Samoto, M., Miyazaki, C., Akasaka, T.. Mori, H., and Kawamura, Y. 1996. Specific binding of allergenic soybean protein Gly m Bd 30 K with α’- and α-subunits of conglycinin in soy milk. Biosci. Biotech. Biochem. 60(6):1006–1010.
Sampson, H.A. and McCaskill, C.C. 1985. Food hypersensitivity and dermatitis: evaluation of 113 patients. J. Pediatr. 107:669–675.
Sandberg, A.S., Carlsson, N.G., and Svanberg, U. 1989. Effect of inositol, tri-, tetra-. penta-, and hexaphosphates on in vitro estimation of iron availability. J. Food Sci. 54(1): 159–161.
Sattar, A. Neelofar, and Akhtar, M.A. 1990. Irradiation and germination effects on phytate, protein, and amino acids of soybeans. Qual. Plant. Plant Foods Hum. Nutr. 40:185.
Satterlee, L.D., Kendrick, J.G., and Miller, G.A. 1977. Rapid in-vitro methods of measuring protein quality. Food Technol. 31(6):77.
Senti, F.R., (Ed.) 1985. Health Aspects of Dietary Trans Fatty Acids. Life Sciences Research Office, Federation of American Societies for Experimental Biology, Bethesda, MD.
Sharon, N. and Lis, H. 1972. Lectins: cell-agglutinating and sugar-specific proteins. Science 177:949–959.
Shibasaki, M., Suzuki, S., Tajima, S., Nemoto, H., and Kuroume T. 1980. Allergenicity of major components of soybean. Int. Arch. Allergy Appl. Immun. 61:441–448.
Simons, P.C.M., Verseegh, H.A.J., Jongbloed, A.W., Kemme, P.A., Slump, P., Bos, K.D., Wolters, M.G.E., Beudeker, R.F., and Verschoor, G.J. 1990. Improvement of phosphorus availability by microbial phytase in broilers and pigs. J. Nutr. 64:225.
Simopoulos, A.P. 1989. Executive summary, in Dietary w3 and w6 Fatty Acids—Biological Effects and Nutritional Essentiality, C. Galli and A.P. Simopoulos (Ed.), pp. 391–404. Plenum, New York.
Sirtori, C.R., Even, R., and Lovati, M.R. 1993. Soybean protein diet and plasma cholesterol: from therapy to molecular mechanisms. Ann. N. Y. Acad. Sci. 676:188.
Sissions, J.W. and Tolman, H. 1991. Anti-nutritional properties of soyabean antigens in calves. In Toxic Factors in Crop Plants. Proceedings of the Second Spring Conference, March 22, J.P.F. D’Mello and C.M. Duffus (Ed.). pp. 62–85. Edinburgh.
Skrede, A. and Krogdahl, A. 1985. Heat affects nutritional characteristics of soybean meal and excretion of proteinases in mink and chicks. Nutr. Rep. Int. 32:479.
Smith, A.K. and Circle, S.J. (Ed.) 1972. Soybeans: Chemistry and Technology. AVI Publishing, Westport, CT.
Smith, A.K. and Nash, A.M. 1961. Water absorption of soybeans. J. Am. Oil Chem. Soc. 38:120.
Smith, R.J. and Gallon, J.R. 1993. Nitrogen Fixation. Ch. 6. In Plant Biochemistry and Molecular Biology, P.J. Lea and R.C. Leegood (Ed.), pp. 129–153. John Wiley & Sons, Chichester.
Smith, C., Megen, W.V., Twaalfhoven, L., and Hitchcock, C. 1980. The determination of trypsin inhibitor levels in foodstuffs. J. Sci. Food Agric. 31:341–350.
Staswick, P.E. and Nielsen, N.C. 1983. Characterization of a soybean cultivar lacking certain glycinin subunits. Arch. Biochem. Biophys. 223:1–8.
Staswick, P.E., Hermodson, M.A., and Nielsen, N.C. 1981. Identification of the acidic and basic subunit complexes of glycinin. J. Biol. Chem. 256:8752–8755.
Steiner, R.F. and Frattali, V. 1969. Purification and properties of soybean protein inhibitors of proteolytic enzymes. J. Agric. Food Chem. 17:513–518.
Streggerda, F.R., Richards, E.A., and Rackis, J.J. 1966. Effects of various soybean products on flatulence in the adult man. Proc. Soc. Expt. Biol. Med. 121:1235–1239.
Suda, I., Hajika, M., Nishiba, Y., Furuta, S., and Igita, K. 1995. Simple and rapid method for the selective detection of individual lipoxygenase isozymes in soybean seeds. J. Agric. Food Chem. 43:742–747.
Sudarmadji, S. and Markakis, P. 1977. The phytate and phytase of soybean tempeh. J. Sci. Food Agric. 28:381–383.
Sutardi and Buckle, K.A. 1985. Reduction in phytic acid levels in soybeans during tempeh production, storage and frying. J. Food Sci. 50:260.
Sykes, G.E. and Gayler, K.R. 1981. Detection and characterization of a new (3-conglycinin from soybean seeds. Arch. Biochem. Biophys. 210:525.
Takasoye, M., Inoue, N. and Knuma, C. 1990. Clinical investigation of feces improvements by soybean oligosaccharides. Rinsho Toh Kenkyu (Clinics and Research), (in Japanese) 67:304–310.
Thanh, V.H. and Shibasaki, K. 1976a. Major proteins of soybean seeds. A straightforward fraction and their characterization. J. Agric. Food Chem. 24(6):1117–1121.
Thanh, V.H. and Shibasaki, K. 1976b. Heterogeneity of (3-conglycinin. Biochim. Biophys. Acta 439:326.
Thanh, V.H. and Shibasaki, K. 1979. Major proteins of soybean seeds. Reconstitution of (3-conglycinin from its subunits. J. Agric. Food Chem. 26:695.
Thanh, V.H., Okubo, K., and Shibasaki, K. 1975a. Isolation and characterization of the multiple 7S globulins of soybean proteins. Plant Physiol. 56:19–22.
Thanh, V.H., Okubo, K., and Shibasaki, K. 1975b. The heterogeneity of the 7S soybean protein by Sepharose gel chromatography and disc gel electrophoresis. Agric. Biol. Chem. 39(7): 1501–1503.
Thompson, D.B. and Erdman, J.W. 1982. Phytic acid determination in soybeans. J. Food Sci. 47:513–517.
Tombs, M.P. 1967. Protein bodies of soybeans. Plant Physiol. 42:797–813.
Tomomatsu, H. 1994. Health effects of oligosaccharides. Food Technol., Oct., pp. 61–65.
Torun, B., Vitery, F.E., and Young, V.R. 1981. Nutritional role of soya protein for humans. J. Am. Oil Chem. Soc. 58:400–406.
Tsien, H.C., Jack, M.A., Schmidt, E.L., and Wold, F. 1983. Lectin in five soybean cultivars previously considered to be lectin-negative. Planta 158:128.
Tsukamoto, C., Kawasakim, Y., Iwasaki, T., and Okubo, K. 1991. A process for the removal of glycosides during tofu production and an evaluation of the marketability of the final product. In Japan part of Proceedings of the International Conference on Soybean Processing and Utilization, K. Okubo (Ed.), pp. 47–51.
Tsukamoto, C., Shimada, S., Igita, K., Kudou, S., Kokubun, M., Okubo, K., and Kitamura, K. 1995. Factors affecting isoflavone content in soybean seeds: changes in isoflavones, saponins, and composition of fatty acids at different temperatures during seed development. J. Agric. Food Chem. 43:1184–1192.
Turner, R.H. and Liener, I.E. 1975. The effect of the selective removal of hemagglutinins on the nutritive value of soybeans. J. Agric. Food Chem. 23:484.
Utsumi, S. and Kinsella, J.E. 1985. Forces involved in soy protein gelation: effect of various reagents on the formation, hardness and solubility of heat-induced gels made from 7S, 11S, and soy isolate. J. Food Sci. 50:1278–1282.
Utsumi, S., Gidamis, A.B., Kanamori, J., Kang, J., and Kito, M. 1993. Effects of deletion of disulfide bonds by protein engineering on the conformation and functional properties of soybean proglycinin. J. Agric. Food Chem. 41:687–691.
Vahouny, G. and Kritchevsky, D. (Ed.) 1986. Dietary Fibers Basic and Clinical Aspects. Plenum Press, New York.
Vaintraub, I.A. and Bulmaga, V.P. 1991. Effect of phytate on the in vitro activity of digestive enzymes. J. Agric. Food Chem. 39:859.
Verdeal, K., Brown, R.R., Richardson, T., and Ryan, D.S. 1980. Affinity of phytoestrogens for estradiol binding proteins and effect of coumesterol on growth of 7,12-dimethylbenz(a)anthracene-induced rat mammary tumors. J. Natl. Cancer Inst. 64:285–290.
Vessby, B. 1994. Implications of long-chain fatty acid studies. INFORM 5(2):182–185.
Walker, A.R.P., Fox, F.W., and Irving, J.T. 1948. Human mineral metabolism. 1. Effect of bread rich in phytate phosphorus on the metabolism of certain mineral salts with special reference to calcium. J. Biochem. 42:452–462.
Walter, E.D. 1941. Genistin (an isoflavone glycoside) and its aglucone, genistein from soybeans. J. Am. Chem. Soc. 63:3273–3276.
Wang, H.-J. and Murphy, P.A. 1994a. Isoflavone composition of American and Japanese soybeans in Iowa: effects of variety, crop year and location. J. Agric. Food Chem. 42:1674–1677.
Wang, H.-J. and Murphy, P.A. 1994b. Isoflavone content in commercial soybean foods. J. Agric. Food Chem. 42:1666–1673.
Wang, H.J. and Murphy, P.A. 1996. Mass balance study of isoflavones during soybean processing. J. Agric. Food Chem. 44:2377–2383.
Wang, H.L., Swain, E.W., Wallen, L.L., and Hasseltine, C. W. Free fatty acids identified as antitryptic factor in soybeans fermented by Rhizopus oligosporus. J. Nutr. 105:1351–1355.
Wardlaw, G.M. and Snook, J.T. 1990. Effect of diets high in butter, corn oil, or high-oleic acid sunflower oil on serum lipids and apolipoproteins in man. Am. J. Clin. Nutr. 51:815–821.
Watanabe, M. 1993. Hypoallergenic rice as a physiologically functional food. Trends Food Sci. Technol. 4:125–128.
Weaver, C.M., Nelson, N., and Elliott, J.G. 1984. Bioavailability of iron to rats from processed soybean fractions determined by intrinsic and extrinsic labeling techniques. J. Nutr. 114:1042–1048.
Wheeler, E.L. and Ferrel, R.E. 1971. A method for phytic acid determination in wheat and wheat fraction. Cereal Chem. 48:312.
Whitaker, J.R. 1991. Lipoxygenase. In Oxidative Enzymes in Foods, D.S. Robinson and N.A.M. Eskin (Ed.). pp. 175–215. Elsevier Applied Sci., London.
Wilkens, W.F., Mattick, L.R., and Hand, D.B. 1967. Effect of processing method on oxidative off-flavor of soybean milk. Food Technol. 21:86.
Wilson, L.A. 1996. Comparison of lipoxygenase-null and lipoxygenase-containing soybeans for foods. Ch. 12. In Lipoxygenase and Lipoxygenase Pathway Enzymes, G.J. Piazza (Ed.), pp. 209–225. AOCS Press, Champaign, IL.
Wolf, W.J. 1969. Soybean protein nomenclature: a progress report. Cereal Sci. Today, 14:75, 76, 78, 129.
Wolf, W.J. 1993. Sulfhydryl content of glycinin: effect of reducing agents. J. Agric. Food Chem. 41:168–176.
Wolf, W.J. and Briggs, D.R. 1959. Purification and characterization of the 11S component of soybean proteins. Arch. Biochem. Biophys. 85:186–199.
Wolf, W.J. and Cowan, J.C. (Ed.). 1975. Soybeans as a Food Source. CRC Press, Cleveland, OH.
Wolf, W.J., Babcock, G.E., and Smith, A.K. 1961. Ultracentrifugal differences in soybean protein composition. Nature 191:1395–1396.
Wong, E. and Flux, D.S. 1962. Estrogenic activity of red clover isoflavones and some of their degradation products. J. Endocrinol. 24:341–348.
Woodham, A.A. and Deans, P.S. 1975. Amino acid requirements of growing chickens. Br. Poult: Sci. 16:269–287.
Wu, Y.V. and Sessa, D.J. 1994. Conformation of Bowman-Birk inhibitor. J. Agric. Food Chem. 42:2136–2138.
Yabuuchi, S., Lister, R.M., Axelrod, B., Wilcox, J.R., and Nielsen, N.C. 1982. Enzyme-linked immunosorbent assay for the determination of lipoxygenase isoenzymes in soybean. Crop Sci. 22:333–337.
Yamauchi, F., Sato, M., Sato, W., Kamata, Y., and Shibasaki, K. 1981. Isolation and identification of a new type of (3-conglycinin in soybean globulins. Agric. Biol. Chem. 45:2863–2868.
Yamauchi, F., Yamagishi, T.. and Iwabuchi, S. 1991. Molecular understanding of soybean protein. Food Rev. Int. 7:283–322.
Young, V.R. 1991. Soy protein in relation to human protein and amino acid nutrition. J. Am. Diet. Asso. 91(7):828–835.
Young, V.R. and Janghorbani, M. 1981. Soy proteins in human diets in relation to bioavailability of iron and zinc: a brief review. Cereal Chem. 58:12.
Young, V.R. and Scrimshaw, N.S. 1978. Nutritional evaluation of protein and protein requirements. In Protein Resources and Technology, M. Milner, N.S. Scrimshaw, and D.I.C. Wang (Ed.). AVI Publishing, Westport, CT.
Young, V.R., Bier, D.M., and Pellett, P.L. 1989. A theoretical basis for increasing current estimates of the amino acid requirements in adult man, with experimental support. Am. J. Clin. Nutr. 50:80–92.
Zarkadas, C.G., Yu, Z., Voldeng, H.D., and Minero-Amador, A. 1993. Assessment of the protein quality of a new high-protein soybean cultivar by amino acid analysis. J. Agric. Food Chem. 41:616–623.
Zemel, M. 1984. In vitro evaluation of the effect of ortho-, tripoly-and hexametaphosphate on zinc, iron and calcium bioavailability. J. Food Sci. 49:1562–1565.
Zock, P.L. and Katan, M.B. 1992. Hydrogenation alternatives: effects of trans fatty acids and stearic acid versus linoleic acid on serum lipids and lipoproteins in humans. Lipid Res. 33:399.
Zuo, Y., Fahey, G.C., Merchen, N.R., and Bajjalieh, N.L. 1996. Digestion responses to low oligosaccharide soybean meal by ileally-cannulated dogs. J. Animal Sci. 74(10):2441–2449.
Author information
Authors and Affiliations
Rights and permissions
Copyright information
© 1997 Springer Science+Business Media Dordrecht
About this chapter
Cite this chapter
Liu, K. (1997). Chemistry and Nutritional Value of Soybean Components. In: Soybeans. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-1763-4_2
Download citation
DOI: https://doi.org/10.1007/978-1-4615-1763-4_2
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4613-5711-7
Online ISBN: 978-1-4615-1763-4
eBook Packages: Springer Book Archive