Research Article | Published:

Stability of food allergens to digestion in vitro

Nature Biotechnology volume 14, pages 12691273 (1996) | Download Citation

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Abstract

An integral part of the safety assessment of genetically modified plants is consideration of possible human health effects, especially food allergy. Prospective testing for allergenicity of proteins obtained from sources with no prior history of causing allergy has been difficult because of the absence of valid methods and models. Food allergens may share physicochemical properties that distinguish them from nonallergens, properties that may be used as a tool to predict the inherent allergenicity of proteins newly introduced into the food supply by genetic engineering. One candidate property is stability to digestion. We have systematically evaluated the stability of food allergens that are active via the gastrointestinal tract in a simple model of gastric digestion, emphasizing the major allergens of plant-derived foods such as legumes (peanuts and soybean). Important food allergens were stable to digestion in the gastric model (simulated gastric fluid). For example, soybean ß-conglycinin was stable for 60 min. In contrast, nonallergenic food proteins, such as spinach ribulose bis-phosphate carboxylase/oxygenase, were digested in simulated gastric fluid within 15 sec. The data are consistent with the hypothesis that food allergens must exhibit sufficient gastric stability to reach the intestinal mucosa where absorption and sensitization (development of atopy) can occur. Thus, the stability to digestion is a significant and valid parameter that distinguishes food allergens from nonallergens.

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References

  1. 1.

    , , , , , et al. 1995. Safety assessment of potatoes resistant to Colorado potato beetle, pp. 148–158 in ACS Symposium Series 605. Genetically modified foods. Safety issues. Engel, K-H., Takeoka, G.R., and Teranishi, R. (eds.). American Chemical Society, Washington, D.C.

  2. 2.

    , , , , , et al. 1996. New weed control opportunities: Development of soybeans with a Roundup Ready™ gene, pp. 53–84 in Herbicide-resistant crops. Agricultural, environmental, economic, regulatory, and technical aspects. Duke, S.O. (ed.). CRC Lewis Publishers, Boca Baton, FL

  3. 3.

    US Food and Drug Administration, Department of Health and Human Services, 1992. Statement of policy: Foods derived from new plant varieties. Fed. Regist. 57: 22984–23005.

  4. 4.

    , , , , and 1996. Identification of a Brazil-nut allergen in transgenic soybeans. N. Engl. J. Med. 334: 688–692.

  5. 5.

    , , , and 1996. Characterization of labile and stable allergens in foods of plant origin, pp. 130–149 in Food allergies and intolerances. Eisenbrand, G., Aulepp, H., Dayan, A.D., Bias, RS., Grunow, W., et al. (eds.). VCH Verlagsgesellschaft mbH, Weinheim.

  6. 7.

    1996. The chemistry and biology of food allergens. Food Tech. 50: 86–92.

  7. 8.

    , , , , , et al. 1993. Safety assessment of the neomycin phosphotransferase II (NPTII) protein. Bio/Technology 11: 1543–1547.

  8. 9.

    , , , , , et al. 1996. Safety assessment of 1-aminocyclopropane-1-carboxylic acid deaminase protein expressed in delayed ripening tomatoes. J. Agric. Food Chem. 44: 388–394.

  9. 10.

    , , and 1992. Fatal and near-fatal analphylactic reactions to food in children and adolescents. N. Engl. J. Med. 327: 380–384.

  10. 11.

    , , , , and 1980. Anaphylactic shock from mustard after ingestion of pizza. Contact Dermatitis 6: 294–295.

  11. 12.

    , , , , and 1980. Allergenicity of major component proteins of soybean. Int. Arch. Allergy Appl. Immunol. 61: 441–448.

  12. 13.

    , , , , , et al. 1991. Investigation of the IgE-binding proteins in soybeans by immunoblotting with the sera of the soybean-sensitive patients with atopic dermatitis. J. Nutr. Sci. Vitaminol. 37: 555–565.

  13. 14.

    , , , , , et al. 1993. Identification of the soybean allergenic protein, Gly m Bd 30K, with the soybean seed 34-kDa oil-body-associated protein. Biosci. Biotech. Biochem. 57: 1030–1033.

  14. 15.

    , , , , , et al. 1994. Identification of peanut agglutinin and soybean trypsin inhibitor as minor legume allergens. Int. Arch. Allergy Immunol. 105: 143–149.

  15. 16.

    , , , , , et al. 1991. Identification of a major peanut allergen, Ara h I , in patients with atopic dermatitis and positive peanut challenges. J. Allergy Clin. Immunol. 88: 172–179.

  16. 17.

    , , , , , et al. 1992. Identification and characterization of a second major peanut allergen, Ara h II, with use of sera of patients with atopic dermatatis and positive peanut challenge. J. Allergy Clin. Immunol. 90: 962–969.

  17. 18.

    , , , and 1988. Primary structure of the major allergen of yellow mustard (Sinapis alba L) seed, Sin a I. Eur. J. Biochem. 177: 159–166.

  18. 19.

    , , and 1991. Isolation and characterization of a major allergen from oriental mustard seeds, Bra j I. Int. Arch. Allergy Appl. Immunol. 96: 263–270.

  19. 20.

    1986. Immunologic and allergic properties of cow's milk proteins in humans. J. Food Protect. 49: 239–250.

  20. 21.

    , , and 1979. IgE antibodies to peptic and peptic-tryptic digests of betalactogbbulin: significance in food hypersensitivity. Ann. Allergy 42: 368–371.

  21. 22.

    , , , , and 1980. Milk hypersensitivity: RAST studies using new antigens generated by pepsin hydrolysis of beta-lactoglobulin. Ann. Allergy 45: 242–245.

  22. 23.

    Board of Trustees (ed.). 1995. Simulated Gastric Fluid, TS., pp. 2053 in The United States Pharmacopeia 23, The National Formulary 18. United States Pharmacopeial Convention, Inc., Rockville, MD.

  23. 24.

    1984. Pepsins, gastricsins and their zymogens, pp. 228–233 in Methods of Enzymatic Analysis. Bergmeyer, H.U. (ed.). Verlag Chemie, Deerfield Beach, FL.

  24. 25.

    and 1987. Tricine-sodium dodecyl sulfate-palyacryl-amide gel electrophoresis for separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166: 368–379.

  25. 26.

    and 1984. A rapid automated procedure for the determination of trypsin inhibitor activity in soy products and common foodstuffs. J. Agric. Food Chem. 32: 908–911.

  26. 27.

    1976. Legume toxins in relation to protein digestibility: A review. J. Food Sci. 41: 1076.

  27. 28.

    and 1987. In vitro enzymatic hydrolysis of phase-olin, the major storage protein of Phaseolus vilgaris L. J. Food Sci. 52: 1326–1329.

  28. 29.

    , , and 1989. Effects of in vitro proteolysis on the allergenicity of major whey proteins. J. Food Sci. 54: 1037–1039.

  29. 30.

    , , , , , et al. 1996. Assessment of the allergenic potential of foods derived from genetically engineered crop plants, in Allergenicity of foods produced by genetic modification. Fuchs, R.D., Fordham, J., Metcalfe, D., Sampson, H., Taylor, S., et al. (eds.). CRC Press, Boca Raton, FL. In press.

  30. 31.

    , , , , and 1995. Safety evaluation of Colorado potato beetle-protected potatoes, pp. 63–78 in Application of the principles of substantial equivalence to the safety evaluation of foods or food components from plants derived by modern biotechnology. World Health Organization, Food Safety Unit.

  31. 32.

    and 1996. Preventing food allergy: emerging technologies. Trends Food Sci.Technol. 7: 219–226.

  32. 33.

    , , , , and 1993. Preparation and application of monoclonal antibodies for a sandwich enzyme-linked immunosor-bant assay of the major soybean allergen, Gly m Bd 30K. J. Nutr. Sci. Vitaminol. 39: 389–397.

  33. 34.

    , , , , et al. 1993. Characterization of a new oriental-mustard (Brassica juncea) allergen, Bra j IE: detection of an allergenic epitope. Biochem. J. 293: 625–632.

  34. 35.

    and 1988. Immunoblotting, pp. 1–726 in Antibodies: A laboratory manual. Cold Spring Harbor Laboratory, Cold Spring Harbor, NY.

  35. 36.

    , , and 1989. Modifications for SDS-PAGE of proteins. BioTechniques 7: 692–693.

  36. 37.

    , , , and 1988. Improved staining of proteins in polyacrylamide gels including isoelectric focusing gels with clear background at nanogram sensitivity using Coumassie brilliant blue G-250 and R-250. Electrophoresis 9: 255–262.

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Author notes

    • Roy L. Fuchs

    Corresponding author (e-mail:rlfuch@ccmailmonsanto.com).

Affiliations

  1. Regulatory Science, Mail Zone 664], Monsanto Company, St. Louis, MO 63198.

    • James D. Astwood
    • , John N. Leach
    •  & Roy L. Fuchs

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DOI

https://doi.org/10.1038/nbt1096-1269

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