Narrow-Leafed Lupin Main Allergen β-Conglutin (Lup an 1) Detection and Quantification Assessment in Natural and Processed Foods
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...
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MDPI AG
2019-10-01
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Online Access: | https://www.mdpi.com/2304-8158/8/10/513 |
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author | Elena Lima-Cabello Juan D. Alché Jose C. Jimenez-Lopez |
author_facet | Elena Lima-Cabello Juan D. Alché Jose C. Jimenez-Lopez |
author_sort | Elena Lima-Cabello |
collection | DOAJ |
description | 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. |
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issn | 2304-8158 |
language | English |
last_indexed | 2024-04-12T10:58:40Z |
publishDate | 2019-10-01 |
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series | Foods |
spelling | doaj.art-1b3f42689deb4fe9a1266118b2dfc6552022-12-22T03:36:01ZengMDPI AGFoods2304-81582019-10-0181051310.3390/foods8100513foods8100513Narrow-Leafed Lupin Main Allergen β-Conglutin (Lup an 1) Detection and Quantification Assessment in Natural and Processed FoodsElena Lima-Cabello0Juan D. Alché1Jose C. Jimenez-Lopez2Department of Biochemistry, Cell & Molecular Biology of Plants, Estacion Experimental del Zaidin, Spanish National Research Council (CSIC), Profesor Albareda 1, E-18008 Granada, SpainDepartment of Biochemistry, Cell & Molecular Biology of Plants, Estacion Experimental del Zaidin, Spanish National Research Council (CSIC), Profesor Albareda 1, E-18008 Granada, SpainDepartment of Biochemistry, Cell & Molecular Biology of Plants, Estacion Experimental del Zaidin, Spanish National Research Council (CSIC), Profesor Albareda 1, E-18008 Granada, SpainThe 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.https://www.mdpi.com/2304-8158/8/10/513vicilin7s-globulinsfood allergenslup an 1sweet lupin speciesfood labellingprocessed food |
spellingShingle | Elena Lima-Cabello Juan D. Alché Jose C. Jimenez-Lopez Narrow-Leafed Lupin Main Allergen β-Conglutin (Lup an 1) Detection and Quantification Assessment in Natural and Processed Foods Foods vicilin 7s-globulins food allergens lup an 1 sweet lupin species food labelling processed food |
title | Narrow-Leafed Lupin Main Allergen β-Conglutin (Lup an 1) Detection and Quantification Assessment in Natural and Processed Foods |
title_full | Narrow-Leafed Lupin Main Allergen β-Conglutin (Lup an 1) Detection and Quantification Assessment in Natural and Processed Foods |
title_fullStr | Narrow-Leafed Lupin Main Allergen β-Conglutin (Lup an 1) Detection and Quantification Assessment in Natural and Processed Foods |
title_full_unstemmed | Narrow-Leafed Lupin Main Allergen β-Conglutin (Lup an 1) Detection and Quantification Assessment in Natural and Processed Foods |
title_short | Narrow-Leafed Lupin Main Allergen β-Conglutin (Lup an 1) Detection and Quantification Assessment in Natural and Processed Foods |
title_sort | narrow leafed lupin main allergen β conglutin lup an 1 detection and quantification assessment in natural and processed foods |
topic | vicilin 7s-globulins food allergens lup an 1 sweet lupin species food labelling processed food |
url | https://www.mdpi.com/2304-8158/8/10/513 |
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