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ARS Home » Southeast Area » New Orleans, Louisiana » Southern Regional Research Center » Food Processing and Sensory Quality Research » Research » Publications at this Location » Publication #141052
Title: THE MAJOR PEANUT ALLERGEN, ARA H 2, FUNCTIONS AS A TRYPSIN INHIBITOR AND ROASTING ENHANCES THIS FUNCTION

Author
item Maleki, Soheila
item VIQUEZ, OLGA - ALABAMA A&M UNIV
item Jacks, Thomas
item DODO, HORTENSE - ALABAMA A&M UNIV
item Champagne, Elaine
item Chung, Si Yin
item LANDRY, SAMUEL - TULANE UNIV

Submitted to: Journal of Allergy Clinical Immunology
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 11/20/2003
Publication Date: 12/14/2003
Citation: Maleki, S.J., Viquez, O., Jacks, T.J., Dodo, H., Champagne, E.T., Chung, S., Landry, S. 2003. The major peanut allergen, ara h 2, functions as a trypsin inhibitor and roasting enhances this function. Journal of Allergy Clinical Immunology. 112(1):190-195.

Interpretive Summary: 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 U.S., U.K. and Canada. In a previous study, the authors showed that allergenic properties of peanut proteins are enhanced due to thermal processing. The objective of this study was to determine if any specific functions were associated with the major peanut allergen, Ara h 2 and if the functionality of this protein is influenced by processing. Towards this aim, 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 allergenic properties of this major peanut allergen. Ara h 2 purified from peanuts is homologous to and functions as a trypsin inhibitor. Roasting caused a 3.5 fold increase in trypsin inhibitory activity. In conclusion the data indicate that thermal processing may play an important role in enhancing the allergenic properties of peanuts. Not only has it been shown to affect the structural and allergic properties of peanut proteins, but also for the first time, the functional characteristics of an allergen that can directly influence allergenicity. This research will benefit the Peanut Industry and people with peanut allergies.

Technical Abstract: 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 U.S., U.K. and Canada. In a previous study, the authors showed that allergenic properties of peanut proteins are enhanced due to thermal processing. The objective of this study was to determine if any specific functions were associated with the major peanut allergen, Ara h 2 and if the functionality of this protein is influenced by processing. Towards this aim, 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 allergenic properties of this major peanut allergen. Ara h 2 purified from peanuts is similar to and functions as a digestive enzyme inhibitor. Roasting caused Ara h 2 to become a stronger digestive enzyme inhibitor and therefore more resistant to digestion. Since resistance to digestion is a classic characteristic of allergens, an increase in this property enhances allergenicity. In conclusion, the data indicates that roasting may play an important role in enhancing the allergenic properties of peanuts. Not only has it been shown to affect the structural and allertic properties of peanut proteins, but also for the first time, the functional characteristics of an allergen that can directly influence allergenicity.