754
Views
22
CrossRef citations to date
0
Altmetric
ARTICLES

Conjugation of functional oligosaccharides reduced in vitro allergenicity of β-lactoglobulin

, , , , &
Pages 379-391 | Received 13 Oct 2011, Accepted 17 Apr 2012, Published online: 18 Jun 2012

References

  • Amit, A.G., Mariuzza, R.A., Phillips, S.E., & Poljak, R.J. (1986). Three-dimensional structure of an antigen antibody complex at 2.8 Å resolution. Science, 233, 747–753.
  • Besler, M., Steinhart, H., & Paschke, A. (2001). Stability of food allergens and allergenicity of processed foods. Journal of Allergy and Clinical Immunology B, 756, 228–238.
  • del Val, G., Yee, B.C., Lozano, R.M., Buchanan, B.B., Ermel, R.W., Lee, Y.M., et al. (1999). Thioredoxin treatment increases digestibility and lowers allergenicity of milk. Journal of Agricultural and Food Chemistry, 103, 690–669.
  • Flower, D.R. (1996). The lipocalin protein family: Structure and function. Biochemical Journal, 318, 1–14.
  • Foegeding, E.A., Kuhn, P.R., & Hardin, C.C. (1992). Specific divalent cation-induced changes during gelation of β-lactoglobulin. Journal of Agricultural and Food Chemistry, 40, 2092–2097.
  • Hambling, S.G., McAlpine, A.S., & Sawyer, L. (1992). β-Lactoglobulin. In P.F. Fox (Ed.), Advanced dairy chemistry (pp. 141–190). London: Elsevier Applied Science.
  • Hattori, M. (2002). Functional improvements in food proteins in multiple aspects by conjugation with saccharides: Case studies of â-lactoglobulin-acidic polysaccharides conjugates. Food Science and Technology Research, 8, 291–299.
  • Hattori, M., Miyakawa, S., Ohama, Y., Kawamura, H., Takashi, Y., Kenji, T., et al. (2004). Reduced Immunogenicity of β-Lactoglobulin by Conjugation with Acidic Oligosaccharides. Journal of Agricultural and Food Chemistry, 52, 4546–4553.
  • Hattori, M., Nagasawa, K., Ametani, A., Kaminogawa, S., & Takahashi, K. (1994). Functional changes in β-Lactoglobulin by conjugation with carboxymethyl dextran. Journal of Agricultural and Food Chemistry, 42, 2120–2125.
  • Hattori, M., Nagasawa, K., Ohgata, K., Sone, N., Fukuda, A., Matsuda, H., et al. (2000a). Reduced immunogenicity of β-Lactoglobulin by conjugation with carboxymethyl dextran. Bioconjugate Chemistry, 11, 84–93.
  • Hattori, M., Numamoto, K., Kobayashi, K., & Takahashi, K. (2000b). Functional changes in β-Lactoglobulin by conjugation with cationic saccharides. Journal of Agricultural and Food Chemistry, 48, 2050–2056.
  • Hattori, M., Ogino, A., Nakai, H., & Takahashi, K. (1997). Functional improvement of β-Lactoglobulin by conjugating with alginate lyase-lysate. Journal of Agricultural and Food Chemistry, 45, 703–708.
  • Hosking, C.S., Heine, R.G., & Hill, D.J. (2000). The Melbourne milk allergy study-two decades of clinical research. Allergy and Clinical Immunology International, 12, 198–205.
  • Ishizaka, K., Okudaira, H., & King, T. (1975). Immunogenic properties of modified antigen E. II. Ability of urea-denatured antigen and a polypeptide chain to prime T cells specific for antigen. Journal of Immunology, 114, 110–115.
  • Jarvinen, K.M., Chatchatee, P., Bardina, L., Beyer, K., & Sampson, H.A. (2010). IgE and IgG binding epitopes on alpha-lactalbumin and beta-lactoglobulin in cow's milk allergy. International Archives of Allergy and Immunology, 126, 111–118.
  • Kinsella, J.E. (1988). Foaming and emulsifying properties of glycosylated â-lactoglobulin. Food Hydrocolloids, 2, 439–449.
  • Kurisaki, J., Nakamura, S., Kaminogawa, S., & Yamauchi, K. (1982). The antigenic properties of β-lactoglobulin examined with mouse IgE antibody. Agricultural and biological chemistry, 46, 2069–2075.
  • Lakowicz, J.R. (1999). Principles of fluorescence spectroscopy (2nd ed). New York: Kluwer Academic/Plenum.
  • Lakowicz, J.R., & Weber, G. (1973). Quenching of protein fluorescence by oxygen. Detection of structural fluctuations in proteins on the nanosecond time scale. Biochemistry, 12, 4171–4179.
  • Mills, E.N.C., Valovirta, E., Madsen, C., Taylor, S.L., Vieths, S., Anklam, E., et al. (2004). Information provision for allergy consumers-where are we going with food allergen labeling. Allergy, 59, 1262–1268.
  • Pèrez, M.D., & Calvo, M. (1995). Interaction of β-lactoglobulin with retinol and fatty acids and its role as a possible biological function for this protein. Journal of Dairy Science, 78, 978–988.
  • Rickard, E.O., David, L.B., Anne, H.B., & Mendel, F. (1990). Effect of Maillard browning reactions of the Kunitz soybean trypsin inhibitor on its interaction with monoclonal antibodies. Journal of Agriculture and Food Chemistry, 38, 258–261.
  • Sawyer, L. (2003). β-lactoglobulin. In P. Fox & P. McSweeney (Eds.), Advanced dairy chemistry (pp. 319–386). New York: Kluwer Academic/Plenum.
  • Sehon, A.H. (1982). Suppression of IgE antibody responses with tolerogenic conjugates of allergens and haptens. Progress in Allergy, 32, 161–202.
  • Selo, I., Clement, G., Bernard, H., Chatel, J., Creminon, C., Peltre, G., et al. (1999). Allergy to bovine beta-lactoglobulin: Specificity of Human IgE to tryptic peptides. Clinical and Experimental Allergy, 29, 1055–1063.
  • Shimizu, M., Saito, M., & Yamauchi, K. (1985). Emulsifying and structural properties of βlactoglobulin at different pHs. Agricultural and biological chemistry, 49, 189–194.
  • Spies, J. (1973). Milk allergy. Milk Food Technology, 36, 225–231.
  • Venyaminov, S.Y., & Vesilenko, K.S. (1994). Determination of protein tertiary structure class from circular dichroism spectra. Analytical Biochemistry, 222, 176–184.
  • Watanabe, M., Suzuki, T., Ikezawa, Z., & Arai, S. (1994). Controlled enzymatic treatment of wheat proteins for production of hypoallergenic flour. Bioscience Biotechnology and Biochemistry, 58, 388–390.
  • Whitmore, L., & Wallace, B.A. (2004). DICHROWEB: An online server for protein secondary structure analyses from circular dichroism spectroscopic data. Nucleic Acids Research, 32, 668–673.
  • Xu, Q., Chao, Y.L., & Wan, Q.B. (2009). Health benefit application of functional oligosaccharides. Carbohydrate Polymers, 77, 435–441.

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.