The evaluation of antigenic reactivity of peanut proteins treated with non-commercial enzyme preparations of plant origin (Cucurbita ficifolia)

<p class="MsoNormal" style="text-align:justify;text-indent:35.4pt;line-height:200%"><span lang="EN-GB" style="font-family:&#39;times new roman&#39; , serif">Peanut allergies (PA) are
among the most reported and severe kinds of food allergies seen in individuals.
In the past 10 years, the prevalence of peanut allergy has more than doubled in
Western countries. PAs are immunoglobulin E (IgE)-mediated type I hypersensitivity
reactions that can lead to fatal (anaphylactic) reactions.</span></p><p class="MsoNormal" style="text-align:justify;text-indent:35.4pt;line-height:200%"><span lang="EN-GB" style="font-family:&#39;times new roman&#39; , serif">Peanut allergens are
classified as cupin superfamily (vicillin: Ara h 1 and legumin: Ara h 3),
conglutin (2S albumins; Ara h2, Ara h6, Ara h7), profilin (Ara h5),
pathogenesis related class-10 protein (Ara h8), nonspecific lipid-transfer
protein (Ara h9), oleosins (Ara h10 and Ara h11) and defensins (Ara h 12 and
Ara h 13). The “major allergens” identified in peanuts are defined as antigens
that bind large amounts of IgE from allergic patients and have biological
activity. They include thermostable proteins such as Ara h1, Ara h2, and Ara
h3.</span></p><p class="MsoNormal" style="text-align:justify;line-height:200%"><span lang="EN-GB" style="font-family:&#39;times new roman&#39; , serif">           
Currently, the only effective treatment for peanut allergy is the avoidance of
this nut in any form. Avoiding peanuts in the daily diet is difficult owing to
their widespread use in products as an economical protein source. Therefore, it
is necessary to explore strategies to decrease the ability of peanuts to elicit
dangerous allergic responses. For several years, new methods for effectively
reducing the allergenic properties of proteins have been investigated.
Enzymatic hydrolysis is widely used in the food industry and is an efficient
process for disrupting sequential and conformational epitopes.</span></p><p class="MsoNormal" style="text-align:justify;text-indent:35.4pt;line-height:200%"><span lang="EN-GB" style="font-family:&#39;times new roman&#39; , serif">Enzymes used for the
hydrolysis of plant and animal proteins are mainly commercial preparations of
digestive enzymes (trypsin, chymotrypsin, pepsin), of plant origin (papain), or
of microbiological origin (Neutrase, Alcalase, Corolase) preparation. However,
new enzymes obtained from readily available sources that can efficiently
hydrolyse food proteins and effectively reduce their allergenicity are
constantly being sought. Non-commercial extracellular serine proteases obtained
from Asian pumpkin (<em>Cucurbita ficifolia</em>) are an attractive group of
enzymes that can be used for such purposes.</span></p><p>

<br /></p><p class="MsoNormal" style="text-align:justify;line-height:200%"><span lang="EN-GB" style="font-family:&#39;times new roman&#39; , serif">This study aimed</span><span lang="EN-GB" style="font-family:&#39;times new roman&#39; , serif"> to evaluate the optimal
conditions for hydrolysing peanut protein fraction isolates using Asian pumpkin
protease. The effects of hydrolysis on the immunoreactivity of the resulting
preparations were also investigated.</span></p>