메뉴 건너뛰기




Volumn 129, Issue 4, 2011, Pages 1598-1605

Digestibility and immunoreactivity of soybean β-conglycinin and its deglycosylated form

Author keywords

Conglycinin; Deglycosylation; Glycan moieties; In vitro digestibility; In vitro immunoreactivity; Soybean

Indexed keywords

CONGLYCININ; DEGLYCOSYLATION; GLYCAN MOIETIES; IN VITRO DIGESTIBILITY; IN VITRO IMMUNOREACTIVITY; SOYBEAN;

EID: 80051784149     PISSN: 03088146     EISSN: 18737072     Source Type: Journal    
DOI: 10.1016/j.foodchem.2011.06.015     Document Type: Article
Times cited : (44)

References (28)
  • 1
    • 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
    • A. Adachi, T. Horikawa, H. Shimizu, Y. Sarayama, T. Ogawa, and S. Sjolander 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 2009 167 173
    • (2009) Clinical and Experimental Allergy , vol.39 , pp. 167-173
    • Adachi, A.1    Horikawa, T.2    Shimizu, H.3    Sarayama, Y.4    Ogawa, T.5    Sjolander, S.6
  • 4
    • 0029764078 scopus 로고    scopus 로고
    • Stability of food allergens to digestion in vitro
    • J.D. Astwood, J.N. Leach, and R.L. Fuchs Stability of food allergens to digestion in vitro Nature Biotechnology 14 10 1996 1269 1273 (Pubitemid 26332788)
    • (1996) Nature Biotechnology , vol.14 , Issue.10 , pp. 1269-1273
    • Astwood, J.D.1    Leach, J.N.2    Fuchs, R.L.3
  • 6
    • 0003104374 scopus 로고
    • Legume storage protein and their genes
    • (vol 3, pp. 1-95) B.J. Miflin, Oxford University Press Oxford, United Kingdom
    • R. Casey, C. Domoney, and N. Ellis Legume storage protein and their genes (vol 3, pp. 1-95) B.J. Miflin, Oxford Surveys of Plant Molecular and Cell Biology 1986 Oxford University Press Oxford, United Kingdom
    • (1986) Oxford Surveys of Plant Molecular and Cell Biology
    • Casey, R.1    Domoney, C.2    Ellis, N.3
  • 7
    • 0035096518 scopus 로고    scopus 로고
    • Enzymatic protein hydrolysates in human nutrition
    • A. Clemente Enzymatic protein hydrolysates in human nutrition Trends in Food Science and Technology 11 2000 254 262
    • (2000) Trends in Food Science and Technology , vol.11 , pp. 254-262
    • Clemente, A.1
  • 8
    • 0032866519 scopus 로고    scopus 로고
    • Production of extensive chickpea (Cicer arietinum L.) Protein hydrolysates with reduced antigenic activity
    • DOI 10.1021/jf981315p
    • A. Clemente, J. Vioque, R. Sanchez-Vioque, J. Pedroche, and F. Millán Production of extensive chickpea (Cicer arietinum L.) protein hydrolysates with reduced antigenic activity Journal of Agricultural and Food Chemistry 47 1999 3776 3781 (Pubitemid 29449505)
    • (1999) Journal of Agricultural and Food Chemistry , vol.47 , Issue.9 , pp. 3776-3781
    • Clemente, A.1    Vioque, J.2    Sanchez-Vioque, R.3    Pedroche, J.4    Millan, F.5
  • 9
    • 0033120873 scopus 로고    scopus 로고
    • Transcellular uptake mechanisms of the intestinal epithelial barrier - Part one
    • DOI 10.1016/S1461-5347(99)00142-X, PII S146153479900142X
    • A.L. Daugherty, and R.J. Mrsny Transcellular uptake mechanisms of the intestinal epithelial barrier - Part one Pharmaceutical Science and Technology Today 2 1999 144 151 (Pubitemid 29195747)
    • (1999) Pharmaceutical Science and Technology Today , vol.2 , Issue.4 , pp. 144-151
    • Daugherty, A.L.1    Mrsny, R.J.2
  • 10
    • 0022977063 scopus 로고
    • The glycosylated seed storage proteins of Glycine max and Phaseolus vulgaris. Structural homologies of genes and proteins
    • J.J. Doyle, M.A. Schuler, W.D. Godette, V. Zenger, R.N. Beachy, and J.L. Slightom The glycosylated seed storage proteins of Glycine max and Phaseolus vulgaris - structural homologies of genes and proteins The Journal of Biological Chemistry 261 1986 9228 9238 (Pubitemid 17218199)
    • (1986) Journal of Biological Chemistry , vol.261 , Issue.20 , pp. 9228-9238
    • Doyle, J.J.1    Schuler, M.A.2    Godette, W.D.3
  • 11
    • 34249904970 scopus 로고    scopus 로고
    • Identification, characterization, epitope mapping, and three-dimensional modeling of the α-subunit of β-conglycinin of soybean, a potential allergen for young pigs
    • DOI 10.1021/jf070211o
    • C.J. Fu, J.M. Jez, M.S. Kerley, G.L. Allee, and H.B. Krishnan Identification, characterization, epitope mapping, and three-dimensional modeling of the α-subunit of α-conglycinin of soybean, a potential allergen for young pigs Journal of Agricultural and Food Chemistry 55 2007 4014 4020 (Pubitemid 46867410)
    • (2007) Journal of Agricultural and Food Chemistry , vol.55 , Issue.10 , pp. 4014-4020
    • Fu, C.1    Jez, J.M.2    Kerley, M.S.3    Allee, G.L.4    Krishnan, H.B.5
  • 15
    • 80051788222 scopus 로고    scopus 로고
    • Assessment of food proteins for allergenic potential
    • B.G. Hammond, CRC Press Taylor & Francis Group Boca Raton
    • S. Mc Clain, S. Vieths, and G.A. Bannon Assessment of food proteins for allergenic potential B.G. Hammond, Food safety of proteins in agricultural biotechnology 2008 CRC Press Taylor & Francis Group Boca Raton 209 222
    • (2008) Food Safety of Proteins in Agricultural Biotechnology , pp. 209-222
    • Mc Clain, S.1    Vieths, S.2    Bannon, G.A.3
  • 16
    • 33846567968 scopus 로고    scopus 로고
    • Gastrointestinal digestion of food allergens: Effect on their allergenicity
    • DOI 10.1016/j.biopha.2006.10.005, PII S0753332206003374
    • F.J. Moreno Gastrointestinal digestion of food allergens: Effect on their allergenicity Biomedicine and Pharmacotherapy 61 2007 50 60 (Pubitemid 46185880)
    • (2007) Biomedicine and Pharmacotherapy , vol.61 , Issue.1 , pp. 50-60
    • Moreno, F.J.1
  • 17
    • 85056063589 scopus 로고    scopus 로고
    • 2S albumin storage proteins: What makes them food allergens?
    • F.J. Moreno, and A. Clemente 2S albumin storage proteins: What makes them food allergens? The Open Biochemistry Journal 2 2008 16 28
    • (2008) The Open Biochemistry Journal , vol.2 , pp. 16-28
    • Moreno, F.J.1    Clemente, A.2
  • 18
    • 33750967379 scopus 로고    scopus 로고
    • Uptake of 2S albumin allergens, Ber e 1 and Ses i 1, across human intestinal epithelial Caco-2 cell monolayers
    • DOI 10.1021/jf061760h
    • F.J. Moreno, L.A. Rubio, A. Olano, and A. Clemente Uptake of 2S albumin allergens, Ber e 1 and Ses i 1, across human intestinal epithelial Caco-2 cell monolayers Journal of Agricultural and Food Chemistry 54 2006 8631 8639 (Pubitemid 44747676)
    • (2006) Journal of Agricultural and Food Chemistry , vol.54 , Issue.22 , pp. 8631-8639
    • Moreno, F.J.1    Rubio, L.A.2    Olano, A.3    Clemente, A.4
  • 20
    • 85007881885 scopus 로고
    • Alpha-subunit of β-Conglycinin, an allergenic protein recognized by IgE antibodies of soybean-sensitive patients with atopic-dermatitis
    • T. Ogawa, N. Bando, H. Tsuji, K. Nishikawa, and K. Kitamura Alpha-subunit of β-Conglycinin, an allergenic protein recognized by IgE antibodies of soybean-sensitive patients with atopic-dermatitis Bioscience, Biotechnology and Biochemistry 59 1995 831 833
    • (1995) Bioscience, Biotechnology and Biochemistry , vol.59 , pp. 831-833
    • Ogawa, T.1    Bando, N.2    Tsuji, H.3    Nishikawa, K.4    Kitamura, K.5
  • 22
    • 48749114467 scopus 로고    scopus 로고
    • Quantification of human IgE immunoreactive soybean proteins in commercial soy ingredients and products
    • Y.S. Song, C. Martinez-Villaluenga, and E.G. de Mejia Quantification of human IgE immunoreactive soybean proteins in commercial soy ingredients and products Journal of Food Science 73 2008 T90 T99
    • (2008) Journal of Food Science , vol.73
    • Song, Y.S.1    Martinez-Villaluenga, C.2    De Mejia, E.G.3
  • 23
    • 0017598953 scopus 로고
    • Beta conglycinin from soybean proteins. Isolation and immunological and physicochemical properties of the monomeric forms
    • V.H. Thanh, and K. Shibasaki β-Conglycinin from soybean proteins isolation and immunological and physicochemical properties of the monomeric forms Biochimica et Biophysica Acta 490 1977 370 384 (Pubitemid 8028475)
    • (1977) Biochimica et Biophysica Acta , vol.490 , Issue.2 , pp. 370-384
    • Thanh, V.H.1    Shibasaki, K.2
  • 25
    • 70450247005 scopus 로고    scopus 로고
    • Comparative study on the stability of soybean (Glycine max)-conglycinin in vivo
    • T. Wang, G.X. Qin, Y. Zhao, and Z.W. Sun Comparative study on the stability of soybean (Glycine max)-conglycinin in vivo Food and Agricultural Immunology 20 2009 295 304
    • (2009) Food and Agricultural Immunology , vol.20 , pp. 295-304
    • Wang, T.1    Qin, G.X.2    Zhao, Y.3    Sun, Z.W.4
  • 26
    • 48749116812 scopus 로고    scopus 로고
    • Purification, thermal stability, and antigenicity of the immunodominant soybean allergen P34 in soy cultivars, ingredients, and products
    • S. Wilson, C. Martinez-Villaluenga, and E.G. de Mejia Purification, thermal stability, and antigenicity of the immunodominant soybean allergen P34 in soy cultivars, ingredients, and products Journal of Food Science 73 6 2008 T106 T114
    • (2008) Journal of Food Science , vol.73 , Issue.6
    • Wilson, S.1    Martinez-Villaluenga, C.2    De Mejia, E.G.3
  • 28
    • 77955675440 scopus 로고    scopus 로고
    • Stability and immunoreactivity of glycinin and β-conglycinin to hydrolysis in vitro
    • Y. Zhao, G.X. Qin, Z.W. Sun, B. Zhang, and T. Wang Stability and immunoreactivity of glycinin and β-conglycinin to hydrolysis in vitro Food Agricultural Immunology 21 2010 253 263
    • (2010) Food Agricultural Immunology , vol.21 , pp. 253-263
    • Zhao, Y.1    Qin, G.X.2    Sun, Z.W.3    Zhang, B.4    Wang, T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.