Effect of heat treatment on the conformational stability of intact and cleaved forms ofthe peanut allergen Ara h 6 in relation to its IgE-binding potency.

Autor: de Jongh HHJ; ProtIn Consultancy, Rozenstraat 19E, 3702 VL Zeist, The Netherlands., de Jong GAH; TNO, Utrechtseweg 48, 3704 HE Zeist, The Netherlands., Apostolovic D; Clinical Immunology and Allergy Unit, Department of Medicine Solna, Karolinska Institutet, Solnavägen 1, 171 77 Solna, Sweden., Taylor SL; Food Allergy Research and Resource Program, Department of Food Science & Technology, University of Nebraska, 279 Food Innovation Center, Lincoln, NE 68588-6207, USA., Baumert JL; Food Allergy Research and Resource Program, Department of Food Science & Technology, University of Nebraska, 279 Food Innovation Center, Lincoln, NE 68588-6207, USA., Koppelman SJ; Food Allergy Research and Resource Program, Department of Food Science & Technology, University of Nebraska, 279 Food Innovation Center, Lincoln, NE 68588-6207, USA. Electronic address: farrp@unl.edu.
Jazyk: angličtina
Zdroj: Food chemistry [Food Chem] 2020 Oct 01; Vol. 326, pp. 127027. Date of Electronic Publication: 2020 May 11.
DOI: 10.1016/j.foodchem.2020.127027
Abstrakt: This work reports on theeffect of heat treatment on the protein conformational stabilityof intact and post-translationallycleaved peanut allergen Ara h 6 in relation to IgE-binding. Intact and post-translationallycleaved Ara h 6 are structurally similar and theirstrong resistance to denaturant-inducedunfolding is comparable. Only upon exposure toautoclave conditions the twoforms of Ara h 6 demonstrated susceptibility toirreversible denaturationresulting in a significant decrease in IgE-binding potency. Thisreduction isfor the intact protein more pronounced than for than for the cleaved form. This isattributed to less conformational constrains of the cleaved form comparedtointact, as suggested by the 2-fold lower activation energy for unfoldingfound for the cleavedform. Overall, harsh conditionsare required to denature Ara h 6 and to significantly reduce its IgE-bindingpotency. The cleavedform possesses more resistance to such denaturation than the intactform.
Competing Interests: Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
(Copyright © 2020 Elsevier Ltd. All rights reserved.)
Databáze: MEDLINE
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