Effect of pH and temperature on the immunogenicity of glycinin (Glycine max L.)

Sensitive immunologic techniques for the detection of alterations that occur in protein antigens were used to evaluate the immunogenicity of soybean glycinin after isolation, heat denaturation and pH alteration. The objective was to determine the effect of these agents on the immunogenic ability of...

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Bibliographic Details
Published in:Plant foods for human nutrition (Dordrecht) 1997, Vol.50 (1), p.63-69
Main Authors: Demonte, A. (Faculty of Pharmaceutical Sciences, Araraquara, Unesp, SP (Brazil). Dept. of Food Nutrition), Carlos, I.Z, Lourenco, E.J, Dutra de Oliveira, J.E
Format: Article
Language:English
Subjects:
ALERGENOS
ALLERGENE
ALLERGENS
Antigens - immunology
Antigens, allergens
Biological and medical sciences
Chemical Phenomena
Chemistry, Physical
Chromatography, Gel
Enzyme-Linked Immunosorbent Assay
Fundamental and applied biological sciences. Psychology
Fundamental immunology
Globulins - chemistry
Globulins - immunology
Glycine max - chemistry
Glycine max - immunology
Hydrogen-Ion Concentration
Immediate hypersensitivity. Allergy. Anaphylaxis, etc
IMMUNE RESPONSE
Immune Sera - immunology
Immunobiology
PROTEINAS
PROTEINE
PROTEINS
REPONSE IMMUNITAIRE
RESPUESTA INMUNOLOGICA
SOJA
Soybean Proteins
SOYBEANS
TEMPERATURA
TEMPERATURE
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Summary:Sensitive immunologic techniques for the detection of alterations that occur in protein antigens were used to evaluate the immunogenicity of soybean glycinin after isolation, heat denaturation and pH alteration. The objective was to determine the effect of these agents on the immunogenic ability of this protein fraction. Immunologic assays performed on heat-denatured glycinin up to 80 degrees C in the presence of antinative glycinin serum demonstrated that glycinin retains its immunogenic properties. Above 90 degrees C this biological property begins to disappear, with protein insolubilization and epitope modification due to the conformational changes imposed by temperature. A reduction in immunogenicity also occurred when glycinin was taken to pH 2.0 (below its pl) and pH 11.00 (above its pl) and exposed to high temperatures in the presence of native antiglycinin serum. From these data one can conclude that, at extreme pH values, intramolecular reactions may occur which, in combination with the structural disorganization caused by high temperatures, may contribute to the reduction of immunogenicity.
ISSN:0921-9668
1573-9104
DOI:10.1007/BF02436044