The influence of genotypic variation in protein composition on emulsifying properties of soy proteins

JAOCS, Journal of the American Oil Chemists' Society

Volumn 82, Issue 9, 2005, Pages 667-672

  Pesic, Mirjana B ^a   Vucelic Radovic, Biljana V ^a   Barac, Miroljub B ^a   Stanojevic, Sladjana P ^a  

^a UNIVERSITY OF BELGRADE   (Serbia)

Author keywords

conglycinin; Emulsifying properties; Extractability; Glycinin; Soybean genotypes; Storage protein

Indexed keywords

CROPS; EMULSIFICATION; PROTEINS;

EMULSIFYING PROPERTIES; EXTRACTABILITY; GLYCININ; SOYBEAN GENOTYPES; STORAGE PROTEIN;

GENETIC ENGINEERING;

EMULSIFICATION; FARM CROPS; GENETIC ENGINEERING; PROTEINS;

GLYCINE MAX;

EID: 33749556860     PISSN: 0003021X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11746-005-1126-x     Document Type: Article

References (23)

1. Mejia, E.G., T. Bradford, and C. Hasler, The Anticacinogenic Potential of Soybean Lectin and Lunasin, Nutr. Rev. 67:239-246
2. Kinsella, J.E., Functional Properties of Soy Proteins, J. Am. Oil Chem.Soc. 56:242-258 (1979).
3. Wagner, J.R., and J. Guéguen, Surface Functional Properties of Native, Acid-Treated, and Reduced Soy Glycinin. 2. Emulsifying Properties, J. Agric. Food Chem. 47:2181-2187 (1999).
4. Khatib, K.A., T.J. Herald, P.M. Aramouni, F. MacRitchie, and W.T. Schapaugh, Characterization and Functional Properties of Soy β-Conglycinin and Glycinin of Selected Genotypes, J. Food Sci. 67:2923-2929 (2002).
5. Molina, E., A. Papadopoulou, and D.A. Ledward, Emulsifying Properties of High Pressure Treated Soy Protein Isolate and 7S and US Globulins, Food Hydrocolloids 75:263-269 (2001).
6. Riblett, A.L., T.J. Herald, K.A. Schmidt, and K.A. Tilley, Characterization of β-Conglycinin and Glycinin Soy Protein Fractions from Four Selected Soybean Genotypes, J. Agric. Food Chem. 49:4983-4989 (2001).
7. Maruyama, N., R. Sato, Y. Wada, Y. Matsumura, H. Goto, E. Okuda, S. Nakagawa, and S. Utsumi, Structure-Physicochemical Function Relationships of Soybean β-Conglycinin Constituent Subunits, Ibid. 47:5278-5284 (1999).
8. Jeong, H.J., J.H. Park, Y. Lam, and B.O. Lumen, Characterization of Lunasin Isolated from Soybean, Ibid. 57:7901-7906 (2003)
9. Mejia, E.G., M. Vasconez, B.O. Lumen, and R. Nelson, Lunasin Concentration in Different Genotypes, Commercial Soy Protein and Isoflavone Products, Ibid. 52:5882-5887 (2004).
10. Murphy. A., and A.P. Resurreccion, Varietal and Environmental Differences in Soybean Glycinin and β-Conglycinin Content, Ibid. 52:911-920 (1984).
11. Cai, T., and K-C. Chang, Processing Effect on Soybean Storage Proteins and Their Relationship with Tofu Quality, Ibid. 47:720-727 (1999).
12. Nakamura, T., S. Utsumi, K. Kitamura, K. Harada, and T. Mori, Cultivar Differences in Gelling Characteristics of Soybean Glycinin, Ibid. 52:647-651 (1984).
13. Lowry, O.H., N.J. Rosebrough, A.L. Fair, and R.J. Randall, Protein Measurement with the Polin Phenol Reagent, J. Biol. Chem. 193:265-215 (1951).
14. Wu, W.U., N.S. Hettiarachchy, and M. Qi, Hydrophobiciiy, Solubility, and Emulsifying Properties of Soy Protein Peptides Prepared by Papain Modification and Ultrafiltration, J. Am. Oil Chem. Soc. 75:845-850 (1998).
15. Fling, S.P., and D.S. Gregerson, Peptide and Protein Molecular Weight Determination by Electrophoresis Using a High-Molarity Tris Buffer System Without Urea, Anal. Biochem. 755:83-88 (1986).
16. Davis, J., Disc Electrophoresis - II Method and Application to Human Serum Proteins, Ann. N.Y. Acad. Sci. 121:404-427 (1964).
17. Than, V.H., and K. Shibasaky, Major Proteins of Soybean Seeds. A Straightforward Fractionation and Their Characterization, J. Agric. Food Chem. 24:1117-1121 (1976)
18. Sato, W., Y. Kamata, M. Fukuda, and F. Yamauchi, Improved Isolation Method and Some Properties of Soybean Gamma-Conglycinin. Phytochemistry 23:1523-1526 (1984)
19. Kwanyuen, P., V.R. Pantalone, J.W. Burton, and R.F. Wilson, A New Approach to Genetic Alteration of Soybean Protein Composition and Quality, J. Am. Oil Chem. Soc. 74:983-987 (1997).
20. Morr, C.W., Current Status of Soy Protein Functionality in Food Systems, Ibid. 67:265-271 (1990).
21. Wagner, J.R., and J. Guéguen, Effect of Dissociation, Deamidation and Reducing Treatment on Structural and Surface Active Properties of Glycinin, J. Agric. Food Chem. 43:1993-2000 (1995).
22. Kato, A., and S. Nakai, Hydrophobicity Determined by a Fluoroscence Probe Method and Its Correlation with Surface Properties of Proteins, Biochim. Biophys. Acta 624:13-20 (1980).
23. Nakai, S.J., Structure-Functional Relationship of Food Proteins with Emphasis on the Importance of the Protein Hydrophobicity, J. Agric. Food Chem. 37:676-683 (1983).