Detection of peanut in legume containing food products

Chung Cho, Rakhi Panda, Katherine Ivens, Anne C. Eischeid, Shaun MacMahon, Gregory O. Noonan, and 

Eric A.E. Garber

Corresponding Author

Chung Cho, Chung.Cho@fda.hhs.gov

Office of Regulatory Science, Center for Food Safety and Applied Nutrition (CFSAN), Food and Drug 

Administration, College Park, MD 20740, USA

Abstract

Food allergies affect 4% of adults and 8% of children, and each year, about 29,000 cases of anaphylaxis 

occur in allergic individuals, resulting in roughly 150 deaths. Peanut allergy affects about 0.6% of adults 

and 0.8% of children in the U.S. is one of the most severe allergies, causing potentially life-threatening 

reactions. Patients do not generally outgrow peanut allergy, and since there is currently no cure, 

avoidance of peanut is the only option for the allergic population. The Food Allergen Labeling and 

Consumer Protection Act of 2004 (FALCPA) mandates that manufacturers label major allergens on food 

labels. However, inadvertent cross-contact of allergens is still possible, threatening the health of allergic 

individuals. Peanuts belongs to the legume family and contain homologous proteins to those present in 

other legume species. In recent years, foods have been recalled due the presence of peanut in legume 

containing products. Current commercial ELISA methods face challenges in detecting peanut in legume 

containing products due to cross-reactivity issues. In this study, the limitations of the ELISA methods have 

been addressed by using orthogonal methods, including the multi-analyte profiling food allergen 

detection assay (xMAP FADA) and a DNA-based PCR method targeting regions of the peanut chloroplast 

genome, to detect the presence of peanut in legume containing food products.

Poster Category: Allergens

Poster Number: ALGN-01

Coauthors

Rakhi Panda, FDA

Katherine Ivens, FDA

Anne C. Eischeid, FDA

Shaun MacMahon, FDA

Gregory O. Noonan, FDA

Eric A.E. Garber, FDA
Development and Validation of a Multiplex Real-time PCR Assay to Detect Allergenic Peanut 

in Complex Food Matrices

Anne Eischeid and Caroline Puente-Lelievre

Corresponding Author

Anne Eischeid, Anne.Eischeid@fda.hhs.gov

U.S. Food and Drug Administration

Abstract

Peanut causes some of the most common and most severe allergic reactions to food in the United States. 

Since there is currently no treatment for food allergy, allergic individuals must rely on accurate labeling 

avoid offending foods. This requires detection methods that are highly sensitive, specific, and robust in 

food products. Previous work has demonstrated that real-time PCR is a well-suited and advantageous 

orthogonal approach to the more standard protein-based allergen detection assays. In this work, we 

developed and validated a multiplex real-time PCR method for detection of peanut in food products. The 

assay utilizes three different peanut-specific targets, all derived from the chloroplast genome. Extensive 

in silico design and evaluation of primers and probes was carried out prior to thorough testing in the 

laboratory before final assay targets were chosen. Food products were spiked with known quantities of 

peanut, then subject to thorough homogenization in detergent buffer and DNA extraction according to 

procedures previously established in our laboratory. PCR conditions were optimized prior to final 

validation in foods. The method proved to have high reaction efficiency and linearity over 6-7 orders of 

magnitude, with lower limits of detection at 0.1-1 mg/kg (parts per million) in baked goods, chocolate, 

and tomato-based products. This is the first peanut detection assay we know of that targets chloroplast 

markers in a real-time multiplex PCR format and has been thoroughly tested in a variety of food products.

Poster Category: Allergens

Poster Number: ALGN-02

Coauthors

Caroline Puente-Lelievre, U.S. Food and Drug Administration
The curation of transcriptomic data for use as a proxy protein database for unsequenced tree 

nuts

Cary Prione-Davies, Melinda A. McFarland, Christine H. Parker, and Timothy R. Croley

Corresponding Author

Cary Prione-Davies, Cary.Pirone@fda.hhs.gov

The U.S. Food and Drug Administration

Abstract

As the apparent incidence of tree nut allergies rises, the development of mass spectrometric methods 

that accurately identify closely related tree nuts in food is critical. The outcome of LC-MS/MS experiments 

relies on the availability of protein sequences for database construction, however, these data are often 

sparse, particularly for non-model species such as tree nuts. We showed previously that translated 

transcriptomic data can serve as a proxy protein database for the analysis of walnut samples. However, 

published transcriptomes are not always available, and instead must be re-assembled from archived RNASeq reads. Reads typically undergo several pre-assembly processing steps including read quality trimming, 

error correction, and normalization. The optimal implementation of these steps for high quality, complete 

transcriptomes is currently under debate, and no information is available regarding their effect on MS/MS 

search results. Here, we determine the impact of read processing workflows on walnut transcriptome 

quality as well as downstream peptide identifications. Raw English walnuts, Juglans regia, were extracted 

and subjected to nLC-MS/MS on an Orbitrap Elite mass spectrometer. Spectra were searched in MASCOT 

against eight custom transcriptomic databases constructed using stringent versus relaxed read quality 

trimming, the application of read error correction or not, and two commonly used normalization standard 

deviation values (100 vs 10,000). A 3-way ANOVA was used to compare the mean number of peptides 

identified when searching against each database (n=3). Searches of databases constructed using read 

error correction and/or a standard deviation value of 100 identified a significantly higher mean number 

of peptides than databases constructed without read error correction and a standard deviation value of 

10,000. In addition, we compared the number of peptides identified when searching against a database 

constructed from nut-specific reads (immature fruit and embryo) versus one made from 16 combined 

walnut tissues.

Poster Category: Allergens

Poster Number: ALGN-03

Coauthors

Melinda A. McFarland, The U.S. Food and Drug Administration

Christine H. Parker, The U.S. Food and Drug Administration

Timothy R. Croley, The U.S. Food and Drug Administration
The Selection of Tree Nut Peptide Markers: A Need for Improved Protein Sequences 

Databases

Weili Xiong, Melinda A. McFarland, Cary Pirone, and Christine H. Parker

Corresponding Author

Weili Xiong, weili.xiong@fda.hhs.gov

U.S. Food and Drug Administration, Center for Food Safety and Applied Nutrition, College Park, MD

Abstract

Mass spectrometry-based detection of allergenic foods relies on the systematic identification of robust 

and selective peptide markers. The selection of proteotypic peptide markers depends on the availability 

of high-quality protein sequence information, a bottleneck for the analysis of many plant-based 

proteomes. The goal of this work was to establish a workflow for the selection of walnut peptide markers, 

which includes the implementation of a comprehensive protein database and the empirical evaluation of 

closely-related food ingredients and commercial food commodities. Raw and roasted varieties of common 

tree nuts (English walnut, black walnut [raw only], pecan and hazelnut) and commercial walnut-containing 

samples were ground, defatted, and extracted for total protein content. Sample extracts were 

concentrated and digested using a modified filter-aided sample preparation (FASP) protocol and LCMS/MS data were evaluated applying a parsimony-driven global proteomics workflow. A two-tier strategy 

was applied to select candidate peptide markers whereby traditional selection criteria including empirical 

MS identification, physiochemical properties, and specificity were complimented by differential peptidebased profiling of peptide markers in processed (e.g. roasted) ingredients and peptide presence in 

commercial food commodities. Candidate peptides (5 peptides per protein family) were selected from 

priority (high abundance) allergen protein families as the foundation for targeted MS method 

development. Using walnut as a case study, this work establishes criteria for the selection of candidate 

peptide markers in tree nut proteomes. Moving forward, improved protein databases will provide a more 

comprehensive view of tree nut protein and peptide identifications and help establish highly-specific 

confirmatory workflows for the detection and quantification of allergenic foods.

Poster Category: Allergens

Poster Number: ALGN-04

Coauthors

Melinda A. McFarland, U.S. Food and Drug Administration, Center for Food Safety and Applied Nutrition, 

College Park, MD

Cary Pirone, U.S. Food and Drug Administration, Center for Food Safety and Applied Nutrition, College 

Park, MD

Christine H. Parker, U.S. Food and Drug Administration, Center for Food Safety and Applied Nutrition, 

College Park, MD
Western Blot Analysis of Fermented-hydrolyzed Gluten Utilizing Antibodies Employed in a 

Novel Multiplex-Competitive ELISA

Rakhi Panda and Eric A.E. Garber

Corresponding Author

Rakhi Panda, Rakhi.Panda@fda.hhs.gov

FDA

Abstract

Methods are lacking for the detection and quantitation of gluten in foods subjected to fermentation and 

other forms of processing that results in hydrolysis. In this study, gluten specific antibodies (G12, R5, 2D4, 

MIoBS and Skerritt), from nine commercial gluten ELISA test kits, previously utilized in the development 

of the multiplex-competitive ELISA, were utilized in western blot analyses of 59 fermented-hydrolyzed 

foods from four food groups (beer, soy-based sauces, vinegar, and sourdough bread). Cluster analysis of 

the estimated gluten concentration values (based on western blot band intensities relative to intact gluten 

standards at 2.5 μg/mL and 100 μg/mL) distinguished products among the different categories of 

fermented-hydrolyzed foods, comparable to what was observed in the multiplex-competitive ELISA. 

Further, unlike the multiplex-competitive ELISA, the western blot analyses distinguished between the 

presence of antigenic proteinaceous materials and false positives due to the presence of binding inhibitors 

(observed with four soy-based sauces and one vinegar). Western blot analysis provides an orthogonal 

approach that can be used to both confirm the multiplex-competitive ELISA while also providing additional 

insight into the protein/peptide profile of fermented-hydrolyzed foods. The use of the two 

complementary approaches should assist in selecting appropriate calibration standards that may be useful 

in the qualitative and quantitative characterization of gluten in fermented-hydrolyzed food products.

Poster Category: Allergens

Poster Number: ALGN-05

Coauthors

Eric A.E. Garber, FDA
Measurements of Specific Milk Allergens in Baked Food Challenge Materials

Stephanie Filep, Bryan Smith, Sabina Wuenschmann, and Martin Chapman

Corresponding Author

Stephanie Filep, sfilep@inbio.com

Indoor Biotechnologies, Inc.

Abstract

Rationale: Oral food challenges (OFC) are considered the ‘gold standard’ to diagnose a true food allergy. 

Allergists use baked milk food preparations for OFC under the assumption that they contain decreased 

allergen levels due to baking. However, the effects of baking on specific allergens has not been thoroughly 

investigated. The aim was to compare levels of major milk allergens and IgE reactivity in uncooked and 

baked milk challenge materials currently used in clinical practice.

Methods: Uncooked and baked muffins were prepared using recipes from Mount Sinai (Jaffe Food Allergy 

Institute) and the UK National Health Service (NHS). Allergen levels were compared using a two-site 

monoclonal antibody ELISA for beta-lactoglobulin (Bosd5) and for beta-casein (Bosd11). IgE reactivity was 

assessed using sera from milk-allergic patients in direct binding and inhibition ELISA.

Results: Bosd5 (β-lactoglobulin) concentration decreased from 722μg/g in uncooked muffin mix to 

0.18μg/g in baked muffin, representing >99% reduction in Bosd5 allergen. The level of Bosd11 (β-casein) 

decreased by 32% from 5,640μg/g in uncooked muffin mix to 3,828μg/g in baked muffin. Bosd11 levels in 

the Mount Sinai muffins (n=35) were higher compared to the NHS muffins (n=15) and varied depending 

on whether the baked muffin was sampled from the top, middle or bottom. Baked muffins retained ~70% 

of the IgE reactivity in uncooked muffin mix while baked muffin extracts inhibited IgE antibody binding to 

uncooked muffin by up to 80%.

Conclusions: The level of major milk allergen Bosd11 remained high in baked muffins used in oral food 

challenges. These findings emphasize the potential risk for adverse reactions to baked milk challenges, 

especially in patients who have high anti-casein IgE antibodies. Measurements of specific milk allergens, 

together with IgE molecular diagnostics, should improve the safety of food products used for OFC and 

reduce the risks associated with milk challenges in clinical practice.

Poster Category: Allergens

Poster Number: ALGN-06

Coauthors

Bryan Smith, Indoor Biotechnologies, Inc.

Sabina Wuenschmann, Indoor Biotechnologies, Inc.

Martin Chapman, Indoor Biotechnologies, Inc.
Simultaneous Quantification of Major Food Allergens Using a Multiplex Immunoassay

Stephanie Filep, Bryan Smith, Kristina Reid Black, and Jessica Lee

Corresponding Author

Stephanie Filep, sfilep@inbio.com

Indoor Biotechnologies, Inc.

Abstract

Rationale: Quantification of food allergens is increasingly important for dose assessments of food 

preparations used in oral food challenges (OFC), food allergy prevention, and monitoring safety in the 

food industry. Generic immunoassays for ‘total protein’ do not measure specific allergens. Our aim was 

to use a molecular approach to food allergy to develop a multiplex immunoassay capable of 

simultaneously measuring specific allergens, the ‘active ingredients’, from peanut, cow’s milk, shellfish, 

egg, cashew, soy and hazelnut.

Methods: The multiplex array was developed on the Luminex xMAP system. Microspheres coupled to 

specific monoclonal antibodies were used for allergen capture. Biotinylated specific monoclonal or 

polyclonal antibodies were used for detection. Reference standards were formulated from natural or 

recombinant allergens, with purity established by mass spectrometry. Full method validations were 

performed to determine parameters of linearity, range, limits of quantification and detection, accuracy 

and precision of the multiplex food immunoassay.

Results: Method validations were completed for the major food allergens. Standard curves for all analytes 

allow for quantification over a broad dynamic range. Limits of detection were as low as 0.01ng/ml. Intraand inter- assay accuracy and precision of three samples assayed in triplicate on four occasions passed 

acceptance criteria within the range of 70-130% recovery and a coefficient of variation of <15%. Food 

products and the NIST SRM 2387 Reference Standard were analyzed using the multiplex immunoassay.

Conclusions: A quantitative, accurate and precise multiplex immunoassay was validated for the 

simultaneous detection of major food allergens. The multiplex array provides a sensitive and efficient tool 

for measuring specific food allergens, as opposed to generic food source proteins, with potential 

applications for risk assessment in the food industry and standardization of clinical OFC.

Poster Category: Allergens

Poster Number: ALGN-07

Coauthors

Bryan Smith, Indoor Biotechnologies, Inc.

Kristina Reid Black, Indoor Biotechnologies, Inc.

Jessica Lee, Indoor Biotechnologies, Inc.
xMAP FADA: A multiplex method for simultaneous detection of 15 food allergens plus gluten

Katherine Ivens, Chung Y. Cho, and Eric Garber

Corresponding Author

Katherine Ivens, katherine.ivens@fda.hhs.gov

FDA

Abstract

The Food Allergen Labeling and Consumer Protection Act of 2004 (FALCPA) imposes strict requirements 

for labeling of foods containing milk, eggs, fish, Crustacean shellfish, tree nuts, peanuts, wheat, or soy. In 

order to ensure the accuracy of labels, FDA relies on highly sensitive and highly specific allergen detection 

methods. The xMAP Food Allergen Detection Assay (xMAP FADA) is a unique and powerful analytical 

method for the simultaneous detection of almond, brazil nut, cashew, coconut, crustacean, egg, gluten, 

hazelnut, macadamia nut, milk, peanut, pine nut, pistachio, sesame, soy, and walnut in complex matrices. 

A strength of the xMAP is its redundancy: the use of at least two antibody capture-based assays per target 

analyte, except for crustacean, provides built-in confirmation of positive responses and the two most 

commonly employed extraction protocols, buffered-detergent (32-plex) and reduced-denatured 

conditions (5-plex). The use of multiple antibodies for each allergen permits the calculation of 

complimentary antibody bead set ratios, thereby allowing results to be interpreted, distinguished from 

cross-reactivity, and simultaneously confirmed. The high sensitivity of the xMAP technology further 

enables the use of multi-antibody profiles as an additional form of secondary end-point confirmation. The 

xMAP FADA is currently being used by the FDA for the analysis of regulatory samples, providing a powerful 

analytical solution particularly when the presence of multiple food allergens is possible. Additionally, the 

xMAP FADA has been used to analyze botanicals including dietary supplements and spices. These 

commodities commonly contain homologous proteins that may cross-react with the antibodies and in 

ELISA analyses generate false positives. Besides reducing cost and increasing through-put, the xMAP FADA 

provides a level of definitive detection, identification, and characterization not possible using ELISA 

technology.

Poster Category: Allergens

Poster Number: ALGN-08

Coauthors

Chung Y. Cho, FDA

Eric Garber, FDA
Optimization of a targeted, multi-allergen LC-MS/MS method for the quantification of egg, 

milk, and peanut in food

Katherine L. Fiedler, Weili Xiong, and Christine H. Parker

Corresponding Author

Katherine L. Fiedler, katherine.l.fiedler@fda.hhs.gov

U.S. Food and Drug Administration

Abstract

Liquid chromatography (LC)-tandem mass spectrometry (MS/MS) can be used as a complimentary 

analytical technique to immunochemical-based assays for allergen detection. A targeted, multi-allergen 

LC-MS/MS method has been previously developed for the simultaneous detection and quantification of 

egg, milk, and peanut. In bakery products, the method provided reliable detection of each allergen at 

concentrations as low as 5 mg/kg (ppm) incurred allergen ingredient using peptide markers from egg 

(lysozyme C and ovalbumin), milk (beta-lactoglobulin and alpha-S1 casein), and peanut (Arah1, Arah2, and 

Arah3). In the absence of established guidelines for MS-based quantification of allergens in food, the goal 

of this work was to evaluate different modes of quantification, establish acceptance criteria, and 

demonstrate transparency in the utilization of conversion factors. Allergen fortified, commercial cookie 

samples were homogenized, defatted, and extracted for total protein content. Sample concentration and 

trypsin digestion was performed using a modified filter-aided sample preparation (FASP) protocol. 

Isotopically-labeled synthetic peptides were added as peptide surrogates. The samples were analyzed on 

multiple LC-MS/MS platforms under both nano- and standard-flow LC conditions using a targeted multiple 

reaction monitoring (MRM) method on a 6500 QTRAP or nano-LC conditions using a parallel reaction 

monitoring (PRM) method on a Q Exactive. Method performance including accuracy, precision, limits of 

detection, and quantification were evaluated for different standards (isotopically-labeled peptide 

surrogates and chemically analogous protein/peptides), reference materials (synthetic native peptides 

and allergen standards), and instrument platforms. The suitability of each method platform for routine 

analysis was evaluated to provide a robust workflow that can be used in support of allergen management 

within the food industry and the protection of consumers with food allergies.

Poster Category: Allergens

Poster Number: ALGN-09

Coauthors

Weili Xiong, U.S. Food and Drug Administration

Christine H. Parker, U.S. Food and Drug Administration
Development of an in vitro Bio-assay using Human Intestinal and Immune Cell-lines to 

Measure the Immuno-pathogenicity of Food Allergens

Prasad Rallabhandi, Cho, Chung Y, MacMahon, Shaun, and Garber, Eric A.E

Corresponding Author

Prasad Rallabhandi, prasad.rallabhandi@fda.hhs.gov

Food & Drug Administration

Abstract

Food allergies are a rapidly growing public health problem that affect >15 million Americans. The FDA’s 

Food Allergen Labeling and Consumer Protection Act (FALCPA) requires that foods containing allergenic 

proteins derived from the eight major food allergens be declared. As strict avoidance is the only option 

for allergic consumers, accurate methods are needed to ensure correct labeling. The currently used 

Immunochemical methods (e.g. ELISA) detect IgG antigenic epitopes, and not allergenic elements. Hence, 

immunochemical methods may not detect antigenic epitopes that are transformed during food 

processing, while the immuno-pathogenicity could continue to persist. To address this gap in analytics, an 

in-vitro bio-assay that employs human intestinal epithelial and immune cell-lines to measure the biological 

effects caused by food allergens was developed. This novel biological activity-based assay compares the 

allergen-induced immuno-biological responses in Caco-2, HT-29 & T84 intestinal epithelial cells 

individually, as well as each co-cultured together with THP-1 cells. The goals of this project are to compare 

the cell signaling and immune modulation induced by different food allergens in a dose-dependent 

manner, and to further develop an in-vitro bio-assay using these cell lines.

Poster Category: Allergens

Poster Number: ALGN-10

Coauthors

Cho, Chung Y, FDA/CFSAN

MacMahon, Shaun, FDA/CFSAN

Garber, Eric A.E, FDA/CFSAN
Characterization and Certification of Milk Proteins as Certified Reference Materials

Derrell Johnson, Kevin Ray, Andria Widaman, Uma Sreenivasan, and Norman Hardt

Corresponding Author

Derrell Johnson, derrell.johnson@milliporesigma.com

MilliporeSigma

Abstract

Milk proteins are important nutritional constituents of milk and important contaminants in allergen 

testing of food products. Whey proteins, α-lactalbumin, β-lactoglobulin and lactoferrin have physiological 

activity through moderating gut micro flora, mineral absorption and immune function. Caseins are the 

main protein constituent in milk and cheese and comprised of related phosphoproteins (αS1, αS2, β, κ). 

Milk proteins are ingredients of choice in the formulation of modern foods, beverages, infant formula and 

nutritional supplements. However, milk proteins can also cause severe allergic effects and are subject of 

contamination control and testing in certain food products. New regulations for infant formula, food and 

allergen testing as well as advances in quantitation of proteins by LC-MS/MS[1] has led to the need for 

fully-intact milk protein Certified Reference Materials (CRMs) for accurate quantitation. Research grade 

proteins do not provide adequate accuracy and consistency in performance. Challenges with 

development, handling and certification of fully-intact protein CRMs will be presented. Critical factors in 

CRM development include proper characterization of the protein and its isoforms, certification of protein 

content, and control of vial-to-vial homogeneity. Research grade whey proteins were purified and 

lyophilized for development of a CRM. Certification was performed by mass balance incorporating purity 

by HPLC-UV-MS, water content by Karl Fischer Coulometry, and inorganic content by ICP-MS and residue 

on ignition. Suitable packaging was developed to preserve protein content. Accelerated stability and real 

time stability include assessment of water content and purity. Preliminary work on characterization of 

Casein by LC-UV/MS will also be presented.

Poster Category: Allergens

Poster Number: ALGN-11

Coauthors

Kevin Ray, MilliporeSigma

Andria Widaman, MilliporeSigma

Uma Sreenivasan, MilliporeSigma

Norman Hardt, MilliporeSigma
Food allergen reference materials - addressing an unmet need

Gill Holcombe, Clare Mills, Malcolm Burns, Chiara Nitride, Adrian Rogers, Malvinder Singh, Victoria Lee, 

Anuradha Balasundaram, Stephen Ellison, Kirstin Gray, Julian Braybrook, and Michael Walker

Corresponding Author

Gill Holcombe, gill.holcombe@lgcgroup.com

LGC

Abstract

Walker et al.[1] described the framework required to address problems detecting and quantifying 

allergenic proteins in foods at clinically relevant concentrations. Part of the solution is the provision of 

reference materials (RM). As well as two existing peanut allergen QC materials, LGC has recently worked 

with the University of Manchester (UoM), and Romer Laboratories Ltd to prepare a RM kit which 

addresses five additional allergens, in the form of skimmed milk powder, egg white powder, almond 

powder, hazelnut powder and walnut powder. Clinical relevance derives from the matrix and the incurred 

allergens. The matrix, a cold swelling starch-based chocolate flavoured paste, was used as the challenge 

vehicle for EuroPrevall food challenge studies. It was later shown to be suitable as an incurred QC material 

for the analysis of allergens in food. The incurred allergens are clinically relevant as they feature as priority 

allergens in food labelling law. The RM kit is industrially relevant as a processed food matrix of medium 

analytical difficulty owing to its polyphenol content with commonly used ingredients. The kit (LGC746-KT) 

contains the allergenic ingredients, the blank matrix and the incurred matrix containing each allergenic 

ingredient at 10 mg/kg of the allergenic protein. The allergens have been characterised by UoM by 

discovery proteomics and LGC-led homogeneity and stability studies (analysis by Romer), which along 

with in-house LGC work estimates the ELISA derived concentrations of 3 of the allergens. Some limited 

characterisation by molecular biology has also taken place within LGC. The kit contains instructions for 

use, indicative ELISA data and clear information on protein conversion factors. 

Acknowledgement : This project was funded by the UK Food Standards Agency (FS101206).

References: [1] Michael Walker et al. 2016, Flawed food allergen analysis–health and supply chain risks 

and a proposed framework to address urgent analytical needs, Analyst, 141, 24 - 35

Poster Category: Allergens

Poster Number: ALGN-12

Coauthors

Clare Mills, The University of Manchester

Malcolm Burns, LGC

Chiara Nitride, The University of Manchester

Adrian Rogers, Romer Labs UK Ltd

Malvinder Singh, LGC

Victoria Lee, The University of Manchester

Anuradha Balasundaram, The University of 

Manchester

Stephen Ellison, LGC

Kirstin Gray, LGC

Julian Braybrook, LGC

Michael Walker, LGC
Reference materials for food allergen analysis

Bert Popping and Roland Poms

Corresponding Author

Bert Popping, bert.popping@focos-food.com

FOCOS - FOCOS - Food Consulting Strategically

Abstract

Effective food allergen risk assessment and food allergen management are important to protect allergic 

consumers and to comply with allergen labelling regulations. Such approaches require reliable analytical 

tools for the detection of allergens in food. Both reference methods and reference materials are urgently 

needed to assure the quality reliability and compatibility of analytical results obtained with different 

methods. Being an important component of this analytical quality assurance, reference materials 

contribute to reliable and accurate results. Ensuring the correctness of analytical results is crucial to 

laboratories, since incorrect results may trigger decisions that can cause economic damage or pose a risk 

to public health. Validated reference materials/quality control materials and certified reference materials 

are indispensable for ⇒ Method development ⇒ Method calibration ⇒ Calibration of instruments ⇒

Validation of methods ⇒ Method verification ⇒ Proficiency testing ⇒ Process control and quality 

assurance in laboratory routine Besides, the use of reference materials is required by ISO/IEC standards.

Poster Category: Allergens

Poster Number: ALGN-14

Coauthors

Roland Poms, MoniQA Association