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MOESM1 of Protease resistance of food proteins: a mixed picture for predicting allergenicity but a useful tool for assessing exposure

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posted on 2018-08-10, 05:00 authored by Jaap Akkerdaas, Muriel Totis, Brian Barnett, Erin Bell, Tom Davis, Thomas Edrington, Kevin Glenn, Gerson Graser, Rod Herman, Andre Knulst, Gregory Ladics, Scott McClain, Lars Poulsen, Rakesh Ranjan, Jean-Baptiste Rascle, Hector Serrano, Dave Speijer, Rong Wang, Lucilia Pereira Mouriès, Annabelle Capt, Ronald Ree
Additional file 1: Fig. E1. Selected SDS-PAGE and immunoblot samples are shown for both albumins, Ara h 2 and pea albumin PA2. Panel a illustrates that pea albumin PA2 is truncated at low PPR but truncated molecules are still detected on immunoblot. Panel b shows gastric digestion of Ara h 2 at low pH and high PPR. Under these conditions the upper band is quite stable but the lower band is truncated. Truncated molecules are not recognized on immunoblot. Panel c and d illustrates that Ara h 2 (panel c) and pea albumin PA2 (panel d) behave differently when gastric digestion at pH 1.2 and pH 2.5 are compared. Ara h 2 is quite stable under both conditions, but if anything slightly more susceptible to digestion at pH 2.5. For pea albumin PA2 this is the other way around. It is clearly more resistant to digestion at pH 2.5 than pH 1.2.

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Health and Environmental Sciences Institute (HESI)

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