Skip to main content
ARS Home » Southeast Area » New Orleans, Louisiana » Southern Regional Research Center » Food Processing and Sensory Quality Research » Research » Publications at this Location » Publication #303498
Title: Decreased immunoglobulin E (IgE) binding to cashew allergens following sodium sulfite treatment and heating

Author
item Mattison, Chris
item Desormeaux, Wendy
item WASSERMAN, RICHARD - Allergy/immunology Research Center Of North Texas
item Yoshioka-Tarver, Megumi
item Condon, Brian
item Grimm, Casey

Submitted to: Journal of Agricultural and Food Chemistry
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 6/13/2014
Publication Date: 6/13/2014
Citation: Mattison, C.P., Desormeaux, W.A., Wasserman, R., Yoshioka-Tarver, M., Condon, B.D., Grimm, C.C. 2014. Decreased immunoglobulin E (IgE) binding to cashew allergens following sodium sulfite treatment and heating. Journal of Agricultural and Food Chemistry. 62:6746-6755.

Interpretive Summary: Cashew nut and other nut allergies can result in serious and sometimes life threatening reactions. These adverse reactions are mediated by immunoglobulin E binding (IgE) to allergens. Methods that alter the shape of nut allergens can reduce immunoglobulin E binding and lessen the likelihood of serious reactions. We demonstrated that the generally recognized as safe (GRAS) compound sodium sulfite can effectively disrupt the structure of some cashew allergens. We determined that addition of sodium sulfite and heating of cashew extracts markedly reduced IgE binding from cashew allergic patients. Our results indicate that incorporation of sodium sulfite, or other food grade reagents with similar characteristics, may be useful in processing methods to reduce or eliminate IgE binding to food allergens. Continued research using clinical studies in this area are needed to determine if the methods developed here could result in processing techniques that can reduce or eliminate the ability of tree nuts and peanuts to cause allergy.

Technical Abstract: Cashew nut and other nut allergies can result in serious and sometimes life threatening reactions. Linear and conformational epitopes within food allergens are important for immunoglobulin E binding. Methods that disrupt allergen structure can reduce immunoglobulin E binding and lessen the likelihood of food allergy reactions. Previous structural and biochemical data have indicated that 2S albumins from tree nuts and peanuts are potent allergens, and their structures are sensitive to strong reducing agents such as dithiothreitol. We demonstrated that the generally recognized as safe (GRAS) compound sodium sulfite can effectively disrupt the structure of the cashew 2S albumin, Ana o 3, whose structure is dependent upon disulfide bonds. We also showed that sulfite is effective at disrupting the disulfide bond within the cashew legumin, Ana o 2. Using immunoblotting and ELISA, we demonstrated that binding of cashew proteins by rabbit IgG or IgE from cashew allergic patients was markedly reduced following treatment with sodium sulfite. Our results indicate that incorporation of sodium sulfite, or other food grade reagents with similar redox potential, may be useful processing methods to reduce or eliminate IgE binding to food allergens.