Identification and Characterization of Ana o 3 Modifications on Arginine Residue-111 in Heated Cashew Nuts
Mattison, C. P., Grimm, C. C., Li, Y., Chial, H. J., McCaslin, D. R., Chung, S. Y., … & Wasserman, R. L.
Raw and roasted cashew nut extracts were evaluated for protein modifications by mass-spectrometry. Independent modifications on the Arg-111 residue of Ana o 3 were observed in roasted but not raw cashew nuts. The mass changes of 72.0064 or 53.9529 Da are consistent with formation of carboxyethyl and hydroimidazolone modifications at the Arg-111 residue. These same modifications were observed in Ana o 3 purified from roasted but not raw cashew nuts, albeit at a relatively low occurrence. Circular dichroism indicated that Ana o 3 purified from raw and roasted cashew nuts had similar secondary structure, and dynamic light scattering analysis indicated there was no observable difference in particle size. The stability of Ana o 3 purified from raw and roasted cashew nuts to trypsin was similar in the absence of or following treatment with a reducing agent. Only minor differences in IgE binding to Ana o 3 were observed by ELISA among a cohort of cashew allergic patient sera.
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