Insoluble and soluble roasted walnut proteins retain antibody reactivity
File(s)Figures_Food Chemistry.pptx (9.17 MB)
Supporting information
Author(s)
Type
Journal Article
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 20 min) on the solubility and immunoreactivity of walnut proteins. A dramatic decrease in walnut protein solubility was observed following dry roasting at 180 °C for 20 min. 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.
Date Issued
2015-08-29
Date Acceptance
2015-08-27
Citation
Food Chemistry, 2015, 194, pp.1013-1021
ISSN
1873-7072
Publisher
Elsevier
Start Page
1013
End Page
1021
Journal / Book Title
Food Chemistry
Volume
194
Copyright Statement
© 2015, Elsevier. Licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International http://creativecommons.org/licenses/by-nc-nd/4.0/
Identifier
PII: S0308-8146(15)01328-X
Subjects
Food allergy
Thermal processing
Tree nut
Walnut
Allergens
Food Hypersensitivity
Immunoglobulin E
Juglans
Nuts
Plant Proteins
Food Science
MD Multidisciplinary
Publication Status
Published