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Analytical Methods for Allergen Control in Food Processing

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A special issue of Foods (ISSN 2304-8158). This special issue belongs to the section "Food Analytical Methods".

Deadline for manuscript submissions: closed (16 December 2021) | Viewed by 52097

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Special Issue Editors

Dr. Nanju Alice Lee

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Guest Editor

School of Chemical Engineering, Universit of New South Wales, Sydney, NSW 2052, Australia
Interests: food safety; food allergy; molecular allergenomics; food immunology; novel food processing; in vitro diagnostics technology
Special Issues, Collections and Topics in MDPI journals

Prof. Dr. Michelle Colgrave

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Guest Editor

1. CSIRO Agriculture & Food, 306 Carmody Road, St Lucia, QLD 4053, Australia
2. School of Science, Edith Cowan University, 270 Joondalup Rd, Joondalup, WA 6027, Australia
Interests: proteins; peptides; proteomics; allergy; food intolerance; alternative proteins; sustainable food production
Special Issues, Collections and Topics in MDPI journals

Prof. Dr. Andreas L. Lopata

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Guest Editor

Molecular and Cell Biology, James Cook University, Townsville, QLD 4811, Australia
Interests: food allergies; seafood allergies; molecular allergology; allergy diagnostics; allergen immunology; antibody cross-reactivity; allergen characterisation
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear colleague,

Food allergy and anaphylaxis have become a significant public health and food safety issue worldwide. The World Allergy Organisation (WAO) has estimated that at least 250 million people live with food allergies. Without a practical cure for food allergy, diligent avoidance of allergenic foods is the best management option for allergic individuals. As a result, many regulatory bodies mandate food allergen labeling to help allergic consumers to make an informed food choice and avoid accidental exposure.

The analytical methodology for the detection and quantification of allergen residues in foods is an integral part of the evidenced-based risk assessment for label decisions including precautionary allergen labelling (PAL). Accurate allergen detection continues to be a challenging task due to high uncertainty. While enzyme-linked immunosorbent assay (ELISA) serves as a gold standard for allergen detection, PCR methods and particularly mass spectrometry have gained momentum in recent years. With the demand for user-friendly rapid on-site testing, biosensors are also emerging as new allergen detection platforms. Binding specificity of biorecognition molecules dictates the accuracy and precision in allergen detection and development of new biorecognition molecules is also emerging. However, in all these methodologies, sample preparation remains to be the most labor-intensive and innovation is needed to simplify this step with greater efficiency.

This Special Issue will welcome original research and review papers that contribute to advances in the allergen detection methodologies that address all aspects of “Analytical Methods for Allergen Control in Food Processing” with special attention to the following key areas: new allergen tests, novel sample preparation methods, novel biorecognition molecules, new analytical platforms (e.g., biosensors, plasmonic ELISAs, mass spectrometric methods, novel PCR), new instrumentation and validation approaches.

Dr. Nanju Alice Lee
Prof. Dr. Michelle Colgrave
Prof. Dr. Andreas L. Lopata
Guest Editors

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Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Foods is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2900 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

food allergens
food allergy
public health
food safety
sample preparation
biosensors
allergen detection methodologies
biorecognition molecules
validation
on-site testing
ELISA
PCR and Mass spectrometry

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Published Papers (13 papers)

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Editorial

Jump to: Research, Review

5 pages, 211 KiB

Open AccessEditorial

Analytical Methods for Allergen Control in Food Processing

by Nanju Alice Lee, Andreas Ludwig Lopata and Michelle Lisa Colgrave

Foods 2023, 12(7), 1439; https://doi.org/10.3390/foods12071439 - 28 Mar 2023

Cited by 3 | Viewed by 2465

Abstract

Food allergy and food-related anaphylaxis have become a growing public health and food safety issue worldwide [...] Full article

(This article belongs to the Special Issue Analytical Methods for Allergen Control in Food Processing)

Research

Jump to: Editorial, Review

18 pages, 3418 KiB

Open AccessArticle

The Fate of IgE Epitopes and Coeliac Toxic Motifs during Simulated Gastrointestinal Digestion of Pizza Base

by Matthew E. Daly, Kai Wang, Xiaoyan Pan, Rosa L. Depau, Justin Marsh, Francesco Capozzi, Phil Johnson, Lee A. Gethings and E. N. Clare Mills

Foods 2022, 11(14), 2000; https://doi.org/10.3390/foods11142000 - 6 Jul 2022

Cited by 1 | Viewed by 2272

Abstract

Understanding how food processing may modify allergen bioaccessibility and the evolution of immunologically active peptides in the gastrointestinal tract is essential if knowledge-based approaches to reducing the allergenicity of food are to be realised. A soy-enriched wheat-based pizza base was subjected to in vitro oral–gastro–duodenal digestion and resulting digests analysed using a combination of sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) and mass spectrometry (MS). The digestion profile of pizza base resembled that of bread crust where higher temperatures during baking reduced protein solubility but still resulted in the generation of a complex mixture of peptides. MS profiling showed numerous peptides carrying IgE epitopes, and coeliac toxic motifs were in excess of 20–30 residues long and were only released after either 120 min of gastric digestion or a combination of gastric and duodenal digestion. In silico prediction tools showed an overestimated number of cleavage sites identified experimentally, with low levels of atypical peptic and chymotryptic cleavage sites identified particularly at glutamine residues. These data suggest that such alternative pepsin cleavage sites may play a role in digestion of glutamine-rich cereal foods. They also contribute to efforts to provide benchmarks for mapping in vitro digestion products of novel proteins which form part of the allergenicity risk assessment. Full article

(This article belongs to the Special Issue Analytical Methods for Allergen Control in Food Processing)

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18 pages, 2073 KiB

Open AccessEditor’s ChoiceArticle

Enzymatic Hydrolysis and Fermentation of Pea Protein Isolate and Its Effects on Antigenic Proteins, Functional Properties, and Sensory Profile

by Verónica García Arteaga, Victoria Demand, Karolin Kern, Andrea Strube, Michael Szardenings, Isabel Muranyi, Peter Eisner and Ute Schweiggert-Weisz

Foods 2022, 11(1), 118; https://doi.org/10.3390/foods11010118 - 4 Jan 2022

Cited by 35 | Viewed by 6371

Abstract

Combinations of enzymatic hydrolysis using different proteolytic enzymes (papain, Esperase^®, trypsin) and lactic fermentation with Lactobacillus plantarum were used to alter potential pea allergens, the functional properties and sensory profile of pea protein isolate (PPI). The order in which the treatments were performed had a major impact on the changes in the properties of the pea protein isolate; the highest changes were seen with the combination of fermentation followed by enzymatic hydrolysis. SDS-PAGE, gel filtration, and ELISA results showed changes in the protein molecular weight and a reduced immunogenicity of treated samples. Treated samples showed significantly increased protein solubility at pH 4.5 (31.19–66.55%) and at pH 7.0 (47.37–74.95%), compared to the untreated PPI (6.98% and 40.26%, respectively). The foaming capacity was significantly increased (1190–2575%) compared to the untreated PPI (840%). The treated PPI showed reduced pea characteristic off-flavors, where only the treatment with Esperase^® significantly increased the bitterness. The results from this study suggest that the combination of enzymatic hydrolysis and lactic fermentation is a promising method to be used in the food industry to produce pea protein ingredients with higher functionality and a highly neutral taste. A reduced detection signal of polyclonal rabbit anti-pea-antibodies against the processed protein preparations in ELISA furthermore might indicate a decreased immunological reaction after consumption. Full article

(This article belongs to the Special Issue Analytical Methods for Allergen Control in Food Processing)

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17 pages, 3442 KiB

Open AccessArticle

Improved Sensitivity of Allergen Detection by Immunoaffinity LC-MS/MS Using Ovalbumin as a Case Study

by Martin Röder, Claudia Wiacek, Frauke Lankamp, Jonathan Kreyer, Wolfgang Weber and Elke Ueberham

Foods 2021, 10(12), 2932; https://doi.org/10.3390/foods10122932 - 27 Nov 2021

Cited by 6 | Viewed by 3250

Abstract

Food allergies are caused by severe hypersensitivity to specific food allergens such as the egg protein ovalbumin. It is therefore important to test food products for the presence of allergens to protect allergic people from accidental ingestion. For egg detection, ELISA is the only reasonable commercially available test format, although the recognition of target allergens can be affected by food processing, which may lead to false negative results. Current mass spectrometry-based detection methods may overcome this issue, but these approaches are often less sensitive. Here we combined the advantages of antibody-based and MS-based methods by developing an immunoaffinity LC-MS/MS technique to detect the common egg allergen Gal d 2. We investigated the principal functionality of this method with incurred cookie material containing whole egg powder. We found that the new method matched easily the sensitivity of egg specific ELISA tests. Further western blot experiments indicated that this strategy may be unaffected by food processing, providing an important alternative strategy for the detection and quantification of allergens in food. Full article

(This article belongs to the Special Issue Analytical Methods for Allergen Control in Food Processing)

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18 pages, 24015 KiB

Open AccessArticle

A Response Surface Methodology (RSM) Approach for Optimizing the Attenuation of Human IgE-Reactivity to β-Lactoglobulin (β-Lg) by Hydrostatic High Pressure Processing

by Xin Sun, Jialing Vivien Chua, Quynh Anh Le, Francisco J. Trujillo, Mi-Hwa Oh, Dianne E. Campbell, Sam Mehr and Nanju Alice Lee

Foods 2021, 10(8), 1741; https://doi.org/10.3390/foods10081741 - 28 Jul 2021

Cited by 6 | Viewed by 2661

Abstract

The response surface methodology (RSM) and central composite design (CCD) technique were used to optimize the three key process parameters (i.e., pressure, temperature and holding time) of the high-hydrostatic-pressure (HHP) processing either standalone or combined with moderate thermal processing to modulate molecular structures of β-lactoglobulin (β-Lg) and α-lactalbumin (α-La) with reduced human IgE-reactivity. The RSM model derived for HHP-induced molecular changes of β-Lg determined immunochemically showed that temperature (temp), pressure (p²) and the interaction between temperature and time (t) had statistically significant effects (p < 0.05). The optimal condition defined as minimum (β-Lg specific) IgG-binding derived from the model was 505 MPa at 56 °C with a holding time of 102 min (R² of 0.81 and p-value of 0.01). The validation carried at the optimal condition and its surrounding region showed that the model to be underestimating the β-Lg structure modification. The molecular change of β-Lg was directly correlated with HHP-induced dimerization in this study, which followed a quadratic equation. The β-Lg dimers also resulted in the undetectable human IgE-binding. Full article

(This article belongs to the Special Issue Analytical Methods for Allergen Control in Food Processing)

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12 pages, 2249 KiB

Open AccessArticle

Electrochemical Immunosensor for the Simultaneous Determination of Two Main Peanut Allergenic Proteins (Ara h 1 and Ara h 6) in Food Matrices

by Maria Freitas, Marta M. P. S. Neves, Henri P. A. Nouws and Cristina Delerue-Matos

Foods 2021, 10(8), 1718; https://doi.org/10.3390/foods10081718 - 25 Jul 2021

Cited by 17 | Viewed by 3455

Abstract

Efficiently detecting peanut traces in food products can prevent severe allergic reactions and serious health implications. This work presents the development of an electrochemical dual immunosensor for the simultaneous analysis of two major peanut allergens, Ara h 1 and Ara h 6, in food matrices. A sandwich immunoassay was performed on a dual working screen-printed carbon electrode using monoclonal antibodies. The antibody–antigen interaction was detected by linear sweep voltammetry through the oxidation of enzymatically deposited silver, which was formed by using detection antibodies labeled with alkaline phosphatase and a 3-indoxyl phosphate/silver nitrate mixture as the enzymatic substrate. The assay time was 2 h 20 min, with a hands-on time of 30 min, and precise results and low limits of detection were obtained (Ara h 1: 5.2 ng·mL⁻¹; Ara h 6: 0.017 ng·mL⁻¹). The selectivity of the method was confirmed through the analysis of other food allergens and ingredients (e.g., hazelnut, soybean and lupin). The dual sensor was successfully applied to the analysis of several food products and was able to quantify the presence of peanuts down to 0.05% (w/w). The accuracy of the results was confirmed through recovery studies and by comparison with an enzyme-linked immunosorbent assay. Tracking food allergens is of utmost importance and can be performed using the present biosensor in a suitable and practical way. Full article

(This article belongs to the Special Issue Analytical Methods for Allergen Control in Food Processing)

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14 pages, 1705 KiB

Open AccessArticle

Survey of Commercial Food Products for Detection of Walnut (Juglans regia) by Two ELISA Methods and Real Time PCR

by Raquel Madrid, Aina García-García, Pablo Cabrera, Isabel González, Rosario Martín and Teresa García

Foods 2021, 10(2), 440; https://doi.org/10.3390/foods10020440 - 17 Feb 2021

Cited by 14 | Viewed by 3482

Abstract

Labeling of food allergens in accordance with legal regulations is important to protect the health of allergic consumers. The requirements for detecting allergens in foods involve adequate specificity and sensitivity to identify very small amounts of the target allergens in complex food matrices and processed foods. In this work, one hundred commercial samples were analyzed for walnut detection using three different methods: a sandwich enzyme-linked immunosorbent assay (ELISA) kit based on polyclonal antibodies, a direct ELISA using a recombinant multimeric scFv, and a real time PCR. The most sensitive method was real time PCR followed by sandwich ELISA kit and multimeric scFv ELISA. There was agreement between the three methods for walnut detection in commercial products, except for some heat-treated samples or those that contained pecan. The walnut ELISA kit was less affected by sample processing than was the multimeric scFv ELISA, but there was cross-reactivity with pecan, producing some false positives that must be confirmed by real time PCR. According to the results obtained, 7.0 to 12.6% of samples (depending on the analytical method) contained walnut but did not declare it, confirming there is a risk for allergic consumers. Moreover, there was one sample (3.7%) labelled as containing walnut but that tested negative for this tree nut. Genetic and immunoenzymatic techniques offer complementary approaches to develop a reliable verification for walnut allergen labeling. Full article

(This article belongs to the Special Issue Analytical Methods for Allergen Control in Food Processing)

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17 pages, 2790 KiB

Open AccessArticle

Effects of Extraction Buffer on the Solubility and Immunoreactivity of the Pacific Oyster Allergens

by Roni Nugraha, Thimo Ruethers, Elecia B. Johnston, Jennifer M. Rolland, Robyn E. O’Hehir, Sandip D. Kamath and Andreas L. Lopata

Foods 2021, 10(2), 409; https://doi.org/10.3390/foods10020409 - 12 Feb 2021

Cited by 27 | Viewed by 3452

Abstract

Despite recent technological advances, novel allergenic protein discovery is limited by their low abundance, often due to specific physical characteristics restricting their recovery during the extraction process from various allergen sources. In this study, eight different extraction buffers were compared for their ability to recover proteins from Pacific oyster (Crassostrea gigas). The protein composition was investigated using high resolution mass spectrometry. The antibody IgE-reactivity of each extract was determined using a pool of serum from five shellfish-allergic patients. Most of the investigated buffers showed good capacity to extract proteins from the Pacific oyster. In general, a higher concentration of proteins was recovered using high salt buffers or high pH buffers, subsequently revealing more IgE-reactive bands on immunoblotting. In contrast, low pH buffers resulted in a poor protein recovery and reduced IgE-reactivity. Discovery of additional IgE-reactive proteins in high salt buffers or high pH buffers was associated with an increase in allergen abundance in the extracts. In conclusion, increasing the ionic strength and pH of the buffer improves the solubility of allergenic proteins during the extraction process for oyster tissue. This strategy could also be applied for other difficult-to-extract allergen sources, thereby yielding an improved allergen panel for increased diagnostic efficiency. Full article

(This article belongs to the Special Issue Analytical Methods for Allergen Control in Food Processing)

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17 pages, 1478 KiB

Open AccessArticle

Production of a Recombinant Single-Domain Antibody for Gluten Detection in Foods Using the Pichia pastoris Expression System

by Aina García-García, Raquel Madrid, Eduardo Garcia-Calvo, Belén Mendoza-Chamizo, Teresa García and Rosario Martin

Foods 2020, 9(12), 1838; https://doi.org/10.3390/foods9121838 - 10 Dec 2020

Cited by 8 | Viewed by 3683

Abstract

The detection of gluten in foodstuffs has become a growing concern in food allergen management as a result of the high ratio of population sensitive to the main gluten-containing cereals. In this study, a promising single-domain antibody previously isolated by phage display (dAb8E) was produced in Pichia pastoris resulting in high levels of the antibody fragment expression (330 mg/L). The purified dAb8E was proved to specifically bind to gluten proteins from wheat, barley and rye, exhibiting no cross reaction to other heterologous species. The dynamic range of the sandwich enzyme-linked immunosorbent assay (ELISA) covered 0.1 to 10 µg/mL of gliadin, reaching a limit of detection of 0.12 µg/mL. When experimental binary mixtures of the target cereals were analyzed, the limit of detection was 0.13 mg/g, which would theoretically correspond to gluten concentrations of approximately 13 mg/kg. Finally, thirty commercially available food products were analyzed by means of the developed assay to further confirm the applicability of the dAb8E for gluten determination. The proposed methodology enabled the generation of a new gluten-specific nanobody which could be used to guarantee the appropriate labelling of gluten-free foods. Full article

(This article belongs to the Special Issue Analytical Methods for Allergen Control in Food Processing)

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11 pages, 1071 KiB

Open AccessArticle

Analysis of Gluten in Dried Yeast and Yeast-Containing Products

by Laura K. Allred, Mitchell G. Nye-Wood and Michelle L. Colgrave

Foods 2020, 9(12), 1790; https://doi.org/10.3390/foods9121790 - 2 Dec 2020

Cited by 5 | Viewed by 3960

Abstract

Yeast are commonly used in the preparation of foods and beverages such as beer and bread and may also be used on their own as a source of nutrients and flavoring. Because of the historical connection of yeast to products made from wheat and barley, consumers maintaining a gluten-free diet can have concerns about the safety of yeast ingredients. Analyzing the safety of yeast and yeast-containing products presents some difficulties, as the yeast organisms actively degrade any gluten in the product, raising questions on the appropriateness of detection by traditional antibody-based methods. This study examines a variety of yeast and yeast-containing products by competitive ELISA and liquid chromatography-mass spectrometry for the estimated level of gluten proteins. While samples such as yeast extracts and nutritional yeast contained gluten levels below the 20 mg/kg (or parts per million, ppm) threshold defined by Codex Alimentarius, one baking yeast and a nutritional yeast supplement sample contained higher levels of gluten. This study demonstrates that both competitive ELISA and liquid chromatography-mass spectrometry provide similar results in the detection of wheat and barley gluten in yeast-containing products. Full article

(This article belongs to the Special Issue Analytical Methods for Allergen Control in Food Processing)

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25 pages, 3443 KiB

Open AccessArticle

Comprehensive Characterization and Relative Quantification of α-Amylase/Trypsin Inhibitors from Wheat Cultivars by Targeted HPLC-MS/MS

by Sorel Tchewonpi Sagu, Lynn Zimmermann, Eva Landgräber, Thomas Homann, Gerd Huschek, Haydar Özpinar, Florian J. Schweigert and Harshadrai M. Rawel

Foods 2020, 9(10), 1448; https://doi.org/10.3390/foods9101448 - 13 Oct 2020

Cited by 16 | Viewed by 4798

Abstract

The α-amylase/trypsin inhibitors (ATIs) are discussed as being responsible for non-celiac wheat sensitivity (NCWS), besides being known as allergenic components for baker’s asthma. Different approaches for characterization and quantification including proteomics-based methods for wheat ATIs have been documented. In these studies generally the major ATIs have been addressed. The challenge of current study was then to develop a more comprehensive workflow encompassing all reviewed wheat-ATI entries in UniProt database. To substantially test proof of concept, 46 German and Turkish wheat samples were used. Two extractions systems based on chloroform/methanol mixture (CM) and under buffered denaturing conditions were evaluated. Three aspects were optimized, tryptic digestion, chromatographic separation, and targeted tandem mass spectrometric analysis (HPLC-MS/MS). Preliminary characterization with sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) documented the purity of the extracted ATIs with CM mixture and the amylase (60–80%)/trypsin (10–20%) inhibition demonstrated the bifunctional activity of ATIs. Thirteen (individual/common) biomarkers were established. Major ATIs (7–34%) were differently represented in samples. Finally, to our knowledge, the proposed HPLC-MS/MS method allowed for the first time so far the analysis of all 14 reviewed wheat ATI entries reported. Full article

(This article belongs to the Special Issue Analytical Methods for Allergen Control in Food Processing)

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Review

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18 pages, 1295 KiB

Open AccessReview

Detection of Allergenic Proteins in Foodstuffs: Advantages of the Innovative Multiplex Allergen Microarray-Based Immunoassay Compared to Conventional Methods

by Lisa Tuppo, Ivana Giangrieco, Maurizio Tamburrini, Claudia Alessandri, Adriano Mari and Maria Antonietta Ciardiello

Foods 2022, 11(6), 878; https://doi.org/10.3390/foods11060878 - 19 Mar 2022

Cited by 15 | Viewed by 5006

Abstract

Several factors can affect the allergen content and profile of a specific food, including processing procedures often leading to a decrease in allergenicity, although no change, or even an increase, have also been reported. Evaluation of the effectiveness of a processing procedure requires the availability of reliable methodologies to assess the variation in molecules able to induce allergic reactions in the analyzed food. Conventional and innovative strategies and methodologies can be exploited to identify allergenic proteins in foodstuffs. However, depending on the specific purposes, different methods can be used. In this review, we have critically reviewed the advantages of an innovative method, the multiplex allergen microarray-based immunoassay, in the detection of allergens in foodstuffs. In particular, we have analyzed some studies reporting the exploitation of an IgE-binding inhibition assay on multiplex allergen biochips, which has not yet been reviewed in the available literature. Unlike the others, this methodology enables the identification of many allergenic proteins, some of which are still unknown, which are recognized by IgE from allergic patients, with a single test. The examined literature suggests that the inhibition test associated with the multiplex allergen immunoassay is a promising methodology exploitable for the detection of IgE-binding proteins in food samples. Full article

(This article belongs to the Special Issue Analytical Methods for Allergen Control in Food Processing)

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20 pages, 634 KiB

Open AccessReview

Effect of Processing on Fish Protein Antigenicity and Allergenicity

by Xingyi Jiang and Qinchun Rao

Foods 2021, 10(5), 969; https://doi.org/10.3390/foods10050969 - 28 Apr 2021

Cited by 23 | Viewed by 4949

Abstract

Fish allergy is a life-long food allergy whose prevalence is affected by many demographic factors. Currently, there is no cure for fish allergy, which can only be managed by strict avoidance of fish in the diet. According to the WHO/IUIS Allergen Nomenclature Sub-Committee, 12 fish proteins are recognized as allergens. Different processing (thermal and non-thermal) techniques are applied to fish and fishery products to reduce microorganisms, extend shelf life, and alter organoleptic/nutritional properties. In this concise review, the development of a consistent terminology for studying food protein immunogenicity, antigenicity, and allergenicity is proposed. It also summarizes that food processing may lead to a decrease, no change, or even increase in fish antigenicity and allergenicity due to the change of protein solubility, protein denaturation, and the modification of linear or conformational epitopes. Recent studies investigated the effect of processing on fish antigenicity/allergenicity and were mainly conducted on commonly consumed fish species and major fish allergens using in vitro methods. Future research areas such as novel fish species/allergens and ex vivo/in vivo evaluation methods would convey a comprehensive view of the relationship between processing and fish allergy. Full article

(This article belongs to the Special Issue Analytical Methods for Allergen Control in Food Processing)

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