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Original Articles

Gelling Properties of Soybean β-Conglycinin Having Different Subunit Compositions

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Pages 1091-1096 | Received 03 Dec 2003, Accepted 27 Jan 2004, Published online: 22 May 2014

  • 1) Catsimpoolas, N., and Meyer, E. W., Gelation phenomena of soybean globulins: Protein-protein interactions. Cereal Chem., 47, 559–570 (1970).
  • 2) Utsumi, S., Plant food protein engineering. In “Advances in Food and Nutrition Research Vol. 36”, ed. Kinsella, J. E., Academic Press, San Diego, CA., pp. 89–208 (1992).
  • 3) Utsumi, S., Matsumura, Y., and Mori, T., Structure-function relationships of soy protein. In “Food Proteins and Their Applications”, eds. Damodaran, S., and Paraf, A., Marcel Dekker, NY, pp. 257–291 (1997).
  • 4) Mori, T., Nakamura, T., and Utsumi, S., Gelation mechanism of soybean 11S globulin: Formation of soluble aggregates as transient intermediates. J. Food Sci., 47, 26–30 (1982).
  • 5) Nakamura, T., Utsumi, S., and Mori, T., Network structure formation in thermally induced gelation of glycinin. J. Agric. Food Chem., 32, 349–352 (1984).
  • 6) Nakamura, T., Utsumi, S., Kitamura, K., Harada, K., and Mori, T., Cultivar differences in gelling characteristics of soybean glycinin. J. Agric. Food Chem., 32, 647–651 (1984).
  • 7) Nakamura, T., Utsumi, S., and Mori, T., Effects of temperature on the different stages in thermal gelling of glycinin. J. Agric. Food Chem., 33, 1201–1203 (1985).
  • 8) Nakamura, T., Utsumi, S., and Mori, T., Mechanism of heat-induced gelation and gel properties of soybean 7S globulins. Agric. Biol. Chem., 50, 1287–1293 (1986).
  • 9) Nagano, T., Hirotsuka, M., Mori, H., Kohyama, K., and Nishinari, K., Dynamic viscoelastic study on the gelation of 7S globulin from soybeans. J. Agric. Food Chem., 40, 941–944 (1992).
  • 10) Kito, M., Moriyama, T., Kimura, Y., and Kambara, H., Changes in plasma lipid levels in young healthy volunteers by adding an extruder cooked soy protein to conventional meals. Biosci. Biotechnol. Biochem., 57, 354–355 (1993).
  • 11) Aoyama, T., Kohno, M., Saito, T., Fukui, K., Takamatsu, K., Yamamoto, T., Hashimoto, Y., Hirotsuka, M., and Kato, M., Reduction by phytate-reduced soybean β-conglycinin of plasma triglyceride level of young and adult rats. Biosci. Biotechnol. Biochem., 65, 1071–1075 (2001).
  • 12) Mori, T., Nakamura, T., and Utsumi, S., Formation of pseudoglycinins and their gel hardness. J. Agric. Food Chem., 30, 828–831 (1982).
  • 13) Nakamura, T., Utsumi, S., and Mori, T., Formation of pseudoglycinins from intermediary subunits of glycinin and their gel properties and network structure. Agric. Biol. Chem., 49, 2733–2740 (1985).
  • 14) Thanh, V. H., and Shibasaki, K., Heterogeneity of beta-conglycinin. Biochim. Biophys. Acta, 439, 326–338 (1976).
  • 15) Thanh, V. H., and Shibasaki, K., Major protein of soybean seeds: Subunit structure of β-conglycinin. J. Agric. Food Chem., 26, 692–695 (1978).
  • 16) Takahashi, K., Banba, H., Kikuchi, A., Ito, M., and Nakamura, S., An induced mutant line lacking the α subunit of β-conglycinin in soybean (Glycine max (L) merril). Breed. Sci., 44, 65–66 (1994).
  • 17) Takahashi, K., Mizuno, Y., Yumoto, S., Kitamura, K., and Nakamura, S., Inheritance of α-subunit deficiency of β-conglycinin in soybean (Glycine max (L) merril) line induced by γ-ray irradiation. Breed. Sci., 46, 251–255 (1996).
  • 18) Maruyama, N., Mohamad Ramlan, M. S., Takahashi, K., Yagasaki, K., Goto, H., Hontani, N., Nakagawa, S., and Utsumi, S., The effect of the N-linked glycan on structural features and physicochemical functions of soybean β-conglycinin homotrimers. J. Am. Oil Chem. Soc., 79, 139–144 (2002).
  • 19) Maruyama, N., Mohamad Ramlan, M. S., Takahashi, K., Yagasaki, K., Goto, H., Hontani, N., Nakagawa, S., and Utsumi, S., Structure-physicochemical function relationships of soybean β-conglycinin heterotrimers. J. Agric. Food Chem., 15, 4323–4326 (2002).
  • 20) Sarver, R. W. Jr., and Krueger, W. C., Protein secondary structure from fourier transform infrared spectroscopy: A data base analysis. Anal. Biochem., 194, 89–100 (1991).
  • 21) Kohyama, K., Murata, M., Tani, F., Sano, Y., and Doi, E., Effect of protein composition on gelation of mixtures containing soybean 7S and 11S globulins. Biosci. Biotechnol. Biochem., 59, 240–245 (1995).
  • 22) Kim, C.-S., Kamiya, S., Sato, T., Utsumi, S., and Kito, M., Improvement of nutritional value and functional properties of soybean glycinin by protein engineering. Protein Eng., 3, 725–731 (1990).
  • 23) Maruyama, N., Katsube, T., Wada, Y., Oh, M. H., Barba de la Rosa, A. P., Okuda, E., Nakagawa, S., and Utsumi, S., The roles of the N-linked glycans and extension regions of soybean β-conglycinin in folding, assembly and structural features. Eur. J. Biochem., 258, 854–862 (1998).
  • 24) Tani, F., Murata, M., Higasa, T., Goto, M., Kitabatake, N., and Doi, E., Heat induced transparent gel from hen lysozyme by a two-step heating method. Biosci. Biotechnol. Biochem., 57, 209–214 (1993).
  • 25) Laemmli, U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680–685 (1970).
  • 26) Damodaran, S., Refolding of thermally unfolded soy proteins during the cooling regime of the gelation process: Effect on gelation. J. Agric. Food Chem., 36, 262–269 (1988).
  • 27) Furukawa, T., Ohta, S., and Yamamoto, A., Texture-structure relationship in heat-induced soy protein gels. J. Texture Stud., 10, 333–346 (1979).
  • 28) Wu, J., Hamann, D. D., and Foegeding, E. A., Myosin gelation kinetic study based on rheological measurements. J. Agric. Food Chem., 39, 229–236 (1991).
  • 29) Doi, E., Gels and gelling of globular proteins. Trends Food Sci. Technol., 4, 1–5 (1993).
  • 30) Hermansson, A. M., Structure of soya glycinin and conglycinin gels. J. Sci. Food Agric., 36, 822–832 (1985).
  • 31) Renkema, J. M., Lakemond, C. M., de Jough, H. H., Gruppen, H., and van Vliet, T., The effect of pH on heat denaturation and gel forming properties of soy proteins. J. Biotechnol., 79, 223–230 (2000).

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