The major 2S albumin allergen from Brazil nuts, Ber e 1, was subjected to gastrointestinal digestion using a physiologically relevantin vitro model sys-tem either before or after heating (100 C for 20 min). Whilst the albumin was cleaved into peptides, these were held together in a much larger struc-ture even when digested by using a simulated phase 1 (gastric) followed by a phase 2 (duodenal) digestion system. Neither prior heating of Ber e 1 nor the presence of the physiological surfactant phosphatidylcholine affected the pattern of proteolysis. After 2 h of gastric digestion, 25% of the allergen remained intact, 50% corresponded to a large fragment ofMr 6400, and.
