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Int Arch Allergy Immunol ; 162(2): 123-30, 2013.
Article in English | MEDLINE | ID: mdl-23921317

ABSTRACT

BACKGROUND: Peanut flour is a high-protein, low-oil, powdered material prepared from roasted peanut seed. In addition to being a well-established food ingredient, peanut flour is also the active ingredient in peanut oral immunotherapy trials. Enzymatic hydrolysis was evaluated as a processing strategy to generate hydrolysates from peanut flour with reduced allergenicity. METHODS: Soluble fractions of 10% (w/v) light roasted peanut flour dispersions were hydrolyzed with the following proteases: Alcalase (pH 8.0, 60°C), pepsin (pH 2.0, 37°C) or Flavourzyme (pH 7.0, 50°C) for 60 min. Western blotting, inhibition ELISA and basophil activation tests were used to examine IgE reactivity. RESULTS: Western blotting experiments revealed the hydrolysates retained IgE binding reactivity and these IgE-reactive peptides were primarily Ara h 2 fragments regardless of the protease tested. Inhibition ELISA assays demonstrated that each of the hydrolysates had decreased capacity to bind peanut-specific IgE compared with nonhydrolyzed controls. Basophil activation tests revealed that all hydrolysates were comparable (p > 0.05) to nonhydrolyzed controls in IgE cross-linking capacity. CONCLUSIONS: These results indicate that hydrolysis of peanut flour reduced IgE binding capacity; however, IgE cross-linking capacity during hydrolysis was retained, thus suggesting such hydrolysates are not hypoallergenic.


Subject(s)
2S Albumins, Plant/immunology , Antigens, Plant/immunology , Glycoproteins/immunology , Peanut Hypersensitivity/immunology , Plant Extracts/immunology , Arachis/immunology , Arachis/metabolism , Binding Sites, Antibody , Endopeptidases/metabolism , Humans , Immunoglobulin E/immunology , Pepsin A/metabolism , Peptide Fragments/immunology , Plant Proteins/immunology , Proteolysis , Subtilisins/metabolism
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