Degradation of soluble proteins including some allergens in brown rice grains by endogenous proteolytic activity during germination and heat-processing

Bioscience, Biotechnology and Biochemistry

Volumn 69, Issue 10, 2005, Pages 1877-1883

  Yamada, Chikako ^a   Izumi, Hidehiko ^a   Hirano, Junko ^a   Mizukuchi, Aya ^b   Kise, Mitsuo ^b   Matsuda, Tsukasa ^c   Kato, Yasuko ^d  

^a NAGOYA UNIVERSITY OF ARTS AND SCIENCES   (Japan)

^b Central Research Development Laboratory Fancl Corporation   (Japan)

^c NAGOYA UNIVERSITY   (Japan)

^d KAWASAKI UNIVERSITY OF MEDICAL WELFARE   (Japan)

Author keywords

amylase trypsin inhibitor; Allergen; Food allergy; Germination; Rice

Indexed keywords

AMINO ACIDS; CROPS; DEGRADATION; ENZYME INHIBITION;

Α-AMYLASE/TRYPSIN INHIBITOR; ALLERGEN; FOOD ALLERGY; HEAT PROCESSING;

ENZYMES;

ALLERGEN; CYSTEINE PROTEINASE; DETERGENT; PEPTIDE HYDROLASE; VEGETABLE PROTEIN;

ARTICLE; CHEMISTRY; ENZYMOLOGY; FOOD ALLERGY; FOOD HANDLING; GERMINATION; HEAT; METABOLISM; PH; PLANT SEED; RICE; SOLUBILITY;

ALLERGENS; CYSTEINE ENDOPEPTIDASES; DETERGENTS; FOOD HANDLING; FOOD HYPERSENSITIVITY; GERMINATION; HEAT; HYDROGEN-ION CONCENTRATION; ORYZA SATIVA; PEPTIDE HYDROLASES; PLANT PROTEINS; SEEDS; SOLUBILITY;

CYSTEINE; DEGRADATION; ENZYMES; GERMINATION; INHIBITION; RICE;

EID: 27644569149     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.69.1877     Document Type: Article

References (28)

1. Block, B. A., Krilis, S., and Wrigley, C. W., Hypersensitive to inhaled flour allergens. Comparison between cereals. Allergy, 35, 45-56 (1980).
2. Ikezawa, Z., Miyakawa, K., Komatsu, H., Suga, C., Miyakawa, A., Sugiyama, A., Sasaki, T., Nakajima, H., Hirai, Y., and Suzuki, Y., A probable involvement of rice allergy in severe type of atopic dermatitis in Japan. Acta Derm. Venereol. Suppl., 176, 103-107 (1992).
3. Miyakawa, K., Hirai, Y., Miyakawa, J., Sugiyama, T., Komatsu, T., Suga, S., Ikezawa, Y., and Nakajima, H., Statistical analyses of the diagnostic criteria, clinical severity, IgE-RAST score, and serum IgE value in patients with atopic dermatitis (AD)-probable involvement of food antigens, especially rice, in severe cases. Jap. J. Allergol., 37, 1101-1110 (1988).
4. Lezaun, A., Igea, J. M., Quirce, S., Cuevas, M., Parra, F., Alonso, M. D., Martin, J. A., and Cano, M. S., Asthma and contact urticaria caused by rice in a house wife. Allergy, 49, 92-95 (1994).
5. Limas, G. G., Salinas, M., Moneo, I., Fischer, S., Wittmann-Liebold, B., and Mendez, E., Purification and characterization of ten new rice NaCl-soluble proteins: identification of four protein-synthesis inhibitors and two immunoglobulin-binding proteins. Planta, 181, 1-9 (1990).
6. Shibasaki, M., Suzuki, S., Nemoto, H., and Kuroume, T., Allergenicity and lymphocyte-stimulating property of rice protein. J. Allergy Clin. Immunol., 64, 259-265 (1979).
7. Urisu, A., Yamada, K., Masuda, S., Komada, H., Wada, E., Kondo, Y., Horiba, F., Yazaki, T., Yamada, M., Torii, S., and Nakamua, R., 16-Kilodalton rice protein is one of the major allergens in rice grains extract and responsible for cross-allergenicity between cereal grains in the Poaceae family. Int. Arch. Allergy Appl. Immunol., 96, 244-252 (1991).
8. Nakase, M., Adachi, T., Urisu, A., Miyashita, T., Alvarez, A. M., Nagasaka, S., Aoki, N., Nakamura, R., and Matsuda, T., Rice (Oryza sativa L.) α-amylase inhibitors of 14-16-kDa are potential allergens and products of a multigene family. J. Agric. Food Chem., 44, 2624-2628 (1996).
9. Izumi, H., Sugiyama, M., Matsuda, T., and Nakamura, R., Structural characterization of the 16-kDa allergen, RA17, in rice seeds. Prediction of the secondary structure and identification of intramolecular disulfide bridges. Biosci. Biotechnol. Biochem., 63, 2059-2063 (1999).
10. Usui, Y., Nakase, M., Hotta, H., Urisu, A., Aoki, N., Kitajima, K., and Matsuda, T., A 33-kDa allergen from rice (Oryza sativa L. Japonica). J. Biol. Chem., 276, 11376-11381 (2001).
11. Izumi, H., Adachi, T., Fujii, N., Matsuda, T., Nakamura, R., Tanaka, K., Urisu, A., and Kurosawa, Y., Nucleotide sequence of cDNA clone encoding majior allergenic protein in rice seeds. FEBS Lett., 302, 213-216 (1992).
12. Adachi, T., Izumi, H., Yamada, T., Tanaka, K., Takeuchi, S., Nakamura, R., and Matsuda, T., Gene structure and expression of rice seed allergenic proteins belonging to the α-amylase/trypsin inhibitor family. Plant Mol. Biol., 21, 239-248 (1993).
13. Alvarez, A. M., Adachi, T., Nakase, M., Aoki, N., Nakamura, R., and Matsuda, T., Classification of rice allergenic protein cDNA belonging to the α-amylase/trypsin inhibitor gene family. Biochim. Biophys. Acta, 1251, 201-204 (1995).
14. Nakamura, R., and Matsuda, T., Rice allergenic protein and molecular-genetic approach for hypoallergenic rice. Biosci. Biotechnol. Biochem., 60, 1215-1221 (1996).
15. Garcia-Olmedo, F., Salcedo, G., Sanchez-Monge, R., Hernandez-Lucas, C., Carmona, M. J., Lopez-Fando, J. J., Fernandez, J. A., Gomez, L., Royo, J., Garcia-Maroto, F., Castagnaro, A., and Carbonero, P., Tripsin/α-amylase inhibitors and thionins: possible defence proteins from barley. In "Barley: Genetic, Biochemistry, Molecular Biology and Biotecnology" vol. 5, ed. Shewry, P. R., International-Walling, Oxon, pp. 335-350 (1992).
16. Barber, D., Sanchez-Monge, R., Gomez, L., Carpizo, J., Armentia, A., Lopez-Otin, C., Juan, F., and Salcedo, G., A barley flour inhibitor of insect alpha-amylase is a major allergen associated with baker's asthma disease. FEBS Lett., 248, 119-122 (1989).
17. Gomez, L., Martin, E., Hernandez, D., Sanchez-Monge, R., Barber, D., Pozo, V., Andres, B., Armentia, A., Lopez, C., Salcedo, G., and Palomino, P., Members of the alpha-amylase inhibitors family from wheat endosperm are major allergens associated with baker's asthma. FEBS Lett., 261, 85-89 (1990).
18. Watanabe, M., Miyakawa, J., Ikezawa, Z., Suzuki, Y., Hirao, T., Yoshizawa, T., and Arai, S., Production of hypoallergenic rice by enzymatic decomposition of constituent proteins. J. Food Sci., 55, 781-783 (1990).
19. Watanabe, M., Yoshizawa, T., Miyakawa, J., Ikezawa, Z., Abe, K., Yanagisawa, T., and Arai, S., Quality improvement and evaluation of hypoallergenic rice grains. J. Food Sci., 55, 1105-1107 (1990).
20. Ikezawa, Z., Ikebe, T., Ogura, H., Odajima, H., Kurosaka, F., Komatu, H., Sase, K., Suga, C., Sugiuchi, M., and Suguro, H., Mass trial of hypoallergenic rice (HRS-1) produced by enzymatic digestion in atopic dermatitis with suspected rice allergy. HRS-1 Research Group. Acta Derm. Venereol. Suppl., 176, 108-112 (1992).
21. Saikusa, T., Horino, T., and Mori, Y., Distribution of free amino acids in the rice kernel and kernel fraction and the effect of water soaking on the distribution. J. Agric. Food Chem., 42, 1122-1125 (1994).
22. Kato, H., and Minamikawa, T., Identification and characterization of a rice cystein endopeptidase that digests glutelin. Eur. J. Biochem., 239, 310-316 (1996).
23. Shaw, J., and Beadle, L. C., A simplified ultramicro Kjeldahl method for the estimation of protein and total nitrogen in fluid samples of less than 1-0 mu 1. J. Exp. Biol., 26, 15-23 (1949).
24. Lowry, O. H., Rosebrough, N. J., Farr, A. L., and Randall, R. J., Protein measurement with the folin phenol reagent. J. Biol. Chem., 193, 265-275 (1951).
25. Laemmli, U., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685 (1970).
26. Towbin, H., Staehelin, T., and Gordon, J., Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. U.S.A., 76, 4350-4354 (1979).
27. Matsuda, T., Nomura, R., Sugiyama, M., and Nakamura, R., Immunochemical studies on rice allergenic proteins. Agric. Biol. Chem., 55, 509-513 (1991).
28. Hayashi, M., and Natori, Y., Molecular-size-dependent degradation of liver cytosolic proteins in vitro. J. Biochem., 79, 221-224 (1976).