Related resources
Full-text held externally
- PMID: 26471647
- UKPMCID: 26471647
- DOI: 10.1016/j.foodchem.2015.08.119
Search for item elsewhere
University researcher(s)
Academic department(s)
Insoluble and soluble roasted walnut proteins retain antibody reactivity.
Downs, Melanie L; Simpson, Angela; Custovic, Adnan; Semic-Jusufagic, Aida; Bartra, Joan; Fernandez-Rivas, Montserrat; Taylor, Steve L; Baumert, Joseph L; Mills, E N Clare
Food chemistry. 2016;194:1013-21.
Access to files
Full-text and supplementary files are not available from Manchester eScholar. Full-text is available externally using the following links:
Full-text held externally
- PMID: 26471647
- UKPMCID: 26471647
- DOI: 10.1016/j.foodchem.2015.08.119
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.