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Volumn 25, Issue 3, 2014, Pages 301-310

Reduction of the allergenic protein in soybean meal by enzymatic hydrolysis

Author keywords

ELISA; protein subunit; proteolysis; soy allergenic protein; soybean meal

Indexed keywords


EID: 84899449649     PISSN: 09540105     EISSN: 14653443     Source Type: Journal    
DOI: 10.1080/09540105.2013.782268     Document Type: Article
Times cited : (44)

References (27)
  • 1
    • 0033836431 scopus 로고    scopus 로고
    • Structural biology of allergens
    • Aalberse, R. C. (2000). Structural biology of allergens. Journal of Allergy and Clinical Immunology, 106(2), 228-238. doi:10.1067/mai.2000.108434
    • (2000) Journal of Allergy and Clinical Immunology , vol.106 , Issue.2 , pp. 228-238
    • Aalberse, R.C.1
  • 2
    • 58149265301 scopus 로고    scopus 로고
    • Soybean β-conglycinin as the main allergen in a patient with food-dependent exercise-induced anaphylaxis by tofu: Food processing alters pepsin resistance
    • Adachi, A., Horikawa, T., Shimizu, H., Sarayama, Y., Ogawaz, T., Sjolander, S., Moriyama, T. (2009). Soybean β-conglycinin as the main allergen in a patient with food-dependent exercise-induced anaphylaxis by tofu: Food processing alters pepsin resistance. Clinical and Experimental Allergy, 39(1), 167-173. doi:10.1111/j.1365-2222.2008.03148.x
    • (2009) Clinical and Experimental Allergy , vol.39 , Issue.1 , pp. 167-173
    • Adachi, A.1    Horikawa, T.2    Shimizu, H.3    Sarayama, Y.4    Ogawaz, T.5    Sjolander, S.6    Moriyama, T.7
  • 3
    • 82655161850 scopus 로고
    • Enzymic hydrolysis of food proteins
    • Adler-Nissen, J. (1989). Enzymic hydrolysis of food proteins. Journal of Food Engineering, 9(2), 165-166. doi:10.1016/0260-8774(89)90015-0
    • (1989) Journal of Food Engineering , vol.9 , Issue.2 , pp. 165-166
    • Adler-Nissen, J.1
  • 4
    • 80051784149 scopus 로고    scopus 로고
    • Digestibility and immunoreactivity of soybean β-conglycinin and its deglycosylated form
    • Amigo-Benavent, M., Clemente, A., Ferranti, P., Caira, S., & Dolores del Castillo, M. (2011). Digestibility and immunoreactivity of soybean β-conglycinin and its deglycosylated form. Food Chemistry, 129(4), 1598-1605. doi:10.1016/j.foodchem.2011.06.015
    • (2011) Food Chemistry , vol.129 , Issue.4 , pp. 1598-1605
    • Amigo-Benavent, M.1    Clemente, A.2    Ferranti, P.3    Caira, S.4    Dolores del Castillo, M.5
  • 6
    • 0033928258 scopus 로고    scopus 로고
    • Molecular and biochemical classification of plant-derived food allergens
    • Breiteneder, H., & Ebner, C. (2000). Molecular and biochemical classification of plant-derived food allergens. Journal of Allergy and Clinical Immunology, 106(1), 27-36. doi:10.1067/mai.2000.106929
    • (2000) Journal of Allergy and Clinical Immunology , vol.106 , Issue.1 , pp. 27-36
    • Breiteneder, H.1    Ebner, C.2
  • 7
    • 0027052241 scopus 로고
    • Allergenicity of peanut and soybean extracts altered by chemical or thermal denat-uration in patients with atopic dermatitis and positive food challenges
    • Burks, A. W., Williams, L. W., Thresher, W., Connaughton, C., Cockrell, G., & Helm, R. M. (1992). Allergenicity of peanut and soybean extracts altered by chemical or thermal denat-uration in patients with atopic dermatitis and positive food challenges. Journal of Allergy and Clinical Immunology, 90(6), 889-897. doi:10.1016/0091-6749(92)90461-A
    • (1992) Journal of Allergy and Clinical Immunology , vol.90 , Issue.6 , pp. 889-897
    • Burks, A.W.1    Williams, L.W.2    Thresher, W.3    Connaughton, C.4    Cockrell, G.5    Helm, R.M.6
  • 9
    • 2442503904 scopus 로고    scopus 로고
    • Soy protein allergy: Incidence and relative severity
    • Retrieved from
    • Cordle, C. T. (2004). Soy protein allergy: Incidence and relative severity. Journal of Nutrition, 134, 1213S-1219S. Retrieved from http://jn.nutrition.org/content/134/5/1213S.full.pdf+html.
    • (2004) Journal of Nutrition , vol.134
    • Cordle, C.T.1
  • 11
    • 29744466425 scopus 로고
    • Determination of serum proteins by means of the biuret reaction
    • Retrieved from
    • Gornall, B. A. G., Bardawill, C. J., & David, M. M. (1949). Determination of serum proteins by means of the biuret reaction. The Journal of Biological Chemistry, 177, 751-766. Retrieved from http://www.fli-leibniz.de/~rake/PDF/gornall1949.pdf.
    • (1949) The Journal of Biological Chemistry , vol.177 , pp. 751-766
    • Gornall, B.A.G.1    Bardawill, C.J.2    David, M.M.3
  • 12
    • 33847305451 scopus 로고    scopus 로고
    • Allergenicity of soybean: New developments in identification of allergenic proteins, cross-reactivities and hypoallergenization technologies
    • L'Hocine, L., & Boye, J. I. (2007). Allergenicity of soybean: New developments in identification of allergenic proteins, cross-reactivities and hypoallergenization technologies. Critical Reviews in Food Science and Nutrition, 47(2), 127-143. doi:10.1080/10408390600626487
    • (2007) Critical Reviews in Food Science and Nutrition , vol.47 , Issue.2 , pp. 127-143
    • L'Hocine, L.1    Boye, J.I.2
  • 13
    • 34147148690 scopus 로고    scopus 로고
    • Detection and quantification of soy allergens in food: Study of two commercial enzyme-linked immunosorbent assays
    • L'Hocine, L., Boye, J. I., & Munyana, C. (2007). Detection and quantification of soy allergens in food: Study of two commercial enzyme-linked immunosorbent assays. Journal of Food Science, 72(3), C145-C153. doi:10.1111/j.1750-3841.2007.00298.x
    • (2007) Journal of Food Science , vol.72 , Issue.3
    • L'Hocine, L.1    Boye, J.I.2    Munyana, C.3
  • 14
    • 34147155531 scopus 로고    scopus 로고
    • Effect of enzymatic hydrolysis of 7S globulin, a soybean protein, on its allergenicity and identification of its allergenic hydrolyzed fragments using SDS-PAGE
    • Retrieved from
    • Keum, E. H., Lee, S. I., & Oh, S. (2006). Effect of enzymatic hydrolysis of 7S globulin, a soybean protein, on its allergenicity and identification of its allergenic hydrolyzed fragments using SDS-PAGE. Food Science and Biotechnology, 15(1), 128-132. Retrieved from http://agris.fao.org/agris-search/search/display.do?f=2007/KR/KR0702.xml;KR2007000370.
    • (2006) Food Science and Biotechnology , vol.15 , Issue.1 , pp. 128-132
    • Keum, E.H.1    Lee, S.I.2    Oh, S.3
  • 15
    • 61449146289 scopus 로고    scopus 로고
    • All three subunits of soybean β-conglycinin are potential food allergens
    • Krishnan, H. B., Kim, W. S., Jang, S. C., & Kerley, M. S. (2009). All three subunits of soybean β-conglycinin are potential food allergens. Journal of Agricultural and Food Chemistry, 57(3), 938-943. doi:10.1021/jf802451g
    • (2009) Journal of Agricultural and Food Chemistry , vol.57 , Issue.3 , pp. 938-943
    • Krishnan, H.B.1    Kim, W.S.2    Jang, S.C.3    Kerley, M.S.4
  • 16
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227(5259), 680-685. doi:10.1038/227680a0
    • (1970) Nature , vol.227 , Issue.5259 , pp. 680-685
    • Laemmli, U.K.1
  • 17
    • 34147142548 scopus 로고    scopus 로고
    • Allergenicity of proteolytic hydrolysates of the soybean 11S globulin
    • Lee, H. W., Keum, E. H., Lee, S. J., Sung, D. E., Chung, D. H., Lee, S. I., & Oh, S. (2007). Allergenicity of proteolytic hydrolysates of the soybean 11S globulin. Journal of Food Sciences, 72(3), C168-C172. doi:10.1111/j.1750-3841.2007.00307.x
    • (2007) Journal of Food Sciences , vol.72 , Issue.3
    • Lee, H.W.1    Keum, E.H.2    Lee, S.J.3    Sung, D.E.4    Chung, D.H.5    Lee, S.I.6    Oh, S.7
  • 18
    • 0032404009 scopus 로고    scopus 로고
    • The roles of the N-linked glycans and extension regions of soybean β-conglycinin in folding, assembly and structural features
    • Maruyama, N., Katsube, T., Wada, Y., Oh, M. H., Barba de larosa, A. P., Okuda, E., Utsumi, S. (1998). The roles of the N-linked glycans and extension regions of soybean β-conglycinin in folding, assembly and structural features. European Journal of Biochemistry, 258(2), 854-862. doi:10.1046/j.1432-1327.1998.2580854.x
    • (1998) European Journal of Biochemistry , vol.258 , Issue.2 , pp. 854-862
    • Maruyama, N.1    Katsube, T.2    Wada, Y.3    Oh, M.H.4    Barba de larosa, A.P.5    Okuda, E.6    Utsumi, S.7
  • 19
    • 0038644459 scopus 로고    scopus 로고
    • Thermally induced structural changes in glycinin, the 11S globulin of soya bean (Giycine max): An in situ spectroscopic study
    • Mills, E. N. C., Marigheto, N. A., Wellner, N., Fairhurst, S. A., Jenkins, J. A., Mann, R., & Belton, P. S. (2003). Thermally induced structural changes in glycinin, the 11S globulin of soya bean (Giycine max): An in situ spectroscopic study. Biochimica et Biophysica Acta, 1648(1-2), 105-114. doi:10.1016/S1570-9639(03)00114-6
    • (2003) Biochimica et Biophysica Acta , vol.1648 , Issue.1-2 , pp. 105-114
    • Mills, E.N.C.1    Marigheto, N.A.2    Wellner, N.3    Fairhurst, S.A.4    Jenkins, J.A.5    Mann, R.6    Belton, P.S.7
  • 20
    • 0036392199 scopus 로고    scopus 로고
    • Hydrolysates of native and modified soy protein isolates: Structural characteristics, solubility and foaming properties
    • Molina Ortiz, S. E., & Wagner, J. R. (2002). Hydrolysates of native and modified soy protein isolates: Structural characteristics, solubility and foaming properties. Food Research International, 35(6), 511-518. doi:10.1016/S0963-9969(01)00149-1
    • (2002) Food Research International , vol.35 , Issue.6 , pp. 511-518
    • Molina Ortiz, S.E.1    Wagner, J.R.2
  • 22
    • 1942467835 scopus 로고    scopus 로고
    • Microarray immunoassay: Association of clinical history, in vitro IgE function, and heterogeneity of allergenic peanut epitopes
    • Shreffler, W. G., Beyer, K., Chu, T. T., Burks, A. W., & Sampson, H. A. (2004). Microarray immunoassay: Association of clinical history, in vitro IgE function, and heterogeneity of allergenic peanut epitopes. Journal of Allergy and Clinical Immunology, 113(4), 776-782. doi:10.1016/j.jaci.2003.12.588
    • (2004) Journal of Allergy and Clinical Immunology , vol.113 , Issue.4 , pp. 776-782
    • Shreffler, W.G.1    Beyer, K.2    Chu, T.T.3    Burks, A.W.4    Sampson, H.A.5
  • 23
    • 0029844186 scopus 로고    scopus 로고
    • Limited proteolysis of β-conglycinin and glycinin, the 7S and 11S storage globulins from soybean (Glycine max (L.)Merr.): Structural and evolutionary implications
    • Shutov, A. D., Kakhovskaya, I. A., Bastrygina, A. S., Bulmaga, V. P., Horstmann, C., & Müntz, K. (1996). Limited proteolysis of β-conglycinin and glycinin, the 7S and 11S storage globulins from soybean (Glycine max (L.)Merr.): Structural and evolutionary implications. European Journal of Biochemistry, 241(1), 221-228. doi:10.1111/j.1432-1033.1996.0221t.x
    • (1996) European Journal of Biochemistry , vol.241 , Issue.1 , pp. 221-228
    • Shutov, A.D.1    Kakhovskaya, I.A.2    Bastrygina, A.S.3    Bulmaga, V.P.4    Horstmann, C.5    Müntz, K.6
  • 24
    • 48749114467 scopus 로고    scopus 로고
    • Quantification of human IgE immunoreactive soybean proteins in commercial soy ingredients and products
    • Song, Y. S., Martinez-Villaluenga, C., & De Mejia, E. G. (2008). Quantification of human IgE immunoreactive soybean proteins in commercial soy ingredients and products. Journal of Food Science, 73(6), T90-T99. doi:10.1111/j.1750-3841.2008.00848.x
    • (2008) Journal of Food Science , vol.73 , Issue.6
    • Song, Y.S.1    Martinez-Villaluenga, C.2    De Mejia, E.G.3
  • 25
    • 0006597308 scopus 로고    scopus 로고
    • Preparation of hypoallergenic soybean protein with processing functionality by selective enzymatic hydrolysis
    • Tsumura, K., Kugimiya, W., Bando, N., Hiemori, M., & Ogawa, T. (1999). Preparation of hypoallergenic soybean protein with processing functionality by selective enzymatic hydrolysis. Food Science and Technology Research, 5(2), 171-175. doi:10.3136/fstr.5.171
    • (1999) Food Science and Technology Research , vol.5 , Issue.2 , pp. 171-175
    • Tsumura, K.1    Kugimiya, W.2    Bando, N.3    Hiemori, M.4    Ogawa, T.5
  • 26
    • 3142603220 scopus 로고    scopus 로고
    • Selective proteolysis of the glycinin and beta-conglycinin fractions in a soy protein isolate by pepsin and papain with controlled pH and temperature
    • Tsumura, K., Saito, T., Kugimiya, W., & Inouye, K. (2004). Selective proteolysis of the glycinin and beta-conglycinin fractions in a soy protein isolate by pepsin and papain with controlled pH and temperature. Journal of Food Science, 69(5), C363-C367. doi:10.1111/j.1365-2621.2004.tb10698.x
    • (2004) Journal of Food Science , vol.69 , Issue.5
    • Tsumura, K.1    Saito, T.2    Kugimiya, W.3    Inouye, K.4
  • 27
    • 77955675440 scopus 로고    scopus 로고
    • Stability and immunoreactivity of glycinin and β-conglycinin to hydrolysis in vitro
    • Zhao, Y., Qin, G. X., Sun, Z. W., Zhang, B., & Wang, T. (2010). Stability and immunoreactivity of glycinin and β-conglycinin to hydrolysis in vitro. Food and Agricultural Immunology, 21(3), 253-263. doi:10.1080/09540101003758954
    • (2010) Food and Agricultural Immunology , vol.21 , Issue.3 , pp. 253-263
    • Zhao, Y.1    Qin, G.X.2    Sun, Z.W.3    Zhang, B.4    Wang, T.5


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