Purification, Identification and Characterization of Brazil Nut Allergen Ber e 1

The allergen protein Ber e 1 was purified from Brazil nuts by crushing, defatting, extraction, and anion exchange chromatography, and identified by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), liquid chromatography-tandem mass spectrometry (LC-MS/MS) and Western blot, and its secondary and tertiary structures were characterized by circular dichroism (CD) and UV spectroscopy. The results showed that the purified target protein was identified as Ber e 1, and the yield of Ber e 1 was more than 20 mg per round, and its purity was higher than 95%. The purified allergen showed undamaged secondary or tertiary structures, and could be recognized by the serum of allergic patients. This purification method is simple and efficient with low instrument requirements, which can provide a basis for Ber e 1 research.