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ARS Home » Southeast Area » New Orleans, Louisiana » Southern Regional Research Center » Food Processing and Sensory Quality Research » Research » Publications at this Location » Publication #308745
Title: Making peanut allergens indigestible: a model system for reducing or preventing an allergic reaction

Author
item Chung, Si Yin
item Reed, Shawndrika

Submitted to: Meeting Abstract
Publication Type: Abstract Only
Publication Acceptance Date: 3/31/2015
Publication Date: 4/27/2015
Citation: Chung, S., Reed, S.S. 2015. Making peanut allergens indigestible: a model system for reducing or preventing an allergic reaction. Meeting Abstract. 135(2):AB33-103.

Interpretive Summary:

Technical Abstract: Peanut allergens are not totally resistant to digestion as previously known. Creating peanut allergen conjugates that are more resistant to digestion may prevent absorption of the allergens into the bloodstream, and thereby, an allergic reaction. Peanut allergen conjugates were prepared by covalently attaching a protease inhibitor, p-aminobenzamidine (pABA), to peanut allergens through activation of a mixture of raw peanut extract and pABA with glutaraldehyde. After dialysis, the pABA-peanut allergen conjugates were subjected to tests for digestion and inhibition of protease. In the model test system, trypsin was used as the protease to digest the native peanut allergens in the presence and absence of the conjugates. Digestion profiles and released free amino groups were determined by SDS-PAGE and trinitrobenzenesulfonic acid (TNBS). IgE bindings of the conjugates and native allergens were determined in ELISA. SDS-PAGE showed that the pABA-peanut allergen conjugate was resistant to digestion, whereas, native peanut allergens (Ara h 1 and Ara h 2) were completely digested into peptide fragments by trypsin in 20 minutes. Digestion of native allergens was inhibited when the conjugate was present. TNBS assay showed that the degree of trypsin inhibition was dependent on the conjugate concentration used. IgE antibodies were not inhibited by the conjugate in ELISA. Trypsin was inhibited by the pABA-peanut allergen conjugate. The conjugate was not recognized by IgE antibodies in ELISA. The conjugate can serve as a model system for making peanut allergens indigestible and feasible to be excreted without causing an allergic reaction.