The major peanut allergen, Ara h 2, functions as a trypsin inhibitor, and roasting enhances this function
- PMID: 12847498
- DOI: 10.1067/mai.2003.1551
The major peanut allergen, Ara h 2, functions as a trypsin inhibitor, and roasting enhances this function
Abstract
Background: The widespread use of peanut products, the severity of the symptoms, and its persistence in afflicted individuals has made peanut allergy a major health concern in western countries such as the United States, United Kingdom, and Canada. In a previous study, the authors showed that the allergenic properties of peanut proteins are enhanced as a result of thermal processing.
Objective: The purpose of this investigation was to determine whether any specific functions are associated with the major peanut allergen, Ara h 2, and whether the functionality of this protein is influenced by processing. An assay was developed and used to assess structure/function changes in Ara h 2 induced by roasting and the effect of these alterations on the allergenic properties of this major peanut allergen.
Methods: A protein domain homology search was used to determine possible functions for Ara h 2. One of the putative functions (protease inhibition) was tested by means of appropriate enzyme assays and protein gel electrophoresis. Circular dichroism was used to compare the structural properties of Ara h 2 purified from raw and roasted peanuts.
Results: Ara h 2 purified from peanuts is homologous to and functions as a trypsin inhibitor. Roasting caused a 3.6-fold increase in trypsin inhibitory activity. Functional and structural comparison of the Ara h 2 purified from roasted peanuts to native and reduced Ara h 2 from raw peanuts revealed that the roasted Ara h 2 mimics the behavior of native Ara h 2 in a partially reduced form.
Conclusions: The data indicate that thermal processing might play an important role in enhancing the allergenic properties of peanuts. Not only has it previously been shown to affect the structural and allergic properties of peanut proteins but also, for the first time, the functional characteristics of an allergen. These structural and functional alterations are likely to influence the allergenicity of peanuts.
Similar articles
-
Influence of thermal processing on the allergenicity of peanut proteins.J Agric Food Chem. 2005 Jun 1;53(11):4547-53. doi: 10.1021/jf050091p. J Agric Food Chem. 2005. PMID: 15913323
-
Structure and stability of 2S albumin-type peanut allergens: implications for the severity of peanut allergic reactions.Biochem J. 2006 May 1;395(3):463-72. doi: 10.1042/BJ20051728. Biochem J. 2006. PMID: 16372900 Free PMC article.
-
Thermal processing effects on peanut allergen Ara h 2 allergenicity in mice and its antigenic epitope structure.Food Chem. 2016 Dec 1;212:657-62. doi: 10.1016/j.foodchem.2016.06.036. Epub 2016 Jun 14. Food Chem. 2016. PMID: 27374581
-
Proteomic screening points to the potential importance of Ara h 3 basic subunit in allergenicity of peanut.Inflamm Allergy Drug Targets. 2008 Sep;7(3):163-6. doi: 10.2174/187152808785748182. Inflamm Allergy Drug Targets. 2008. PMID: 18782022 Review.
-
[Progress of researches on the allergens Ara h 1, Ara h 2 and Ara h 3 from peanut].Sheng Wu Yi Xue Gong Cheng Xue Za Zhi. 2010 Dec;27(6):1401-5. Sheng Wu Yi Xue Gong Cheng Xue Za Zhi. 2010. PMID: 21375004 Review. Chinese.
Cited by
-
Heating Affects Structure, Enterocyte Adsorption and Signalling, As Well as Immunogenicity of the Peanut Allergen Ara h 2.Open Allergy J. 2011 Dec 9;4:24-34. doi: 10.2174/1874838401104010024. Open Allergy J. 2011. PMID: 22318448 Free PMC article.
-
Assessment of the sensitizing potential of processed peanut proteins in Brown Norway rats: roasting does not enhance allergenicity.PLoS One. 2014 May 7;9(5):e96475. doi: 10.1371/journal.pone.0096475. eCollection 2014. PLoS One. 2014. PMID: 24805813 Free PMC article.
-
Conformational IgE epitopes of peanut allergens Ara h 2 and Ara h 6.Clin Exp Allergy. 2016 Aug;46(8):1120-1128. doi: 10.1111/cea.12764. Epub 2016 Jun 27. Clin Exp Allergy. 2016. PMID: 27238146 Free PMC article.
-
Interaction of Monocyte-Derived Dendritic Cells with Ara h 2 from Raw and Roasted Peanuts.Foods. 2020 Jul 2;9(7):863. doi: 10.3390/foods9070863. Foods. 2020. PMID: 32630617 Free PMC article.
-
Antioxidant Properties of Protein-Rich Plant Foods in Gastrointestinal Digestion-Peanuts as Our Antioxidant Friend or Foe in Allergies.Antioxidants (Basel). 2023 Apr 5;12(4):886. doi: 10.3390/antiox12040886. Antioxidants (Basel). 2023. PMID: 37107261 Free PMC article. Review.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources