Abstract
The increasing prevalence of lupin allergy as a consequence to the functional characteristics of a growing number of sweet lupin-derived foods consumption makes the imperious necessity to develop analytical tools for the detection of allergen proteins in foodstuffs. The current study developed a new highly specific, sensitive and accurate ELISA method to detect, identify and quantify the lupin main allergen β-conglutin (Lup an 1) protein in natural and processed food. The implementation of accurate standards made with recombinant conglutin β1, and an anti-Lup an 1 antibody made from a synthetic peptide commonly shared among β-conglutin isoforms from sweet lupin species was able to detect up to 8.1250 ± 0.1701 ng (0.0406 ± 0.0009 ppm) of Lup an 1. This identified even lupin traces present in food samples which might elicit allergic reactions in sensitized consumers, such as β-conglutin proteins detection and quantification in processed (roasted, fermented, boiled, cooked, pickled, toasted, pasteurized) food, while avoiding cross-reactivity (false positive) with other legumes as peanut, chickpea, lentils, faba bean, and cereals. This study demonstrated that this new ELISA method constitutes a highly sensitive and reliable molecular tool able to detect, identify and quantify Lup an 1. This contributes to a more efficient management of allergens by the food industry, the regulatory agencies and clinicians, thus helping to keep the health safety of the consumers.
Highlights
Lupine is a legume that belongs to the genus Lupinus and is included in the Leguminosae family, which is of great interest to the food industry, for chickpeas, beans, peanuts, soya bean, lentils, and peas
A globular structure was built for the rest of the β-conglutin sequence integrated by 2 β-barrels of antiparallel β-sheets (Figure 1) with large conserved areas, where it was included in the sequence used to make the synthetic peptide (Figure S1) and the anti-β-conglutin antibody used in this enzyme-linked immunosorbent assay (ELISA) method
A newly developed ELISA assay was assessed for its capability to detect, identify and quantify the lupin main allergen β-conglutin protein (Lup an 1) in natural products and processed foodstuffs
Summary
Lupine is a legume that belongs to the genus Lupinus and is included in the Leguminosae family, which is of great interest to the food industry, for chickpeas, beans, peanuts, soya bean, lentils, and peas. Only the four known as the sweet lupin group have gained interest since they are used in human food production [2] for their low levels of alkaloids [3] contained in their seeds. These four species include Lupinus albus (white lupine), Lupinus angustifolius (blue lupin or narrow-leafed lupin, NLL), Lupinus luteus (yellow lupine) [4], and Lupinus mutabilis (pearl or Andean lupin) that are mostly cultivated and consumed in central and. Sweet lupin species are a promising source of innovative ingredients for functional food, those from the vicilin or β-conglutin family, Foods 2019, 8, 513; doi:10.3390/foods8100513 www.mdpi.com/journal/foods
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