메뉴 건너뛰기




Volumn 61, Issue 24, 2013, Pages 5903-5913

Effect of simulated gastric and intestinal digestion on temporal stability and immunoreactivity of peanut, almond, and pine nut protein allergens

Author keywords

digestibility; food allergens; immunoreactivity; peanuts; tree nuts

Indexed keywords

DIGESTIBILITY; FOOD ALLERGEN; IMMUNOREACTIVITIES; PEANUTS; TREE NUTS;

EID: 84879376452     PISSN: 00218561     EISSN: 15205118     Source Type: Journal    
DOI: 10.1021/jf400953q     Document Type: Article
Times cited : (26)

References (38)
  • 1
    • 0023491404 scopus 로고
    • Food allergens: Structure and immunologic properties
    • Taylor, S.; Lemanske, R., Jr.; Bush, R.; Busse, W. Food allergens: structure and immunologic properties Ann. Allergy 1987, 59, 93-99
    • (1987) Ann. Allergy , vol.59 , pp. 93-99
    • Taylor, S.1    Lemanske, Jr.R.2    Bush, R.3    Busse, W.4
  • 2
    • 0002810940 scopus 로고    scopus 로고
    • Allergenicity assessment of foods derived from genetically modified plants
    • Fuchs, R.; Astwood, J. Allergenicity assessment of foods derived from genetically modified plants Food Technol. 1996, 50, 83-88
    • (1996) Food Technol. , vol.50 , pp. 83-88
    • Fuchs, R.1    Astwood, J.2
  • 4
    • 0018956182 scopus 로고
    • Milk hypersensitivity: RAST studies using new antigens generated by pepsin hydrolysis of beta-lactoglobulin
    • Schwartz, H.; Nerurkar, L.; Spies, J.; Scanlon, R.; Bellanti, J. Milk hypersensitivity: RAST studies using new antigens generated by pepsin hydrolysis of beta-lactoglobulin Ann. Allergy 1980, 45, 242-245
    • (1980) Ann. Allergy , vol.45 , pp. 242-245
    • Schwartz, H.1    Nerurkar, L.2    Spies, J.3    Scanlon, R.4    Bellanti, J.5
  • 5
    • 0020825442 scopus 로고
    • Immunochemical and physical properties of peptic-digested ovomucoid
    • Matsuda, T.; Watanabe, K.; Nakamura, R. Immunochemical and physical properties of peptic-digested ovomucoid J. Agric. Food Chem. 1983, 31, 942-946
    • (1983) J. Agric. Food Chem. , vol.31 , pp. 942-946
    • Matsuda, T.1    Watanabe, K.2    Nakamura, R.3
  • 6
    • 0037100401 scopus 로고    scopus 로고
    • Protein structure plays a critical role in peanut allergen stability and may determine immunodominant IgE-binding epitopes
    • Sen, M.; Kopper, R.; Pons, L.; Abraham, E.; Burks, A.; Bannon, G. Protein structure plays a critical role in peanut allergen stability and may determine immunodominant IgE-binding epitopes J. Immunol. 2002, 169, 882-887
    • (2002) J. Immunol. , vol.169 , pp. 882-887
    • Sen, M.1    Kopper, R.2    Pons, L.3    Abraham, E.4    Burks, A.5    Bannon, G.6
  • 7
    • 0019570118 scopus 로고
    • Amino acids, sugars, and inorganic elements in the sweet almond (Prunus amygdalus)
    • Calixto, F.; Bauza, M.; Martinez De Toda, F.; Argamernteria, A. Amino acids, sugars, and inorganic elements in the sweet almond (Prunus amygdalus) J. Agric. Food Chem. 1981, 290, 509-511
    • (1981) J. Agric. Food Chem. , vol.290 , pp. 509-511
    • Calixto, F.1    Bauza, M.2    Martinez De Toda, F.3    Argamernteria, A.4
  • 8
    • 84985376634 scopus 로고
    • Protein extractability of almond (Prunus amygdalus Batsch) seed
    • Esteban, R.; Lopex-Andreo, F.; Carpena, O. Protein extractability of almond (Prunus amygdalus Batsch) seed J. Sci. Food Agric. 1985, 36, 485-490
    • (1985) J. Sci. Food Agric. , vol.36 , pp. 485-490
    • Esteban, R.1    Lopex-Andreo, F.2    Carpena, O.3
  • 9
    • 0033393790 scopus 로고    scopus 로고
    • Food allergy: When and how to perform oral food challenges
    • Sicherer, S. Food allergy: when and how to perform oral food challenges Pediatr. Allergy Immunol. 1999, 10, 226-234
    • (1999) Pediatr. Allergy Immunol. , vol.10 , pp. 226-234
    • Sicherer, S.1
  • 11
    • 0029764078 scopus 로고    scopus 로고
    • Stability of food allergens to digestion in vitro
    • Astwood, J.; Leach, J.; Fuchs, R. Stability of food allergens to digestion in vitro Nat. Biotechnol. 1996, 14, 1269-1273
    • (1996) Nat. Biotechnol. , vol.14 , pp. 1269-1273
    • Astwood, J.1    Leach, J.2    Fuchs, R.3
  • 12
    • 84879350105 scopus 로고    scopus 로고
    • U.S. Pharmacopeia 23, Simulated Gastric Fluid and Simulated Intestinal Fluid, The National Formulary 18; U.S. Pharmacopeial Convention, Inc. Rockville, MD
    • U.S. Pharmacopeia 23, Simulated Gastric Fluid and Simulated Intestinal Fluid, The National Formulary 18; U.S. Pharmacopeial Convention, Inc.: Rockville, MD, 2006; pp 3171.
    • (2006) , pp. 3171
  • 13
    • 84879325696 scopus 로고    scopus 로고
    • Food and Agriculture Organization ProdStat Database, (accessed Jan 19)
    • Food and Agriculture Organization ProdStat Database, http://faostat.foa. org (accessed Jan 19, 2012).
    • (2012)
  • 15
    • 0034921889 scopus 로고    scopus 로고
    • A voluntary registry for peanut and tree nut allergy: Characteristics of the first 5149 registrants
    • Sicherer, S.; Furlong, T.; Muñoz-Furlong, A.; Burks, A.; Sampson, H. A voluntary registry for peanut and tree nut allergy: characteristics of the first 5149 registrants J Allergy Clin Immunol. 2001, 108, 128-132
    • (2001) J Allergy Clin Immunol. , vol.108 , pp. 128-132
    • Sicherer, S.1    Furlong, T.2    Muñoz-Furlong, A.3    Burks, A.4    Sampson, H.5
  • 16
    • 0033213201 scopus 로고    scopus 로고
    • Production and characterization of rabbit polyclonal antibodies to almond (Prunus dulcis L.) major storage protein
    • Acosta, M.; Roux, K.; Teuber, S.; Sathe, S. Production and characterization of rabbit polyclonal antibodies to almond (Prunus dulcis L.) major storage protein J. Agric. Food Chem. 1999, 47, 4053-4059
    • (1999) J. Agric. Food Chem. , vol.47 , pp. 4053-4059
    • Acosta, M.1    Roux, K.2    Teuber, S.3    Sathe, S.4
  • 17
    • 84856831464 scopus 로고    scopus 로고
    • Almond allergens: Molecular characterization, detection, and clinical relevance
    • Costa, J.; Mafra, I.; Carrapatoso, I.; Oliveira, M. Almond allergens: molecular characterization, detection, and clinical relevance J. Agric. Food Chem. 2012, 60, 1337-1349
    • (2012) J. Agric. Food Chem. , vol.60 , pp. 1337-1349
    • Costa, J.1    Mafra, I.2    Carrapatoso, I.3    Oliveira, M.4
  • 18
    • 84986454536 scopus 로고
    • Solubilization, electrophoretic characterization and in vitro digestibility of almond (Prunus amygdalus) proteins
    • Sathe, J. Solubilization, electrophoretic characterization and in vitro digestibility of almond (Prunus amygdalus) proteins J. Food Biochem. 1993, 16, 249-264
    • (1993) J. Food Biochem. , vol.16 , pp. 249-264
    • Sathe, J.1
  • 19
    • 0034877015 scopus 로고    scopus 로고
    • Electrophoretic and immunological analyses of almond (Prunus dulcis L.) genotypes and hybrids
    • Sathe, S.; Teuber, S.; Gradziel, T.; Roux, K. Electrophoretic and immunological analyses of almond (Prunus dulcis L.) genotypes and hybrids J. Agric. Food Chem. 2001, 49, 2043-2052
    • (2001) J. Agric. Food Chem. , vol.49 , pp. 2043-2052
    • Sathe, S.1    Teuber, S.2    Gradziel, T.3    Roux, K.4
  • 21
    • 84987277445 scopus 로고
    • IgE-binding proteins in almonds (Prunus amygdalus); Identification by immunoblotting with sera from almond-allergic adults
    • Bargman, T.; Rupnow, J.; Taylor, S. IgE-binding proteins in almonds (Prunus amygdalus); identification by immunoblotting with sera from almond-allergic adults J. Food Sci. 1992, 57, 717-720
    • (1992) J. Food Sci. , vol.57 , pp. 717-720
    • Bargman, T.1    Rupnow, J.2    Taylor, S.3
  • 27
    • 77954381622 scopus 로고    scopus 로고
    • Detection and structural characterization of natural Ara h 7, the third peanut allergen of the 2S albumin family
    • Schmidt, H.; Krause, S.; Gelhaus, C.; Petersen, A.; Janssen, O.; Becker, W. Detection and structural characterization of natural Ara h 7, the third peanut allergen of the 2S albumin family J. Proteome Res. 2010, 9, 3701-3709
    • (2010) J. Proteome Res. , vol.9 , pp. 3701-3709
    • Schmidt, H.1    Krause, S.2    Gelhaus, C.3    Petersen, A.4    Janssen, O.5    Becker, W.6
  • 28
    • 78649887557 scopus 로고    scopus 로고
    • Digestion of peanut allergens Ara h 1, Ara h 2, Ara h 3, and Ara h 6: A comparative in vitro study and partial characterization of digestion-resistant peptides
    • Koppelman, S.; Hefle, S.; Taylor, S.; de Jong, G. Digestion of peanut allergens Ara h 1, Ara h 2, Ara h 3, and Ara h 6: a comparative in vitro study and partial characterization of digestion-resistant peptides Mol. Nutr. Food Res. 2010, 54, 1711-1721
    • (2010) Mol. Nutr. Food Res. , vol.54 , pp. 1711-1721
    • Koppelman, S.1    Hefle, S.2    Taylor, S.3    De Jong, G.4
  • 29
    • 17744371487 scopus 로고    scopus 로고
    • Purification and immunoglobulin E-binding properties of peanut allergen Ara h 6: Evidence for cross-reactivity with Ara h 2
    • Koppelman, S.; de Jong, G.; Laaper-Ertmann, M.; Peeters, K.; Knulst, A.; Hefle, S.; Knol, E. Purification and immunoglobulin E-binding properties of peanut allergen Ara h 6: evidence for cross-reactivity with Ara h 2 Clin. Exp. Allergy 2005, 35, 490-497
    • (2005) Clin. Exp. Allergy , vol.35 , pp. 490-497
    • Koppelman, S.1    De Jong, G.2    Laaper-Ertmann, M.3    Peeters, K.4    Knulst, A.5    Hefle, S.6    Knol, E.7
  • 30
    • 2042449746 scopus 로고    scopus 로고
    • Relevance of Ara h1, Ara h2 and Ara h3 in peanut-allergic patients, as determined by immunoglobulin e Western blotting, basophil-histamine release and intracutaneous testing: Ara h2 is the most important peanut allergen
    • Koppelman, S.; Wensing, M.; Ertmann, M.; Knulst, A.; Knol, E. Relevance of Ara h1, Ara h2 and Ara h3 in peanut-allergic patients, as determined by immunoglobulin E Western blotting, basophil-histamine release and intracutaneous testing: Ara h2 is the most important peanut allergen Clin. Exp. Allergy 2004, 34, 583-590
    • (2004) Clin. Exp. Allergy , vol.34 , pp. 583-590
    • Koppelman, S.1    Wensing, M.2    Ertmann, M.3    Knulst, A.4    Knol, E.5
  • 31
    • 0032812397 scopus 로고    scopus 로고
    • Selective cloning of peanut allergens, including profilin and 2S albumins, by phage display technology
    • Kleber-Janke, T.; Crameri, R.; Appenzeller, U.; Schlaak, M.; Becker, W. Selective cloning of peanut allergens, including profilin and 2S albumins, by phage display technology Int. Arch. Allergy Immunol. 1999, 119, 265-274
    • (1999) Int. Arch. Allergy Immunol. , vol.119 , pp. 265-274
    • Kleber-Janke, T.1    Crameri, R.2    Appenzeller, U.3    Schlaak, M.4    Becker, W.5
  • 32
    • 0035053448 scopus 로고    scopus 로고
    • Four novel recombinant peanut allergens: More information, more problems
    • Becker, W.; Kleber-Janke, T.; Lepp, U. Four novel recombinant peanut allergens: more information, more problems Int. Arch. Allergy Immunol. 2001, 124, 100-102
    • (2001) Int. Arch. Allergy Immunol. , vol.124 , pp. 100-102
    • Becker, W.1    Kleber-Janke, T.2    Lepp, U.3
  • 33
    • 9644262438 scopus 로고    scopus 로고
    • Ara h 8, a Bet v 1-homologous allergen from peanuts is a major allergen in patients with combined birch pollen and peanut allergy
    • Mittag, D.; Akkerdaas, J.; Ballmer-Weber, B.; Vogel, L. Ara h 8, a Bet v 1-homologous allergen from peanuts is a major allergen in patients with combined birch pollen and peanut allergy J. Allergy Clin. Immunol. 2004, 114, 1410-1417
    • (2004) J. Allergy Clin. Immunol. , vol.114 , pp. 1410-1417
    • Mittag, D.1    Akkerdaas, J.2    Ballmer-Weber, B.3    Vogel, L.4
  • 35
    • 84876725555 scopus 로고    scopus 로고
    • Redefining the major peanut allergens
    • Zhuang, Y.; Dreskin, S. Redefining the major peanut allergens Immunol. Res. 2013, 55, 125-134
    • (2013) Immunol. Res. , vol.55 , pp. 125-134
    • Zhuang, Y.1    Dreskin, S.2
  • 36
    • 0001049205 scopus 로고    scopus 로고
    • Digestibility of peanut and hazelnut allergens investigated by a simple in vitro procedure
    • Veiths, S.; Reindl, J.; Muller, U.; Hoffmann, A. Digestibility of peanut and hazelnut allergens investigated by a simple in vitro procedure Eur. Food Res. Technol. 1999, 209, 379-388
    • (1999) Eur. Food Res. Technol. , vol.209 , pp. 379-388
    • Veiths, S.1    Reindl, J.2    Muller, U.3    Hoffmann, A.4
  • 37
    • 0030183514 scopus 로고    scopus 로고
    • Why are some proteins allergenic? Implications for biotechnology
    • Lehrer, S.; Horner, W.; Reese, G. Why are some proteins allergenic? Implications for biotechnology Crit. Rev. Food Sci. Nutr. 1996, 36, 553-564
    • (1996) Crit. Rev. Food Sci. Nutr. , vol.36 , pp. 553-564
    • Lehrer, S.1    Horner, W.2    Reese, G.3
  • 38
    • 0034120710 scopus 로고    scopus 로고
    • Structure of the major peanut allergen Ara h 1 may protect IgE-binding epitopes from degradation
    • Maleki, S.; Kopper, R.; Shin, D.; Park, C.; Compadre, C.; Sampson, H.; Burks, A.; Bannon, G. Structure of the major peanut allergen Ara h 1 may protect IgE-binding epitopes from degradation J. Immunol. 2000, 164, 5844-5849
    • (2000) J. Immunol. , vol.164 , pp. 5844-5849
    • Maleki, S.1    Kopper, R.2    Shin, D.3    Park, C.4    Compadre, C.5    Sampson, H.6    Burks, A.7    Bannon, G.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.