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, Sue L. Hefle, Steve L. Taylor, Govardus A.H. De Jong

Research output: Contribution to journalArticle

84 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)1711-1721
Number of pages11
JournalMolecular Nutrition and Food Research
Volume54
Issue number12
DOIs
StatePublished - Dec 1 2010

Fingerprint

allergens
in vitro studies
peanuts
Digestion
Pepsin A
digestion
pepsin
peptides
Peptides
Allergens
Trypsin
trypsin
Polyacrylamide Gel Electrophoresis
In Vitro Techniques
Arachis hypogaea Ara h 1 protein
sulfides
Disulfides
proteolysis
Proteolysis
Stomach

Keywords

  • Allergen
  • Digestion
  • Peanut
  • Pepsin
  • Trypsin

ASJC Scopus subject areas

  • Biotechnology
  • Food Science

Cite this

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. / Koppelman, Stef J.; Hefle, Sue L.; Taylor, Steve L.; De Jong, Govardus A.H.

In: Molecular Nutrition and Food Research, Vol. 54, No. 12, 01.12.2010, p. 1711-1721.

Research output: Contribution to journalArticle

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AB - 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.

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