Functional improvements to β-lactoglobulin by preparing an edible conjugate with cationic saccharide using microbial mransglutaminase (MTGase)

Bioscience, Biotechnology and Biochemistry

Volumn 72, Issue 5, 2008, Pages 1227-1234

  Ikeuchi, Tomomi ^a   Aoki, Tomomi ^a   Yoshida, Tadashi ^a   Takahashi, Koji ^a   Hattori, Makoto ^a  

^a TOKYO UNIVERSITY OF AGRICULTURE AND TECHNOLOGY   (Japan)

Author keywords

lactoglobulin; Functional improvement; Neoglycoconjugate; Protein conjugation; Transglutaminase

Indexed keywords

ANTIBODIES; BIOCATALYSTS; CHEMICAL REACTIONS; DIFFUSERS (OPTICAL); EMULSIFICATION; FOOD PRODUCTS; GLUCOSE; LUMINESCENCE; MICROFLUIDICS; MONOCLONAL ANTIBODIES; PH; PH EFFECTS; SCAFFOLDS; SUGARS;

(MIN ,MAX ,+) FUNCTIONS; (R ,S)-CONJUGATE; ACIDIC PH; ANTIGENICITY; BALB/C MICE; BINDING ACTIVITIES; EMULSIFYING PROPERTIES; IMMUNOGENICITY; LACTOGLOBULIN; MAILLARD REACTIONS; MICROBIAL TRANSGLUTAMINASE (MTGASES); MOLAR RATIOS; NATIVE STRUCTURES; POLY-LYSINE (PL); RETINOL (VITAMIN A); SDS-PAGE;

LIGHT EMISSION;

DEXTRAN; DRUG DERIVATIVE; EMULSIFYING AGENT; LACTOGLOBULIN; POLYLYSINE; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE;

ANIMAL; ARTICLE; CATTLE; CHEMISTRY; ENZYME LINKED IMMUNOSORBENT ASSAY; FEMALE; FOOD; IMMUNOLOGY; ISOLATION AND PURIFICATION; METABOLISM; MOUSE;

ANIMALS; CATTLE; DEXTRANS; EMULSIFYING AGENTS; ENZYME-LINKED IMMUNOSORBENT ASSAY; FEMALE; FOOD; LACTOGLOBULINS; MICE; POLYLYSINE; TRANSGLUTAMINASES;

BOVINAE; MUS;

EID: 45749144262     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.70702     Document Type: Article

References (26)

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. Shimizu, M., Saito, M., and Yamauchi, K., Emulsifying and structural properties of β-lactoglobulin at different pHs. Agric. Biol. Chem., 49, 189-194 (1985).
3. Mulvihill, D. M., and Kinsella, J. E., Gelation characteristics of whey proteins and β-lactoglobulin. Food Technol., 41(9), 102-111 (1987).
4. Waniska, R. D., and Kinsella, J. E., Foaming and emulsifying properties of glycosylated β-lactoglobulin. Food Hydrocolloids, 2, 439-449 (1988).
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. Bioconjug. 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. Bioconjug. 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., 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 -lactoglobulin upon conjugation with carboxymethyl cyclodextrin. J. Agric. Food Chem., 48, 3789-3794 (2000).
17. Folk, J. E., and Chung, S. I., Transglutaminases. Methods Enzymol., 113, 358-375 (1985).
18. Armstrong, J. M., McKenzie, H. A., and Sawyer, W. H., On the fractionation of beta-lactoglobulin and alpha-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. Dubois, M., Gilles, K. A., Hamilton, J. K., Rebers, P. A., and Smith, F., Colorimetric method for determination of sugars and related substances. Anal. Chem., 28, 350-356 (1956).
21. Habeeb, A. F., Determination of free amino groups in proteins by trinitrobenzenesulfonic acid. Anal. Chem., 14, 328-336 (1966).
22. Laemmli, U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685 (1970).
23. Pearce, K. N., and Kinsella, J. E., Emulsifying properties of proteins: evaluation of a turbidimetric technique. J. Agric. Food Chem., 26, 716-723 (1978).
24. Aoki, T., Iskandar, S., Yoshida, T., Takahashi, K., and Hattori, M., Reduced immunogenicity of β-lactoglobulin by conjugation with chitosan. Biosci. Biotechnol. Biochem., 70, 2349-2356 (2006).
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. 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).