Improvement of digestibility, reduction in allergenicity, and induction of oral tolerance of wheat gliadin by deamidation

Bioscience, Biotechnology and Biochemistry

Volumn 71, Issue 4, 2007, Pages 977-985

  Kumagai, Hitomi ^a   Suda, Akihiro ^a   Sakurai, Hidetoshi ^a   Kumagai, Hitoshi ^b   Arai, Soichi ^c   Inomata, Naoko ^d   Ikezawa, Zenro ^d  

^a NIHON UNIVERSITY   (Japan)

^b KYORITSU WOMEN'S UNIVERSITY   (Japan)

^c TOKYO UNIVERSITY OF AGRICULTURE   (Japan)

^d YOKOHAMA CITY UNIVERSITY   (Japan)

Author keywords

Allergenicity; Deamidation; Digestibility; Oral tolerance; Wheat gliadin

Indexed keywords

AMINES; AMINO ACIDS; PROTEINS; RESINS;

ALLERGENICITY; DEAMIDATION; ORAL TOLERANCE; WHEAT GLIADIN;

CROPS;

AMIDE; ENZYME; GLIADIN; IMMUNOGLOBULIN E; IMMUNOGLOBULIN G; PANCREATIN; PEPSIN A; PROTEIN HYDROLYSATE;

ANIMAL; ARTICLE; BAGG ALBINO MOUSE; CHEMISTRY; DIGESTIVE SYSTEM; FOOD ALLERGY; HUMAN; HYDROLYSIS; IMMUNOLOGY; ION EXCHANGE CHROMATOGRAPHY; METABOLISM; MOUSE; PH; RABBIT; SOLUBILITY; WHEAT;

AMIDES; ANIMALS; CHROMATOGRAPHY, ION EXCHANGE; DIGESTIVE SYSTEM; ENZYMES; FOOD HYPERSENSITIVITY; GLIADIN; HUMANS; HYDROGEN-ION CONCENTRATION; HYDROLYSIS; IMMUNOGLOBULIN E; IMMUNOGLOBULIN G; MICE; MICE, INBRED BALB C; PANCREATIN; PEPSIN A; PROTEIN HYDROLYSATES; RABBITS; SOLUBILITY; TRITICUM;

AMINO ACIDS; DIGESTIBILITY; PROTEINS; SYNTHETIC POLYMERS; WHEAT;

RATTUS; TRITICUM AESTIVUM;

EID: 34247518721     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.60645     Document Type: Article

References (35)

1. Kumagai, H., Shizawa, Y., Sakurai, H., and Kumagai, H., Influence of phytate removal and structural modification on the calcium-binding properties of soybean globulins. Biosci. Biotechnol. Biochem., 62, 341-346 (1998).
2. Kumagai, H., Ishida, S., Koizumi, A., Sakurai, H., and Kumagai, H., Preparation of phytate-removed, deamidated soybean globulins by ion exchangers and characterization of their calcium-binding ability. J. Agric. Food Sci., 50, 172-176 (2002).
3. Kumagai, H., Koizumi, A., Suda, A., Sato, N., Sakurai, H., and Kumagai, H., Enhanced calcium absorption in the small intestine by a phytate-removed deamidated soybean globulin preparation. Biosci. Biotechnol. Biochem., 68, 1598-1600 (2004).
4. Kumagai, H., Koizumi, A., Sato, N., Ishikawa, Y., Suda, A., Sakurai, H., and Kumagai, H., Effect of phytate removal and deamidation of soybean proteins on calcium absorption in in situ rats. BioFactors, 22, 21-24 (2004).
5. Kumagai, H., Norimatsu, Y., Hashizume, N., Sakurai, H., and Kumagai, H., Deamidation of wheat-flour gliadin with ion-exchange resin. Nippon Shokuhin Kagaku Kogaku Kaishi (in Japanese), 48, 884-890 (2001).
6. Norimatsu, Y., Kumagai, H., Nagai, R., Sakurai, H., and Kumagai, H., Deamidation of wheat-flour gluten with ion-exchange resin and its functional properties. Nippon Shokuhin Kagaku Kogaku Kaishi (in Japanese), 49, 639-645 (2002).
7. Palosuo, K., Update on wheat hypersensitivity. Curr. Opin. Allergy Clin. Immunol., 3, 205-209 (2003).
8. Jarvinen, K. M., Turpeinen, M., and Suomalainen, H., Concurrent cereal allergy in children with cow's milk allergy manifested with atopic dermatitis. Clin. Exp. Allergy, 33, 1060-1066 (2003).
9. Lehto, M., Palosuo, K., Varjonen, E., Majuri, M. L., Andersson, U., Reunala, T., and Alenius, H., Humoral and cellular responses to gliadin in wheat-dependent, exercise-induced anaphylaxis. Clin. Exp. Allergy, 33, 90-95 (2003).
10. Matsuo, H., Morita, E., Tatham, A. S., Morimoto, K., Horikawa, T., Osuna, H., Ikezawa, Z., Kaneko, S., Kohno, K., and Dekio, S., Identification of the IgE-binding epitope in ω-5 gliadin, a major allergen in wheat-dependent exercise-induced anaphylaxis. J. Biol. Chem., 279, 12135-12140 (2004).
11. Yokota, S., Tsubaki, K., Shimizu, H., Matsuyama, S., Takahashi, K., and Ikezawa, Z., Study of immune-responsiveness to wheat antigen by IgG, IgA, and IgE immunoblotting with sera from patients with atopic dermatitis. Acta Dermatol. Venereol. Suppl. (Stockh), 176, 45-48 (1992).
12. Varjonen, E., Vainio, E., and Kalimo, K., Antigliadin IgE-indicator of wheat allergy in atopic dermatitis. Allergy, 55, 386-391 (2000).
13. Takizawa, T., Arakawa, H., Tokuyama, K., and Morikawa, A., Identification of allergen fractions of wheat flour responsible for anaphylactic reactions to wheat products in infants and young children. Int. Arch. Allergy Immunol., 125, 51-56 (2001).
14. Simonato, B., De Lazzari, F., Pasini, G., Polato, F., Giannattasio, M., Gemignani, C., Peruffo, A. D. B., Santucci, B., Plebani, M., and Curioni, A., IgE binding to soluble and insoluble wheat flour proteins in atopic and non-atopic patients suffering from gastrointestinal symptoms after wheat ingestion. Clin. Exp. Allergy, 31, 1771-1778 (2001).
15. Battais, F., Pineau, F., Popineau, Y., Aparicio, C., Kanny, G., Guerin, L., Moneret-Vautrin, D. A., and Denery-Papini, S., Food allergy to wheat: identification of immunoglobulin E- and immunoglobulin G-binding proteins with sequential extracts and purified proteins from wheat flour. Clin. Exp. Allergy, 33, 962-970 (2003).
16. Watanabe, M., Tanabe, S., Suzuki, T., Ikezawa, Z., and Arai, S., Primary structure of an allergenic peptide occurring in the chymotryptic hydrolysate of gluten. Biosci. Biotechnol. Biochem., 59, 1596-1597 (1995).
17. Tanabe, S., Arai, S., Yanagihara, Y., Mita, H., Takahashi, K., and Watanabe, M., A major wheat allergen has a Gln-Gln-Gln-Pro-Pro motif identified as an IgE-binding epitope. Biochem. Biophys. Res. Commun., 219, 290-293 (1996).
18. Matsuo, H., Morita, E., Tatham, A. S., Morimoto, K., Horikawa, T., Osuna, H., Ikezawa, Z., Kaneko, S., Kohno, K., and Dekio, S., Identification of the IgE-binding epitope in ω-5 gliadin, a major allergen in wheat-dependent exercise-induced anaphylaxis. J. Biol. Chem., 279, 12135-12140 (2004).
19. Wagner, J. R., and Guéguen, J., Effects of dissociation, deamidation, and reducing treatment on structural and surface active properties of soy glycinine. J. Agric. Food Chem., 42, 1993-2000 (1995).
20. Matsudomi, N., Sasaki, T., Kato, A., and Kobayashi, K., Conformational changes and functional properties of acid-modified soy protein. Agric. Biol. Chem., 49, 1251-1256 (1985).
21. Ma, C. Y., and Khanzada, G., Functional properties of deamidated oat protein isolates. J. Food Sci., 52, 1583-1587 (1987).
22. Chan, W. M., and Ma, C. Y., Acid modification of proteins from soymilk residue (okara). Food Res. Int., 32, 119-127 (1999).
23. Goulet, G., Amiot, J., Simard, C., Delisle, J., and Brisson, G. J., Effect of mild autoclaving and deamidisation on the nutritive value of protein fractions. J. Sci. Food Agric., 36, 305-310 (1985).
24. Lakkis, J., and Villota, R., Comparative performance of chemically and enzymically modified whey proteins. Food Chem., 43, 93-105 (1992).
25. Kato, A., Tanaka, A., Matsudomi, N., and Kobayashi, K., Deamidation of food proteins by protease in alkaline pH. J. Agric. Food Chem., 35, 224-227 (1987).
26. Hamada, J. S., and Marshall, W. E., Enhancement of peptidoglutaminase deamidation of soy protein by heat treatment and/or proteolysis. J. Food Sci., 53, 1132-1134, 1149 (1988).
27. Yong, Y. H., Yamaguchi, S., Gu, Y. S., Mori, T., and Matsumura, Y., Effects of enzymatic deamidation by protein-glutaminase on structure and functional properties of α-zein. J. Agric. Food Chem., 52, 7094-7100 (2004).
28. Shih, F. F., Deamidation of protein in a soy extract by ion-exchange resin catalysis. J. Food Sci., 52, 1529-1531 (1987).
29. Conway, E. J., and Byrne, A., An absorption apparatus for the micro-determination of certain volatile substances. I. The micro-determination of ammonia. Biochem. J., 27, 419-429 (1933).
30. Akamatsu, S., Some micromethods for enzyme studies. J. Biochem., 39, 203-210 (1952).
31. Kotts, C., and Jenness, R., Rennin and pepsin in stomachs of rats (Rattus norvegicus). J. Dairy Sci., 59, 1398-1400 (1976).
32. Kageyama, T., New World monkey pepsinogens A and C, and prochymosins. Purification, characterization of enzymatic properties, cDNA cloning, and molecular evolution. J. Biochem., 127, 761-770 (2000).
33. Troncone, R., and Ferguson, A., Gliadin presented via the gut induces oral tolerance in mice. Clin. Exp. Immunol., 72, 284-287 (1988).
34. Watanabe, M., Suzuki, T., Ikezawa, Z., and Arai, S., Controlled enzymatic treatment of wheat proteins for production of hypoallergenic flour. Biosci. Biotechnol. Biochem., 58, 388-390 (1994).
35. Watanabe, J., Tanabe, S., Watanabe, M., Kasai, T., Sonoyama, K., Suzuki, T., Ikezawa, Z., and Arai, S., Consumption of hypoallergenic flour prevents gluten-induced airway inflammation in Brown Norway rats. Biosci. Biotechnol. Biochem., 65, 1729-1735 (2001).