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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 #160268
Title: Determining the digestibility of the major allergens from differently processed peanuts.

Author
item Maleki, Soheila
item LEWENSON, CRYSTAL - MIAMI DADE UNIV.
item YAMAKI, K - National Agricultural Research Center - Japan
item Galeano, Marie
item Champagne, Elaine
item SHINOHARA, K - National Food Research Institute - Japan

Submitted to: United States Japan Natural Resources Protein Panel
Publication Type: Proceedings
Publication Acceptance Date: 5/25/2003
Publication Date: 8/30/2003
Citation: Maleki, S.J., Champagne, E.T., Galeano, M.J., Shinohara, K., Yamaki, K., Lewenson, C. 2003. Determining the digestibility of the major allergens from differently processed peanuts. United States Japan Natural Resources Protein Panel. 321-328.

Interpretive Summary: Peanut allergies are on the rise, often severe, and rarely outgrown. Approximately 1% of the American population suffers from peanut allergy. Previously, our laboratory has shown that certain processing methods, such as roasting, can increase the allergenic properties of peanuts. To understand the mechanisms involved in this enhancement, we chose to explore some of the known properties of allergens. One of the classic properties of food allergens is that they are resistant to digestion with digestive enzymes. This makes it possible for large, undigested fragments, to become absorbed into the blood stream where they are more likely to cause an allergic reaction. Therefore, we wanted to determine if the digestibility of peanut allergens are affected by roasting. Based on previous work in a model system, we believe that the two major allergens, Ara h 1 and Ara h 2 from roasted peanuts, would be more resistant to digestion than the same allergens purified from raw peanuts. Therefore, purified allergens from raw, light roast (LR) and dark roast (DR) peanuts, were subject to digestion with two digestive enzymes, pepsin and trypsin. Following empirical determination of assay conditions, we found that both Ara h 1 and Ara h 2, purified from roasted peanuts, were more resistant to digestive enzymes than their raw counterparts. Also, we determined that Ara h 2 is slightly more resistant to trypsin digestion than Ara h 1, whereas, it is approximately 200 fold more resistant to pepsin digestion than Ara h 1. Our studies indicate that the digestibility, and therefore, the allergenic properties of the major allergens, can be altered as a result of processing.

Technical Abstract: Peanut allergies are on the rise, often severe, and rarely outgrown. Approximately 1% of the American population suffers from peanut allergy. Previously, our laboratory has shown that certain processing methods, such as roasting, can increase the allergenic properties of peanuts. To understand the mechanisms involved in this enhancement, we chose to explore some of the known properties of allergens. One of the classic properties of food allergens is that they are resistant to digestion with digestive enzymes. This makes it possible for large, undigested fragments, to become absorbed into the blood stream where they are more likely to cause an allergic reaction. Therefore, we wanted to determine if the digestibility of peanut allergens are affected by roasting. Based on previous work in a model system, we believe that the two major allergens, Ara h 1 and Ara h 2 from roasted peanuts, would be more resistant to digestion than the same allergens purified from raw peanuts. Therefore, purified allergens from raw, light roast (LR) and dark roast (DR) peanuts, were subject to digestion with two digestive enzymes, pepsin and trypsin. Following empirical determination of assay conditions, we found that both Ara h 1 and Ara h 2, purified from roasted peanuts, were more resistant to digestive enzymes than their raw counterparts. Also, we determined that Ara h 2 is slightly more resistant to trypsin digestion than Ara h 1, whereas, it is approximately 200 fold more resistant to pepsin digestion than Ara h 1. Our studies indicate that the digestibility, and therefore, the allergenic properties of the major allergens, can be altered as a result of processing.