Food Biophysics

, Volume 6, Issue 1, pp 26–36 | Cite as

Effect of Soy Protein Subunit Composition on the Rheological Properties of Soymilk during Acidification

  • Amir Malaki Nik
  • Marcela Alexander
  • Vaino Poysa
  • Lorna Woodrow
  • Milena CorredigEmail author


The effect of soy protein subunit composition on the acid-induced aggregation of soymilk was investigated by preparing soymilk from different soybean lines lacking specific glycinin and β-conglycinin subunits. Acid gelation was induced by glucono-δ-lactone (GDL) and analysis was done using diffusing wave spectroscopy and rheology. Aggregation occurred near pH 5.8 and the increase in radius corresponded to an increase in the elastic modulus measured by small deformation rheology. Diffusing wave spectroscopy was also employed to follow acid gelation, and data indicated that particle interactions start to occur at a higher pH than the pH of onset of gelation (corresponding to the start of the rapid increase in elastic modulus). The protein subunit composition significantly affected the development of structure during acidification. The onset of aggregation occurred at a higher pH for soymilk samples containing group IIb (the acidic subunit A3) of glycinin, than for samples prepared from Harovinton (a commercial variety containing all subunits) or from genotypes null in glycinin. The gels made from lines containing group I (A1, A2) and group IIb (A3) of glycinin resulted in stiffer acid gels compared to the lines containing only β-conglycinin. These results confirmed that the ratio of glycinin/β-conglycinin has a significant effect on gel structure, with an increase in glycinin causing an increase in gel stiffness. The type of glycinin subunits also affected the aggregation behavior of soymilk.


Soymilk Gelation Colloidal properties Soybean subunits composition 


  1. 1.
    N.C. Nielsen, C.D. Dickinson, T.J. Cho et al., Characterization of the glycinin gene family in soybean. Plant Cell 1, 313–328 (1989)CrossRefGoogle Scholar
  2. 2.
    M. Adachi, Y. Takenaka, A.B. Gidamis, B. Mikami, S. Utsumi, Crystal structure of soybean proglycinin A1aB1b homotrimer. J Mol Biol 305, 291–305 (2001)CrossRefGoogle Scholar
  3. 3.
    M. Adachi, J. Kanamori, T. Masuda et al., Crystal structure of soybean 11S globulin: glycinin A3B4 homohexamer. Proc Natl Acad Sci USA 100, 7395–7400 (2003)CrossRefGoogle Scholar
  4. 4.
    K. Yagasaki, T. Takagi, M. Sakai, K. Kitamura, Biochemical characterization of soybean protein consisting of different subunits of glycinin. J Agric Food Chem 45, 656–660 (1997)CrossRefGoogle Scholar
  5. 5.
    F. Yamauchi, T. Yamagishi, S. Iwabuchi, Molecular understanding of heat induced phenomena of soybean proteins. Food Rev Int 7, 283–322 (1991)CrossRefGoogle Scholar
  6. 6.
    H. Zhang, M. Takenaka, S. Isobe, DSC and electrophoretic studies on soymilk protein denaturation. J Therm Anal Calorim 75, 719–726 (2004)CrossRefGoogle Scholar
  7. 7.
    Y.M.a.T.M.S.Utsumi, “Structure-Function Relationships of Soy Proteins,” in Food Proteins and Their Applications, (Marcel Dekker, New York, 1997), p. 257–291Google Scholar
  8. 8.
    B. German, S. Damodaran, J.E. Kinsella, Thermal-dissociation and association behavior of soy proteins. J Agric Food Chem 30, 807–811 (1982)CrossRefGoogle Scholar
  9. 9.
    C.M.M. Lakemond, H.H.J. de Jongh, H. Gruppen, A.G.J. Voragen, Differences in denaturation of genetic variants of soy glycinin. J Agric Food Chem 50, 4275–4281 (2002)CrossRefGoogle Scholar
  10. 10.
    K. Kohyama, K. Nishinari, Rheological studies on the gelation process of soybean 7S and 11S proteins in the presence of glucono-delta-lactone. J Agric Food Chem 41, 8–14 (1993)CrossRefGoogle Scholar
  11. 11.
    V. Poysa, L. Woodrow, Stability of soybean seed composition and its effect on soymilk and tofu yield and quality. Food Res Int 35, 337–345 (2002)CrossRefGoogle Scholar
  12. 12.
    S. Utsumi, S. Damodaran, J.E. Kinsella, Heat-induced interactions between soybean proteins—preferential association of 11S basic subunits and beta-subunits of 7S. J Agric Food Chem 32, 1406–1412 (1984)CrossRefGoogle Scholar
  13. 13.
    T. Nakamura, S. Utsumi, T. Mori, Interactions during heat-induced gelation in a mixed system of soybean-7S and 11S-globulins. Agric Biol Chem 50, 2429–2435 (1986)Google Scholar
  14. 14.
    C.H. Wang, S. Damodaran, Thermal gelation of globular-proteins—influence of protein conformation on gel strength. J Agric Food Chem 39, 433–438 (1991)CrossRefGoogle Scholar
  15. 15.
    K. Kohyama, Y. Sano, E. Doi, Rheological characteristics and gelation mechanism of tofu (soybean curd). J Agric Food Chem 43, 1808–1812 (1995)CrossRefGoogle Scholar
  16. 16.
    T. Nagano, Y. Fukuda, T. Akasaka, Dynamic viscoelastic study on the gelation properties of beta-conglycinin-rich and glycinin-rich soybean protein isolates. J Agric Food Chem 44, 3484–3488 (1996)CrossRefGoogle Scholar
  17. 17.
    T.D. Cai, K.C. Chang, Characteristics of production-scale tofu as affected by soymilk coagulation method: propeller blade size, mixing time and coagulant concentration. Food Res Int 31, 289–295 (1998)CrossRefGoogle Scholar
  18. 18.
    J.M.S. Renkema, T. van Vliet, Heat-induced gel formation by soy proteins at neutral pH. J Agric Food Chem 50, 1569–1573 (2002)CrossRefGoogle Scholar
  19. 19.
    S.L. Tay, C.O. Perera, Physicochemical properties of 7S and 11S protein mixtures coagulated by glucono-delta-lactone. J Food Sci 69, E139–E143 (2004)Google Scholar
  20. 20.
    S.T. Guo, T. Ono, The role of composition and content of protein particles in soymilk on tofu curding by glucono-delta-lactone or calcium sulfate. J Food Sci 70, C258–C262 (2005)CrossRefGoogle Scholar
  21. 21.
    H.L. Bhardwaj, A.S. Bhagsari, J.M. Joshi, M. Rangappa, V.T. Sapra, M.S.S. Rao, Yield and quality of soymilk and tofu made from soybean genotypes grown at four locations. Crop Sci 39, 401–405 (1999)CrossRefGoogle Scholar
  22. 22.
    S. Min, Y. Yu, S. St Martin, Effect of soybean varieties and growing locations on the physical and chemical properties of soymilk and tofu. J Food Sci 70, C8–C12 (2005)CrossRefGoogle Scholar
  23. 23.
    M. Yoshida, K. Kohyama, K. Nishinari, Gelation properties of soymilk and soybean 11S globulin from Japanese-grown soybeans. Biosci Biotechnol Biochem 56, 725–728 (1992)CrossRefGoogle Scholar
  24. 24.
    V. Poysa, L. Woodrow, K. Yu, Effect of soy protein subunit composition on tofu quality. Food Res Int 39, 309–317 (2006)CrossRefGoogle Scholar
  25. 25.
    K. Yagasaki, F. Kousaka, K. Kitamura, Potential improvement of soymilk gelation properties by using soybeans with modified protein subunit compositions. Breeding Science 50, 101–107 (2000)Google Scholar
  26. 26.
    W.J. Mullin, J.A. Fregeau-Reid, M. Butler et al., An interlaboratory test of a procedure to assess soybean quality for soymilk and tofu production. Food Res Int 34, 669–677 (2001)CrossRefGoogle Scholar
  27. 27.
    T. Ono, M.R. Choi, A. Ikeda, S. Odagiri, Changes in the composition and size distribution of soymilk protein particles by heating. Agric Biol Chem 55, 2291–2297 (1991)Google Scholar
  28. 28.
    M. Alexander, D.G. Dalgleish, Dynamic light scattering techniques and their applications in food science. Food Biophys 1, 2–13 (2006)CrossRefGoogle Scholar
  29. 29.
    D.A. Weitz, J.X. Zhu, D.J. Durian, H. Gang, D.J. Pine, Diffusing-wave spectroscopy—the technique and some applications. Phys Scr T49B, 610–621 (1993)CrossRefGoogle Scholar
  30. 30.
    M. Alexander, D.G. Dalgleish, Application of transmission diffusing wave spectroscopy to the study of gelation of milk by acidification and rennet. Colloids Surf B Biointerfaces 38, 83–90 (2004)CrossRefGoogle Scholar
  31. 31.
    T. Nakamura, S. Utsumi, K. Kitamura, K. Harada, T. Mori, Cultivar differences in gelling characteristics of soybean glycinin. J Agric Food Chem 32, 647–651 (1984)CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media, LLC 2010

Authors and Affiliations

  • Amir Malaki Nik
    • 1
  • Marcela Alexander
    • 1
  • Vaino Poysa
    • 2
  • Lorna Woodrow
    • 2
  • Milena Corredig
    • 1
    Email author
  1. 1.Department of Food ScienceUniversity of GuelphGuelphCanada
  2. 2.Agriculture and Agri-Food CanadaGreenhouse and Processing Crops Research CentreHarrowCanada

Personalised recommendations