Digestion of peanut allergens Ara h 1, Ara h 2, Ara h 3, and Ara h 6: a comparative in vitro study and partial characterization of digestion-resistant peptides - PubMed (original) (raw)

Comparative Study

. 2010 Dec;54(12):1711-21.

doi: 10.1002/mnfr.201000011.

Affiliations

• PMID: 20603832
• DOI: 10.1002/mnfr.201000011

Comparative Study

Digestion of peanut allergens Ara h 1, Ara h 2, Ara h 3, and Ara h 6: a comparative in vitro study and partial characterization of digestion-resistant peptides

Stef J Koppelman et al. Mol Nutr Food Res. 2010 Dec.

Abstract

Scope: There are differences in stability to pepsin between the major allergens in peanut; however, data are from different reports using different digestion models. This study provides a comprehensive comparison of the digestibility of the major peanut allergens.

Methods and results: Peanut allergens Ara h 1, Ara h 2, Ara h 3 and Ara h 6 were incubated with pepsin to mimic the effect of gastric digestion. Samples were analyzed using SDS-PAGE. To further investigate resistance to digestion, Ara h 2 was additionally subjected to digestion with trypsin and residual peptides were characterized. Ara h 1 and Ara h 3 were rapidly hydrolyzed by pepsin. On the contrary, Ara h 2 and Ara h 6 were resistant to pepsin digestion, even at very high concentrations of pepsin. In fact, limited proteolysis could only be demonstrated by SDS-PAGE performed under reducing conditions, indicating an important role for the disulfide bridges in maintaining the quaternary structure of Ara h 2 and Ara h 6. Trypsin digestion of Ara h 2 similarly resulted in large residual peptides and these were identified.

Conclusion: Ara h 2 and Ara h 6 are considerably more stable towards digestion than Ara h 1 and Ara h 3.

Copyright © 2010 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

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