Back to Search
Start Over
Allergenic Properties of Enzymatically Hydrolyzed Peanut Flour Extracts
- Source :
- International Archives of Allergy and Immunology. 162:123-130
- Publication Year :
- 2013
- Publisher :
- S. Karger AG, 2013.
-
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.
- Subjects :
- Arachis
Immunology
Peanut allergy
Ingredient
Hydrolysis
Endopeptidases
Inhibition elisa
medicine
Humans
Immunology and Allergy
Peanut Hypersensitivity
Subtilisins
Food science
Glycoproteins
Plant Proteins
Plant Extracts
Chemistry
fungi
food and beverages
General Medicine
Antigens, Plant
Immunoglobulin E
medicine.disease
Pepsin A
Peptide Fragments
Proteolysis
Binding Sites, Antibody
2S Albumins, Plant
Subjects
Details
- ISSN :
- 14230097 and 10182438
- Volume :
- 162
- Database :
- OpenAIRE
- Journal :
- International Archives of Allergy and Immunology
- Accession number :
- edsair.doi.dedup.....5c506d5953cd95a988e666730f369dbc