Reduced allergenicity of β-lactoglobulin in vitro by tea catechins binding

References

• Batra, A., & Saxena, R.K. (2005). Potential tannase producers from the genera Aspergillus and Penicillium. Process Biochemistry, 40, 1553–1557.
   Web of Science ®Google Scholar
• 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.
   Google Scholar
• 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 Allergy and Clinical Immunology, 103, 690–669.
   PubMed Web of Science ®Google Scholar
• Flower, D.R. (1996). The lipocalin protein family: Structure and function. Biochemical Journal, 318, 1–14.
   PubMed Web of Science ®Google Scholar
• Foegeding, E.A., Kuhn, P.R., & Hardin, C.C. (1992). Specific divalent cation-induced changes during gelation of β-lactoglobulin. Journal of Agriculture and Food Chemistry, 40, 2092–2097.
   Web of Science ®Google Scholar
• Fox, P.F. (2001). Milk proteins as food ingredients. International Journal of Dairy Technology, 54, 41–55.
   Web of Science ®Google Scholar
• Fugate, R., & Song, P. (1980). Spectroscopic characterization of β-lactoglobulin retinol complex. Biochimica and Biophysica Acta, 625, 28–42.
   PubMed Web of Science ®Google Scholar
• Hattori, M., Ogino, A., Nakai, H., & Takahashi, K. (1997). Functional improvement of β-lactoglobulin by conjugating with alginate lyase-lysate. Journal of Agriculture and Food Chemistry, 45, 703–708.
   Web of Science ®Google Scholar
• Hattori, M., Nagasawa, K., Ametani, A., Kaminogawa, S., & Takahashi, K. (1994). Functional changes in β-lactoglobulin by conjugation with carboxymethyl dextran. Journal of Agriculture and Food Chemistry, 42, 2120–2125.
   Web of Science ®Google Scholar
• 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 Chemisty, 11, 84–93.
   PubMed Web of Science ®Google Scholar
• Hattori, M., Numamoto, K., Kobayashi, K., & Takahashi, K. (2000b). Functional changes in β-lactoglobulin by conjugation with cationic saccharides. Journal of Agriculture and Food Chemistry, 48, 2050–2056.
   PubMed Web of Science ®Google Scholar
• 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 Immunology, 114, 110–115.
   PubMed Web of Science ®Google Scholar
• 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.
   Google Scholar
• Jaziri, I., Slama, M.B., Mhadhbi, H., Urdaci, M.C., & Hamdi, M. (2009). Effect of green and black teas (Camellia sinensis L.) on the characteristic microflora of yogurt during fermentation and refrigerated storage. Food Chemistry, 112, 614–620.
   Web of Science ®Google Scholar
• Kanakis, C.D., Hasni, I., Bourassa, P., Tarantilis, P.A., Polissiou, M.G., & Tajmir-Riahi, H.A. (2011). Milkβ-lactoglobulin complexes with tea polyphenols. Food Chemistry, 127, 1046–1055.
   PubMed Web of Science ®Google Scholar
• Kurisaki, J., Nakamura, S., Kaminogawa, S., & Yamauchi, K. (1982). The antigenic properties of β-lactoglobulin examined with mouse IgE antibody. Agricultural Biology and Chemistry, 46, 2069–2075.
   Web of Science ®Google Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• Monaci, L., Tregodt, V., Hengel, A.J.V., & Anklam, E. (2006). Milk allergens, their characteristics and their detection in food: A review. European Food Research and Technology, 223, 149–179.
   Web of Science ®Google Scholar
• O'Connell, J.E., & Fox, P.F. (1999). Effect of extracts of oak (Quercus petraea) bark, oak leaves, aloe vera (Curacao aloe), coconut shell and wine on the colloidal stability of milk and concentrated milk. Food Chemistry, 66, 93–96.
   Web of Science ®Google Scholar
• Pèrez, M.D., & Calvo, M. (1995). Interaction of â-lactoglobulin with retinol and fatty acids and its role as a possible biological function for this protein. Journal of Dairy Science, 78, 978–988.
   PubMed Web of Science ®Google Scholar
• Prigent, S.V.E., Gruppen, H., Visser, A.J.W.G., Van Koningsveld, G.A., De Jong, G.A.H., & Voragen, A.G.J. (2003). Effect of non-covalent interactions with 5-ocoffeoylquinic acid (chlorogenic acid) on the heat denaturation and solubility of globular proteins. Journal of Agriculture and Food Chemistry, 51, 5088–5095.
   PubMed Web of Science ®Google Scholar
• Selo, I., Clement, G., Bernard, H., Chatel, J.M., Creminon, C., Peltre, G., & Wal, J.M. (1999). Allergy to bovine beta-lactoglobulin: specificity of Human IgE to tryptic peptides. Clinical and Experimental Allergy, 78, 1055–1063.
   Google Scholar
• Shimizu, M., Saito, M., & Yamauchi, K. (1985). Emulsifying and structural properties of β-lactoglobulin at different pHs. Agricultural Biology and Chemistry, 49, 189–194.
   Web of Science ®Google Scholar
• Spies, J. (1973). Milk allergy. Milk Food Technology, 36, 225–231.
   Web of Science ®Google Scholar
• Svetli, D., Guy, S., & Heidar-Ali, T. (2010). Dual effect of milk on the antioxidant capacity of green, Darjeeling, and English breakfast teas. Food Chemistry, 122, 539–545.
   Web of Science ®Google Scholar
• Venyaminov, S.Y., & Vesilenko, K.S. (1994). Determination of protein tertiary structure class from circular dichroism spectra. Analytical Biochemistry, 222, 176–184.
   PubMed Web of Science ®Google Scholar
• Watanabe, M., Suzuki, T., Ikezawa, Z., & Arai, S. (1994). Controlled enzymatic treatment of wheat proteins for production of hypoallergenic flour. Bioscience Biotechnology & Biochemistry, 58, 388–390.
   PubMed Web of Science ®Google Scholar
• Zerrin, Y., Elif, A., & Yasar, K.E. (2010). Characterization of binding interactions between green tea flavanoids and milk proteins. Food Chemistry, 121, 450–456.
   Web of Science ®Google Scholar