Email updates

Keep up to date with the latest news and content from Clinical and Translational Allergy and BioMed Central.

This article is part of the supplement: Food Allergy and Anaphylaxis Meeting 2011

Open Access Open Badges Oral presentation

Roasting or heating increases elicitation capacity of peanut allergens but does not affect their sensitisation potential in a brown Norway rat model for food allergy

Stine Kroghsbo1*, Neil Rigby2, Yvonne Vissers3, Clare Mills2 and Charlotte Madsen1

  • * Corresponding author: Stine Kroghsbo

Author Affiliations

1 DTU National Food Institute, Soborg, Denmark

2 Institute of Food Research, Norwich, UK

3 Wageningen University, Wageningen, Denmark

For all author emails, please log on.

Clinical and Translational Allergy 2011, 1(Suppl 1):O20  doi:10.1186/2045-7022-1-S1-O20

The electronic version of this article is the complete one and can be found online at:

Published:12 August 2011

© 2011 Kroghsbo et al; licensee BioMed Central Ltd.

This is an open access article distributed under the terms of the Creative Commons Attribution License (, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


Allergenic potential of processed food allergens has primarily been studied by their IgE-binding capacity (elicitation). Roasting of peanuts has been shown to increase IgE-binding capacity. In this study we examined whether processing of whole peanuts or of the major peanut allergen Ara h 1 influenced the sensitisation potential.


Brown Norway rats were either dosed orally by gavage each day for 42 days with finely ground whole peanut products (blanched or roasted peanuts or peanut butter) mixed with water [~2 mg Ara h 1/rat/day] or immunised i.p. three times with 200 μg of native, heated or heat glycated Ara h 1. Sera obtained at sacrifice were analysed for specific IgG and IgE by ELISA and for biological functionality of IgE by rat basophilic leukaemia (RBL) assay.


Processing was found to decrease solubility and thus extractability of Ara h 1 from peanut products. Aggregation state and secondary structure changes induced by heating of purified Ara h 1 were identical to those observed when Ara h 1 was heated in the presence of glucose. Although a significant anti-Ara h 1 IgE response was only found when dosing rats with roasted peanuts, examination of functional specific IgE by RBL assay showed that processing of peanuts did not influence sensitisation potential. However, extract from roasted peanuts was found to be a superior elicitor compared to extract from blanched peanuts irrespective of the peanut product used for sensitisation. Processing of purified native Ara h 1 did not influence the sensitisation capacity. Nonetheless, ELISA results indicated that new epitopes are formed or disclosed by heating of Ara h 1. Furthermore, IgG1-binding capacity was found to reflect whether rats were sensitised to native or processed Ara h 1 or dosed with blanched or roasted peanut products.


Roasted peanuts, either as such or as peanut butter, do not have a higher sensitisation capacity than blanched peanuts. This is supported by the finding that process-modified Ara h 1 has a similar sensitisation capacity as native Ara h 1. Yet, our results show that roasting increases elicitation capacity.