Czech J. Food Sci., 2012, 30(2):99-107 | DOI: 10.17221/91/2011-CJFS

Microwave-assisted phosphorylation of soybean protein isolates and their physicochemical properties

Xi-Bo Wang1, Yu-Jie Chi1,2
1 College of Food Science, Northeast Agricultural University, Harbin, Heilongjiang, P.R. China
2 Key Laboratory of Soybean Biology of Ministry of Education and Heilongjiang Province, Harbin, Heilongjiang, P.R. China

In order to improve the functional properties of soybean protein isolates (SPI), microwave-assisted phosphorylation (MAP) was applied. The result showed that after microwaving at 600 W for 3 min, the phosphorylation level of SPI reached 35.72 mg/g, emulsifying activity and stability were increased 2 times and 1.4 times, respectively, the solubility was increased by 26.0% and the apparent viscosity was decreased by 13.5%. The charge density, content of sulfhydryl groups, and surface hydrophobicity increased significantly. The infra-red spectroscopic analysis indicated PO43- primary and lysine residues for phosphoric acid esterification. The change of amide bond Ι and fluorescence spectrum of variation suggested that the MAP made the secondary and tertiary structures of SPI into a compact conformation. Compared to the regular phosphorylation, the preparation time applied in MAP of SPI was much shorter. These results indicated that MAP can be used as an efficient method to improve the functional properties of SPI.

Keywords: soybean protein; sodium tripoly phosphate; microwave-phosphorylation; emulsifying properties; molecular characteristics

Published: April 30, 2012  Show citation

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Wang X, Chi Y. Microwave-assisted phosphorylation of soybean protein isolates and their physicochemical properties. Czech J. Food Sci. 2012;30(2):99-107. doi: 10.17221/91/2011-CJFS.
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    References

    1. Chuan H.T., Yan J. (2007): Modulation of mechanical and surface hydrophobic properties of food protein films by transglutaminase treatment. Food Research International, 40: 504-509. Go to original source...
    2. Damodaran S., Anand K. (1997): Sulfhydryl-disulfide interchange-induced interparticle protein polymerization in whey protein-stabilized emulsions and its relation to emulsion stability. Journal of Agricultural and Food Chemistry, 45: 3813-3820. Go to original source...
    3. Dalgleish D.G. (1997): Absorption of protein and the stability of emulsions. Trends in Food Science & Technology, 8: 1-6. Go to original source...
    4. Gan C.Y., Cheng L.H., Easa A.M. (2008): Physicochemical properties and microstructures of soy protein isolate gels produced using combined cross-linking treatments of microbial transglutaminase and Maillard cross-linking. Food Research International, 41: 600-605. Go to original source...
    5. Hai R.H., Chi Y.J. (2009): Research of improving emulsifying property of SPI by microwave-assisted phosphorylation. Journal of Chinese Grain and Oil, 24: 36-40.
    6. Herman E.M., Helm R.M., Jung R. (2003): Genetic modification removes an immunodominant allergen from soybean. Plant Physiology, 132: 36-43. Go to original source... Go to PubMed...
    7. Hidalgo F.J., Kinsella J.E. (1989): Changes induced in beta-lactoglobulin B following interactions with linoleic acid 13-hydroperoxide. Journal of Agricultural and Food Chemistry, 37: 860-866. Go to original source...
    8. Hirotsuka M., Taniguchi H., Narita H. (1984): Functionality and digestibility of a highly phosphorylated soybean protein. Journal of Biological Chemistry, 48: 93-100. Go to original source...
    9. Jafari S.M., He Y., Bhandari B. (2007): Production of submicron emulsions by ultrasound and microfluidization techniques. Journal of Food Engineering, 82: 478-488. Go to original source...
    10. Kinsella J.E. (1979): Functional properties of soy proteins. Journal of the American Oil Chemistry Society, 227: 680-685. Go to original source...
    11. Lidstrom P., Tierney J., Wathey B., Westman J. (2001): Microwave assisted organic synthesis - a review. Tetrahedron, 57: 9225-9283. Go to original source...
    12. Luan G.Z., Cheng Y.Q., Lu Z.H. (2007): Intermolecular force of SPI solidified by alkali protease Alcalase. Journal of Agricultural Engineering, 23: 266-270.
    13. Malhotra A., Coupland J.N. (2004): The effect of surfactants on the solubility, zeta potential, and viscosity of soy protein isolates. Food Hydrocolloids, 18: 101-108. Go to original source...
    14. Matheis G., Whitaker J.R. (2007): Modification of proteins by polyphenol oxidase and peroxidase and their products. Journal of Food Biochemistry, 8: 137-162. Go to original source...
    15. Meng L.Z., Gong S.L., He Y.B. (2003): Analysis of Organic Spectrum. 2nd Ed. Wuhan University Press, WuHan: 214-215.
    16. Qi M., Hettiarachy N.S., Kalapathy U. (2006): Solubility and emulsifying properties of soy protein isolates modified by pancreatin. Journal of Food Science, 62: 1110-1115. Go to original source...
    17. Royer C.A. (2006): Probing protein folding and conformational transitions with fluorescence. Chemical Reviews, 106: 1769-1784. Go to original source... Go to PubMed...
    18. Sabina K., Frederic D., Alicia H., Andrzej L., Voilley A. (2010): Protein and glycerol contents affect physicochemical properties of soy protein isolate-based edible films. Innovative Food Science & Emerging Technologies, 11: 503-510. Go to original source...
    19. Schreiber G. (2002): Kinetic studies of protein-protein interactions. Current Opinion in Structural Biology, 12: 41-47. Go to original source... Go to PubMed...
    20. Sung H.Y., Chen H.J., Liu T.Y., Su J.C. (1983): Improvement of functionalities of soy protein isolate through chemical phosphorylation. Food Science, 48: 716-720. Go to original source...
    21. Tao W.S., Li W., Jiang Y.M. (1995): Foundation of Protein Molecules. 2nd Ed. Higher Education Press, BeiJing: 260-263.
    22. Wagner J.R., Sorgentini D.A., Añón M.C. (2000): Relation between solubility and surface hydrophobicity as an indicator of modification during preparation processes of commercial and laboratory-prepared soy protein isolates. Journal of Agricultural and Food Chemistry, 48: 3159-3165. Go to original source... Go to PubMed...
    23. Wang X.S., Tang C.H., Li B.S., Yang X.-Q., Li L., Ma C.-Y (2008): Effects of high-pressure treatment on some physicochemical and functional properties of soy protein isolates. Food Hydrocolloids, 22: 560-567. Go to original source...
    24. Zhang X., Huang L.X., Nie S.Q. (2003): FTIR characteristic of the secondary structure of insulin encapsulated within liposome. Journal of Chinese Phannaceutieal Science, 12: 11-14.
    25. Zhang K., Li Y., Ren Y. (2007): Research on the phosphorylation of soy protein isolate with sodium tripolyphosphate. Journal of Food Engineering, 79: 1233-1237. Go to original source...
    26. Zhao X., Chen F., Xue W., Lee L. (2008): FTIR spectra studies on the secondary structures of 7S and 11S globulins from soybean proteins using AOT reverse micellar extraction. Food Hydrocolloids, 22: 568-575. Go to original source...

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