Reduced immunogenicity of β-lactoglobulin by conjugating with chitosan

Bioscience, Biotechnology and Biochemistry

Volumn 70, Issue 10, 2006, Pages 2349-2356

  Aoki, Tomomi ^a   Iskandar, Silvia ^a   Yoshida, Tadashi ^a   Takahashi, Koji ^a   Hattori, Makoto ^a  

^a TOKYO UNIVERSITY OF AGRICULTURE AND TECHNOLOGY   (Japan)

Author keywords

lactoglobulin; Chitosan; Functional improvement; Protein conjugation; Reduced immunogenicity

Indexed keywords

ANTIBODIES; CHROMATOGRAPHIC ANALYSIS; FLUORESCENCE; HYDROPHOBICITY; SOLUBILITY; WATER;

Β-LACTOGLOBULIN; CHITOSAN; FUNCTIONAL IMPROVEMENT; PROTEIN CONJUGATION; REDUCED IMMUNOGENICITY;

IMMUNOLOGY;

CHITOSAN; CROSS LINKING REAGENT; CYANAMIDE; EPITOPE; LACTOGLOBULIN; RETINOL;

ANIMAL; ARTICLE; C3H MOUSE; CATTLE; CHEMICAL STRUCTURE; CHEMISTRY; ENZYME LINKED IMMUNOSORBENT ASSAY; IMMUNOLOGY; METABOLISM; MOUSE;

ANIMALS; CARBODIIMIDES; CATTLE; CHITOSAN; CROSS-LINKING REAGENTS; ENZYME-LINKED IMMUNOSORBENT ASSAY; EPITOPES, B-LYMPHOCYTE; LACTOGLOBULINS; MICE; MICE, INBRED C3H; MOLECULAR STRUCTURE; VITAMIN A;

BOS TAURUS;

EID: 33750463405     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.50398     Document Type: Article

References (34)

1. McKenzie, H. A., β-Lactoglobulins. Chemistry and molecular biology. In "Milk Proteins," ed. McKenzie, H. A., Academic Press, New York, pp. 257-330 (1971).
2. Mulvihill, D. M., and Kinsella, J. E., Gelation characteristics of whey proteins and β-lactoglobulin. Food Technol., 41, 102-111 (1987).
3. Waniska, R. D., and Kinsella, J. E., Foaming and emulsifying properties of glycosylated β-lactoglobulin. Food Hydrocolloids, 2, 439-449 (1988).
4. Shimizu, M., Saito, M., and Yamauchi, K., Emulsifying and structural properties of β-lactoglobulin at different pHs. Agric. Biol. Chem., 49, 189-194 (1985).
5. Spies, J., Milk allergy. J. Milk Food Technol., 36, 225-231 (1973).
6. Hattori, M., Functional improvements in food proteins in multiple aspects by conjugation with saccharides: case studies of β-lactoglobulin-acidic polysaccharides conjugates. Food Sci. Technol. Res., 8, 291-299 (2002).
7. Hattori, M., Nagasawa, K., Ametani, A., Kaminogawa, S., and Takahashi, K., Functional changes in β-lactoglobulin by conjugation with carboxymethyl dextran. J. Agric. Food Chem., 42, 2120-2125 (1994).
8. Nagasawa, K., Takahashi, K., and Hattori, M., Improved emulsifying properties of β-lactoglobulin by conjugating with carboxymethyl dextran. Food Hydrocolloids, 10, 63-67 (1996).
9. Nagasawa, K., Ohgata, K., Takahashi, K., and Hattori, M., Role of the polysaccharide content and net charge on the emulsifying properties of β-lactoglobulin-carboxymethyl dextran conjugates. J. Agric. Food Chem., 44, 2538-2543 (1996).
10. Hattori, M., Nagasawa, K., Ohgata, K., Sone, N., Fukuda, A., Matsuda, H., and Takahashi, K., Reduced immunogenicity of β-lactoglobulin by conjugation with carboxymethyl dextran. Bioconjugate Chem., 11, 84-93 (2000).
11. Kobayashi, K., Hirano, A., Ohta, A., Yoshida, T., Takahashi, K., and Hattori, M., Reduced immunogenicity of β-lactoglobulin by conjugation with carboxymethyl dextrans differing in molecular weight. J. Agric. Food Chem., 49, 823-831 (2001).
12. Kobayashi, K., Yoshida, T., Takahashi, K., and Hattori, M., Modulation of T cell response to β-lactoglobulin by conjugation with carboxymethyl dextran. Bioconjugate Chem., 14, 168-176 (2003).
13. Hattori, M., Aiba, Y., Nagasawa, K., and Takahashi, K., Functional improvements in alginic acid by conjugating with β-lactoglobulin. J. Food Sci., 61, 1171-1176 (1996).
14. Hattori, M., Ogino, A., Nakai, H., and Takahashi, K., Functional improvement of β-lactoglobulin by conjugating with alginate lyase-lysate. J. Agric. Food Chem., 45, 703-708 (1997).
15. Hattori, M., Numamoto, K.-I., Kobayashi, K., and Takahashi, K., Functional changes in β-lactoglobulin by conjugation with cationic saccharides. J. Agric. Food Chem., 48, 2050-2056 (2000).
16. Hattori, M., Okada, Y., and Takahashi, K., Functional changes in β-lactoglobulin upon conjugation with carboxymethyl cyclodextrin. J. Agric. Food Chem., 48, 3789-3794 (2000).
17. Winterowd, J. G., and Sandford, P. A., Chitin and chitosan. In "Food Polysaccharides and Their Applications," ed. Stephan, A. M., Marcel Dekker, Inc., New York, pp. 441-462 (1995).
18. Armstrong, J. M., McKenzie, H. A., and Sawyer, W. H., On the fractionation of β-lactoglobulin and α-lactalbumin. Biochim. Biophys. Acta, 147, 60-72 (1967).
19. Davis, B. J., DISC ELECTROPHORESIS-II: method and application to human serum proteins. Ann. NY Acad. Sci., 121, 404-427 (1964).
20. Kaminogawa, S., Shimizu, M., Ametani, A., Hattori, M., Ando, O., Hachimura, S., Nakamura, Y., Totsuka, M., and Yamauchi, K., Monoclonal antibodies as probes for monitoring the denaturation process of bovine β-lactoglobulin. Biochim. Biophys. Acta, 998, 50-56 (1989).
21. Weber, K., and Osborn, M., The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J. Biol. Chem., 244, 4406-4412 (1969).
22. Dische, Z., and Borenfreund, E., A spectrophotometric method for the microdetermination of hexosamines. J. Biol. Chem., 184, 517-522 (1950).
23. Futterman, S., and Heller, J., The enhancement of fluorescence and decreased susceptibility to enzyme oxidation of retinol complexed with bovine serum albumin, β-lactoglobulin, and the retinol-binding protein of human plasma. J. Biol. Chem., 247, 5168-5172 (1972).
24. Cogan, U., Kopelman, M., Mokady, S., and Shintzky, M., Binding affinities of retinol and related compounds to retinol binding proteins. Eur. J. Biochem., 65, 71-78 (1976).
25. Hattori, M., Ametani, A., Katakura, Y., Shimizu, M., and Kaminogawa, S., Unfolding/refolding studies on bovine β-lactoglobulin with monoclonal antibodies as probes: does a renatured protein completely refold? J. Biol. Chem., 268, 22414-22419 (1993).
26. Hattori, M., Miyakawa, S., Ohama, Y., Kawamura, H., Yoshida, T., To-o, K., Kuriki, T., and Takahashi, K., Reduced immunogenicity of β-lactoglobulin by conjugating with acidic oligosaccharides. J. Agric. Food Chem., 52, 4546-4553 (2004).
27. Kaminogawa, S., Hattori, M., Ando, O., Kurisaki, J., and Yamauchi, K., Preparation of monoclonal antibody against bovine β-lactoglobulin and its unique affinity. Agric. Biol. Chem., 51, 797-802 (1987).
28. Hogg, P. J., Johnson, S. C., Bowles, M. R., Pond, S. M., and Winzor, D. J., Evaluation of equilibrium constants for antigen-antibody interaction by solid-phase immunoassay: the binding of paraquant to its elicited mouse monoclonal antibody. Mol. Immunol., 24, 797-801 (1987).
29. Ball, G., Shelton, M. J., Walth, B. J., Hill, D. J., Hosking, C. S., and Howden, M. E. H., A major continuous allergenic epitope of bovine β-lactoglobulin recognized by human IgE binding. Clin. Exp. Allergy, 24, 758-764 (1994).
30. Kohri, E., Maurice, L., Bourgeois, C., Bour, J. B., and Pothier, P., Epitope mapping of the major inner capsid protein of group A rotavirus using peptide synthesis. Virology, 194, 110-116 (1993).
31. Gammon, G., Geysen, H. M., Apple, R. J., Pickett, E., Palmer, M., Ametani, A., and Sercarz, E. E., T cell determinant structure: cores and determinant envelopes in three mouse major histocompatibility complex haplotypes. J. Exp. Med., 173, 609-617 (1991).
32. Takata, M., Maiti, P. K., Kubo, R. T., Chen, Y. H., Holford, S. V., Rector, E. S., and Sehon, A. H., Cloned suppressor T cells derived from mice tolerized with conjugates of antigen and monomethoxypolyethylene glycol. Relationship between monoclonal T suppressor factor and the T cell receptor. J. Immunol., 145, 2846-2853 (1990).
33. Ito, H. O., So, T., Hirata, M., Koga, T., Ueda, T., and Imoto, T., Tolerogenic activity of polyethylene glycolconjugated lysozyme distinct from that of the native counterpart. Immunology, 93, 200-207 (1998).
34. So, T., Ito, H. O., Koga, T., Watanabe, S., Ueda, T., and Imoto, T., Depression of T-cell epitope generation by stabilizing hen lysozyme. J. Biol. Chem., 272, 32136-32140 (1997).