Influence of Roasting Temperature on the Detectability of Potentially Allergenic Lupin by SDS-PAGE, ELISAs, LC-MS/MS, and Real-Time PCR
Seeds of “sweet lupins” have been playing an increasing role in the food industry. Lupin proteins may be used for producing a variety of foods, including pasta, bread, cookies, dairy products, and coffee substitutes. In a small percentage of the population, lupin consumption may elicit allergic reac...
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MDPI AG
2024-02-01
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author | Bruno Beyer Dominik Obrist Philipp Czarda Katharina Pühringer Filip Vymyslicky Barbara Siegmund Stefano D’Amico Margit Cichna-Markl |
author_facet | Bruno Beyer Dominik Obrist Philipp Czarda Katharina Pühringer Filip Vymyslicky Barbara Siegmund Stefano D’Amico Margit Cichna-Markl |
author_sort | Bruno Beyer |
collection | DOAJ |
description | Seeds of “sweet lupins” have been playing an increasing role in the food industry. Lupin proteins may be used for producing a variety of foods, including pasta, bread, cookies, dairy products, and coffee substitutes. In a small percentage of the population, lupin consumption may elicit allergic reactions, either due to primary sensitization to lupin or due to cross-allergy with other legumes. Thus, lupin has to be declared on commercial food products according to EU food regulations. In this study, we investigated the influence of roasting seeds of the <i>L. angustifolius</i> cultivar “Boregine” on the detectability of lupin by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), ELISAs, LC-MS/MS, and real-time PCR. Seeds were roasted by fluidized bed roasting, and samples were drawn at seed surface temperatures ranging from 98 °C to 242 °C. With increasing roasting temperature, the extractability of proteins and DNA decreased. In addition, roasting resulted in lower detectability of lupin proteins by ELISAs and LC-MS/MS and lower detectability of DNA by real-time PCR. Our results suggest reduced allergenicity of roasted lupin seeds used for the production of “lupin coffee”; however, this has to be confirmed in in vivo studies. |
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spelling | doaj.art-dc40a713a15243b3bd7007c010750d4a2024-03-12T16:44:04ZengMDPI AGFoods2304-81582024-02-0113567310.3390/foods13050673Influence of Roasting Temperature on the Detectability of Potentially Allergenic Lupin by SDS-PAGE, ELISAs, LC-MS/MS, and Real-Time PCRBruno Beyer0Dominik Obrist1Philipp Czarda2Katharina Pühringer3Filip Vymyslicky4Barbara Siegmund5Stefano D’Amico6Margit Cichna-Markl7Department of Analytical Chemistry, Faculty of Chemistry, University of Vienna, Währinger Straße 38, 1090 Vienna, AustriaDepartment of Analytical Chemistry, Faculty of Chemistry, University of Vienna, Währinger Straße 38, 1090 Vienna, AustriaDepartment of Analytical Chemistry, Faculty of Chemistry, University of Vienna, Währinger Straße 38, 1090 Vienna, AustriaDepartment of Analytical Chemistry, Faculty of Chemistry, University of Vienna, Währinger Straße 38, 1090 Vienna, AustriaDepartment of Analytical Chemistry, Faculty of Science, Charles University, Hlavova 8/2030, 12843 Prague 2, Czech RepublicInstitute of Analytical Chemistry and Food Chemistry, Graz University of Technology, Stremayrgasse 9/II, 8010 Graz, AustriaAGES—Austrian Agency for Health and Food Safety, Institute for Animal Nutrition and Feed, Spargelfeldstrasse 191, 1220 Vienna, AustriaDepartment of Analytical Chemistry, Faculty of Chemistry, University of Vienna, Währinger Straße 38, 1090 Vienna, AustriaSeeds of “sweet lupins” have been playing an increasing role in the food industry. Lupin proteins may be used for producing a variety of foods, including pasta, bread, cookies, dairy products, and coffee substitutes. In a small percentage of the population, lupin consumption may elicit allergic reactions, either due to primary sensitization to lupin or due to cross-allergy with other legumes. Thus, lupin has to be declared on commercial food products according to EU food regulations. In this study, we investigated the influence of roasting seeds of the <i>L. angustifolius</i> cultivar “Boregine” on the detectability of lupin by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), ELISAs, LC-MS/MS, and real-time PCR. Seeds were roasted by fluidized bed roasting, and samples were drawn at seed surface temperatures ranging from 98 °C to 242 °C. With increasing roasting temperature, the extractability of proteins and DNA decreased. In addition, roasting resulted in lower detectability of lupin proteins by ELISAs and LC-MS/MS and lower detectability of DNA by real-time PCR. Our results suggest reduced allergenicity of roasted lupin seeds used for the production of “lupin coffee”; however, this has to be confirmed in in vivo studies.https://www.mdpi.com/2304-8158/13/5/673lupin<i>Lupinus angustifolius</i>cultivar Boreginefood allergenroastingdetectability |
spellingShingle | Bruno Beyer Dominik Obrist Philipp Czarda Katharina Pühringer Filip Vymyslicky Barbara Siegmund Stefano D’Amico Margit Cichna-Markl Influence of Roasting Temperature on the Detectability of Potentially Allergenic Lupin by SDS-PAGE, ELISAs, LC-MS/MS, and Real-Time PCR Foods lupin <i>Lupinus angustifolius</i> cultivar Boregine food allergen roasting detectability |
title | Influence of Roasting Temperature on the Detectability of Potentially Allergenic Lupin by SDS-PAGE, ELISAs, LC-MS/MS, and Real-Time PCR |
title_full | Influence of Roasting Temperature on the Detectability of Potentially Allergenic Lupin by SDS-PAGE, ELISAs, LC-MS/MS, and Real-Time PCR |
title_fullStr | Influence of Roasting Temperature on the Detectability of Potentially Allergenic Lupin by SDS-PAGE, ELISAs, LC-MS/MS, and Real-Time PCR |
title_full_unstemmed | Influence of Roasting Temperature on the Detectability of Potentially Allergenic Lupin by SDS-PAGE, ELISAs, LC-MS/MS, and Real-Time PCR |
title_short | Influence of Roasting Temperature on the Detectability of Potentially Allergenic Lupin by SDS-PAGE, ELISAs, LC-MS/MS, and Real-Time PCR |
title_sort | influence of roasting temperature on the detectability of potentially allergenic lupin by sds page elisas lc ms ms and real time pcr |
topic | lupin <i>Lupinus angustifolius</i> cultivar Boregine food allergen roasting detectability |
url | https://www.mdpi.com/2304-8158/13/5/673 |
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