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Gewählte Publikation:

Marzban, G; Herndl, A; Pietrozotto, S; Banerjee, S; Obinger, C; Maghuly, F; Hahn, R; Boscia, D; Katinger, H; Laimer, M.
(2009): Conformational changes of Mal d 2, a thaumatin-like apple allergen, induced by food processing
FOOD CHEM. 2009; 112(4): 803-811. FullText FullText_BOKU

Abstract:
Mal d 2, a thaumatin-like protein from apple was previously described to react to almost 75% of the apple allergic patient sera. Based on the molecular structure of this protein, the present study focused on the conformational stability of Mal d 2 in relation to in vitro IgE-binding under different physico-chemical conditions and proteolysis. The structural integrity of Mal d 2 was monitored using SDS-PAGE, Western blotting using polyclonal antibodies and human sera. fluorescence spectrometry and circular dichroism. Results confirmed the stability of Mal d 2. However, Mal d 2 was reactive to human serum IgEs mainly after reduction of disulphide bridges fixing the alpha-helical domain II. Contrary to previous assumptions, the current findings suggest that the allergenic epitopes of Mal d 2 are hidden inside the protein Structure and none of the rigorous conditions applied in industrial juice processing or digestive proteolysis enhance or reduce the binding to IgE molecules. (c) 2008 Elsevier Ltd. All rights reserved.
Autor*innen der BOKU Wien:
Hahn Rainer
Katinger Hermann
Laimer Margit
Maghuly Fatemeh
Marzban Gorji
Obinger Christian

Find related publications in this database (Keywords)
Fruit processing
Apple allergen
IgE-reactivity
Allergen stability


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