Abstract
It has been suggested that the boiling or frying of peanuts leads to less allergenic products than roasting. Here, we have compared the digestibility of the major peanut allergens in the context of peanuts subjected to boiling, frying or roasting and in purified form. The soluble peanut extracts and the purified allergens were digested with either trypsin or pepsin and analyzed by gel electrophoresis and western blot. T-cell proliferation was measured for the purified allergens. In most cases, boiled and raw peanut proteins were similarly digestible, but the Ara h 1 protein in the boiled extracts was more resistant to digestion. Most proteins from fried and roasted peanuts were more resistant to digestion than in raw and boiled samples, and more IgE binding fragments survived digestion. High-molecular-weight fragments of Ara h1 were resistant to digestion in fried and roasted samples. Ara h 1 and Ara h 2 purified from roasted peanuts were the most resistant to digestion, but differed in their ability to stimulate T-cells. The differences in digestibility and IgE binding properties of the major allergens in roasted, fried and boiled peanuts may not explain the difference between the prevalence of peanut allergy in different countries that consume peanut following these varied processing methods.
Highlights
5% of adults and 8% of children have a food allergy, and there is evidence for an increasing prevalence
In order to determine if diverse processing methods can alter the digestibility of thermally processed peanut proteins, soluble extracts were made from raw, roasted, boiled and fried peanut extracts, which were subjected to digestion with trypsin (Figure 1) several times prior to SDS-PAGE analysis (Figure 1A)
An anti-Ara h 1 western blot on the same extracts shows that the Ara h 1 in the boiled sample is more resistant to digestion than in the raw sample (Figure 1B)
Summary
5% of adults and 8% of children have a food allergy, and there is evidence for an increasing prevalence. We addressed the effects of thermal processing on some of the allergenic properties of peanut proteins [11,12]. Thermal processing, such as roasting, curing and various types of cooking, can cause multiple non-enzymatic, biochemical reactions to occur in food [13]. Some of the roasting-induced biophysical mechanisms for enhanced allergenic properties of the major peanut allergens were previously explored in a simulated roasting model [11] Both Ara h 1 and Ara h 2 bound higher levels of IgE, and the increase in IgE binding was correlated with increased carboxymethyllysine (CML) modifications on the surface of the protein [25]. The effects of different thermal processes on Ara h 1 and Ara h 2 were assessed for digestibility with trypsin and pepsin, IgE binding and stimulation of T-cells from peanut allergic individuals
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