Select | PubMed ID | Description |
| 18727014 | Mol Nutr Food Res. 2008 Nov;52 Suppl 2:S272-85. doi: 10.1002/mnfr.200700524.
Purification and characterisation of a panel of peanut allergens suitable for use in allergy diagnosis.
Marsh J(1), Rigby N, Wellner K, Reese G, Knulst A, Akkerdaas J, van Ree R, Radauer C, Lovegrove A, Sancho A, Mills C, Vieths S, Hoffmann-Sommergruber K, Shewry PR.
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| 23495786 | J Agric Food Chem. 2013 Apr 17;61(15):3714-25. doi: 10.1021/jf305347r. Epub 2013 Apr 8.
Analysis of crude protein and allergen abundance in peanuts (Arachis hypogaea cv. Walter) from three growing regions in Australia.
Walczyk NE(1), Smith PM, Tovey E, Wright GC, Fleischfresser DB, Roberts TH.
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| 24057594 | Biol Chem. 2014 Feb;395(2):239-50. doi: 10.1515/hsz-2013-0206.
Roasting and lipid binding provide allergenic and proteolytic stability to the peanut allergen Ara h 8.
Petersen A, Rennert S, Kull S, Becker WM, Notbohm H, Goldmann T, Jappe U.
Abstract Ara h 8 is the peanut allergen homologous to the birch pollen allergen Bet v 1. Because Bet v 1 has been shown to bind lipophilic ligands, the aim of this investigation was to determine the impact of lipid binding and roasting on the Ara h 8 structure and their influences on allergenicity. For the characterization of natural Ara h 8 (nAra h 8) from roasted and unroasted peanuts, circular dichroism spectroscopy, hydrophobic binding assay, immunohistochemistry, and immunoblot with sera of peanut allergic patients were performed and compared with results from recombinant Ara h 8 (rAra h 8) and Bet v rAra h 8 displayed stronger hydrophobicity than rBet v 1. Patients' sera showed IgE reactivity with rAra h 8 and nAra h 8 from roasted peanuts, whereas fewer sera recognized nAra h 8 from unroasted peanuts. Simulated gastric digestion experiments demonstrated low proteolytic stability of rAra h 8, whereas the stability of nAra h 8 was increasingly higher in unroasted and roasted peanuts. The results demonstrate that IgE reactivity and thermal and proteolytic stability are reinforced in nAra h 8 after roasting, most likely due to Maillard reactions, lipid oxidations, and lipophilic associations. These aspects must be considered when estimating the allergenicity of Bet v 1-homologous proteins.
DOI: 10.1515/hsz-2013-0206 PMID: 24057594 [Indexed for MEDLINE]
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