MOESM2 of Protease resistance of food proteins: a mixed picture for predicting allergenicity but a useful tool for assessing exposure

Additional file 2: Fig. E2. Selected SDS-PAGE and immunoblot samples are shown for both tropomyosins, from shrimp (Pen a 1) and pig. At pH 1.2 and PPR 0.1 shrimp tropomyosin is fully resistant to pepsin digestion up to 1 h (panel a). At pH 2.5 some truncation is observed, with truncated molecules still being recognized on immunoblot (panel b). For pig tropomyosin, the upper band is not anymore recognized on immunoblot after 60 min of pepsinolysis at pH 1.2 and PPR 0.1 (panel c). Panel d illustrates the susceptibility of shrimp tropomyosin to duodenal digestion after a preceding gastric digestion at pH 1.2/PPR 10: truncated molecules are still detected by rabbit antibodies.