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Abstract
The accidental uptake of peanuts can cause severe health reactions in allergic individuals. Reliable determination of traces of peanuts in food products is required to support correct labelling and therefore minimise consumers’ risk. The immunoanalytical detectability of potentially allergenic peanut proteins is dependent on previous heat treatment, the extraction capacity of the applied buffer and the specificity of the antibody. In this study a lateral flow device (LFD) for the detection of peanut protein was developed and the capacity of 30 different buffers to extract proteins from mildly and strongly roasted peanut samples as well as their influence on the test strip performance were investigated. Most of the tested buffers showed good extraction capacity for putative Ara h 1 from mildly roasted peanuts. Protein extraction from dark-roasted samples required denaturing additives, which were proven to be incompatible with LFD performance. High-pH buffers increased the protein yield but inhibited signal generation on the test strip. Overall, the best results were achieved using neutral phosphate buffers but equal detectability of differently altered proteins due to food processing cannot be assured yet for immunoanalytical methods.
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Acknowledgements
The authors would like to thank Karin Hoffmann-Sommergruber, Department of Pathophysiology and Allergy Research, Medical University of Vienna, Austria, for testing the antibodies for their allergen specificities. They also thank Dr Marcela Herman, Medical University Vienna, Max Perutz Laboratories, for the immunisations and housing of the rabbits. All the animal work was done according to Austrian Federal Law and Austrian Animal Protection Law. This work was carried out within the CD Laboratory for Rapid Test Systems for Allergenic Food Contaminants, financed by the Christian Doppler Research Association and Romer Labs.
