TITLE:
Peanut Allergens Attached with p-Aminobenzamidine Are More Resistant to Digestion than Native Allergens
AUTHORS:
Si-Yin Chung, Shawndrika Reed, Dunhua Zhang
KEYWORDS:
p-Aminobenzamidine, Peanut Allergens, Ara h 1 and Ara h 2, Resistance to Digestion
JOURNAL NAME:
Food and Nutrition Sciences,
Vol.7 No.14,
December
5,
2016
ABSTRACT: Despite being known as resistant proteins, peanut allergens (Ara h 1 and Ara h 2)
can be digested and cause allergic reactions. Making the allergens more resistant to
digestion may aid in non-absorption and excretion of the allergens. Our objectives
were to make Ara h 1 and Ara h 2 more resistant to digestion and test them in a
model system using trypsin as the digestive enzyme. The resistant allergens were
prepared by covalently attaching p-aminobenzamidine (pABA), a protease inhibitor,
to peanut allergens in an extract or on a PVDF membrane using glutaraldehyde, and
were then tested for resistance to trypsin digestion. SDS-PAGE and Western blot
were performed to determine the allergenic capacity of the modified allergens. A
control was prepared using glycine instead. Results showed that Ara h 2, when covalently
attached with pABA, was more resistant to trypin digestion than the native allergen.
Similarly, Ara h 1, prepared on a PVDF membrane and treated with pABA,
displayed a resistance to trypsin digestion. Treatment of the allergens with glycine (a
control) instead of pABA showed that the modified allergens were as digestible as
native allergens. Blot assays showed that the pABA-treated allergens exhibited a lower
allergenic capacity than native allergens. It was concluded that pABA, when attached
to peanut allergen Ara h 1 or Ara h 2, inhibited digestion of the allergen by
trypsin and reduced their allergenic capacity as well.