Mass Spectrum Study about the Effect of Roast on the Potential Allergenicity of Peanut Allergen Ara h 1

Abstract

Abstract: Peanut allergy is one of the most common lethal allergic reactions worldwide. Roast is a common thermal processing method for peanuts. Total protein was extracted from raw and roasted peanuts by chaotropic salt solution, and submitted to polyacrylamide gel electrophoresis for comparation. The band of dominant peanut allergen Ara h 1 was analyzed by mass spectrometry. Results showed that the roasted peanut protein sample showed macromolecular polymer and diffused protein bands. This indicated that protein could aggregate or possibly degrade during roasting. In raw peanut sample, 70 peptides were found with a coverage rate of 79.2%. After roasting, 40 of those peptides could not be detected, but one another peptide was acquired, while the coverage reduced to 43.9%. These peptides involved 18 linear IgE-binding epitopes of Ara h 1, and during the preparation of mass spectrum technology, 16 epitopes were destroyed by enzymatic hydrolysis in raw peanut, but only 12 were destroyed in roast peanut. Roast could reduce the destruction of linear IgE-binding epitopes by changing the spatial structure of proteins, masking some enzyme cutting sites. This might be the reason contributed to the higher allergenicity of Ara h 1 in roasted peanut but not in raw peanut.

Key words: roast, Ara h 1, mass spectrum, structure, allergenicity

References

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