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Updated: Mar 31, 2026
Protein Membrane Overlay Assay: A Protocol to Test Interaction Between Soluble and Insoluble Proteins in vitro
Published on: August 14, 2011
Insoluble and soluble roasted walnut proteins retain antibody reactivity
Melanie L Downs1, Angela Simpson2, Adnan Custovic2
1Food Allergy Research and Resource Program, Department of Food Science and Technology, Food Innovation Center, 1901 North 21st Street, University of Nebraska-Lincoln, Lincoln, NE 68588-6205, USA; Institute of Inflammation and Repair, Manchester Academic Health Sciences Centre and Manchester Institute of Biotechnology, University of Manchester, 131 Princess Street, Manchester M1 7DN, UK.
Abstract:
Thermal processing techniques commonly used during food production have the potential to impact food allergens by inducing physical and/or chemical changes to the proteins. English walnuts (Juglans regia) are among the most commonly allergenic tree nuts, but little information is available regarding how walnut allergens respond to thermal processing. This study evaluated the effects of dry roasting (132 or 180°C for 5, 10, or 20min) on the solubility and immunoreactivity of walnut proteins. A dramatic decrease in walnut protein solubility was observed following dry roasting at 180°C for 20min. However, both the soluble and insoluble protein fractions from roasted walnuts maintained substantial amounts of IgG immunoreactivity (using anti-raw and anti-roasted walnut antisera), with similar patterns of reactivity observed for human IgE from walnut-allergic individuals. Thus, walnut proteins are relatively stable under certain thermal processing conditions, and IgE reactivity remains present even when insoluble aggregates are formed.
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