Medical Specialties Commons^™

Peanut Allergen Reaction Thresholds During Controlled Food Challenges In 2 Canadian Randomized Studies (Canada-Arm1 And Pisces), Derek K. Chu, Joseph L. Baumert, Steve L. Taylor, Julie A. Nordlee, Tina Nham, Jonathan Bramson, Sébastien La Vieille, Michael A. Abbott, Paul Spill, Andrea Marrin, Manel Jordana, Susan Waserman

Department of Food Science and Technology: Faculty Publications

In 2 randomized studies addressing peanut allergy (Canada-Food Allergy Risk Management 1 [NCT01812798] and Peanut Immunotherapy Starting in Canada, Evaluation and DiScovery [NCT0 1601522]), we quantified peanut allergen thresholds to food challenge using Bayesian stacked model averaging to inform policy and clinical practice. About 50% of patients tolerated more than 70 mg (~ ¼ peanut).

Purification And Characterization Of Naturally Occurring Post-Translationally Cleaved Ara H 6, An Allergen That Contributes Substantially To The Allergenic Potency Of Peanut, Govardus A. H. De Jong, Shyamali Jayasena, Phil Johnson, Justin Marsh, Danijela Apostolovic, Marianne Van Hage, Julie Nordlee, Joe Baumert, Steve L. Taylor, Camille Roucairol, Harmen De Jongh, Stef J. Koppelman

Department of Food Science and Technology: Faculty Publications

The 2S albumin Ara h 6 is one of the most important peanut allergens. A post-translationally cleaved Ara h 6 (pAra h 6) was purified from Virginia type peanuts, and the cleavage site was mapped using high-resolution mass spectrometry. Compared to intact Ara h 6, pAra h 6 lacks a 5-amino acid stretch, resembling amino acids 43−47 (UniProt accession number Q647G9) in the nonstructured loop. Consequently, pAra h 6 consists of two chains: an N-terminal chain of approximately 5 kDa and a C-terminal chain of approximately 9 kDa, held together by disulfide bonds. Intermediate post-translationally cleaved products, in which this …

In Vitro Digestion And Characterization Of 2s Albumin And Digestion-Resistant Peptides In Pecan, Jelena Spiric, Stef J. Koppelman, Andre Knulst, Julie A. Nordlee, Steve L. Taylor, Joseph L. Baumert

Department of Food Science and Technology: Faculty Publications

The 2S albumins are one of the major protein families involved in severe food allergic reactions to nuts, seeds, and legumes, thus potentially making these proteins clinically relevant for allergic sensitization and potential diagnostic markers. In this study, we sought to purify native 2S albumin protein from pecan to further characterize this putative allergen. The purified 2S albumin, Car i 1, from pecan was found to be resistant to digestion by pepsin in simulated gastric fluid (SGF) and comparatively stable to proteolysis by trypsin and pancreatin in simulated intestinal fluid (SIF). Digestion of purified Car i 1 in SGF and …

Peanut Allergen Threshold Study (Pats): Novel Single-Dose Oral Food Challenge Study To Validate Eliciting Doses In Children With Peanut Allergy, Jonathan O'B. Hourihane, Katrina J. Allen, Wayne G. Shreffler, Gillian Dunngalvin, Julie A. Nordlee, Giovanni A. Zurzolo, Audrey Dunngalvin, Lyle C. Gurrin, Joseph L. Baumert, Steve L. Taylor

Department of Food Science and Technology: Faculty Publications

Background: Eliciting doses (EDs) of allergenic foods can be defined by the distribution of threshold doses for subjects within a specific population. The ED₀₅ is the dose that elicits a reaction in 5% of allergic subjects. The predicted ED₀₅ for peanut is 1.5 mg of peanut protein (6 mg of whole peanut). Objective: We sought to validate the predicted peanut ED₀₅ (1.5 mg) with a novel single-dose challenge. Methods: Consecutive eligible children with peanut allergy in 3 centers were prospectively invited to participate, irrespective of previous reaction severity. Predetermined criteria for objective reactions were used to identify …

Threshold Dose Distribution And Eliciting Dose Of Cashew Nut Allergy, Johanna P. M. Van Der Valk, Roy Gerth Van Wijk, J. L. Baumert, J. A. Nordlee, Berber J. Vlieg-Boerstra, Hans De Groot, Anthony E. J. Dubois, Nicolette W. De Jong

Department of Food Science and Technology: Faculty Publications

A previous study found that 137 of 179 cashew nut sensitized children (76.5%) suspected of having cashew nut allergy had a positive double-blind, placebo-controlled food challenge (DBPCFC result), with 63 of 137 children (46%) manifesting subjective and/or objective symptoms to the lowest dose (1 mg of cashew nut protein). The primary aim of this study was to determine the distribution of threshold doses and the eliciting doses (EDs) in this population. The secondary aim was to investigate whether children who reacted to 1 mg of cashew nut (n = 63) could react to even lower doses than 1 mg (low-dose …

Rnai-Mediated Control Of Aflatoxins In Peanut: Method To Analyze Mycotoxin Production And Transgene Expression In The Peanut/Aspergillus Pathosystem, Renee S. Arias, Phat M. Dang, Victor S. Sobolev

United States Department of Agriculture-Agricultural Research Service / University of Nebraska-Lincoln: Faculty Publications

The Food and Agriculture Organization of the United Nations estimates that 25% of the food crops in the world are contaminated with aflatoxins. That represents 100 million tons of food being destroyed or diverted to non-human consumption each year. Aflatoxins are powerful carcinogens normally accumulated by the fungi Aspergillus flavus and A. parasiticus in cereals, nuts, root crops and other agricultural products. Silencing of five aflatoxin-synthesis genes by RNA interference (RNAi) in peanut plants was used to control aflatoxin accumulation following inoculation with A. flavus. Previously, no method existed to analyze the effectiveness of RNAi in individual peanut transgenic events, …

Comparison Of Six Commercial Elisa Kits For Their Specificity And Sensitivity In Detecting Different Major Peanut Allergens, Shyamali Jayasena, Mieke Smits, Daniëlle Fiechter, Aard De Jong, Julie Nordlee, Joe Baumert, Steve L. Taylor, Raymond H. Pieters, Stef J. Koppelman

Department of Food Science and Technology: Faculty Publications

Six commercial peanut enzyme-linked immunosorbent assay kits were assessed for their ability to recover peanut from the standard reference material 2387 peanut butter and also for their specificity in detecting four major peanut allergens, Ara h 1, Ara h 2, Ara h 3, and Ara h 6. The percentage recovery of peanut from peanut butter differed across different kits as well as at different sample concentrations. The highest recovery was observed with the Romer and R-Biopharm kits, while four other kits were found to underestimate the protein content of the reference peanut butter samples. Five of the kits were most …

The Mucosal Expression Pattern Of Interferon-Ε In Rhesus Macaques, Andrew Demers, Guobin Kang, Fangrui Ma, Wuxun Lu, Zhe Yuan, Yue Li, Mark Lewis, Edmundo N. Kraiselburd, Luis Montaner, Qingsheng Li

Qingsheng Li Publications

Type I IFNs play an important role in innate and adaptive immunity against viral infections. A novel type I IFN, namely IFN-ε, which can protect against vaginal transmission of HSV2 and Chlamydia muridarum bacterial infection, has been described in mice and humans. Nevertheless, the principle cell type and the expression pattern of IFN-ε in tissues remain uncertain. In addition, the expression of IFN-ε in Indian rhesus macaques (Macaca mulatta) has not been reported. Here, we analyzed IFN-ε expression in multiple mucosal sites of uninfected or SIV-infected Indian rhesus macaques using IHCS. We report for the first time the …

Sulfites, Steve L. Taylor, Robert K. Bush, Julie A. Nordlee

Department of Food Science and Technology: Faculty Publications

Key Concepts

Sulfites are frequently used food and drug additives.

Ingestion of sulfite residues has been documented to trigger asthmatic reactions in sensitive individuals.

Sulfite-induced asthma occurs in less than 5% of asthmatic individuals, and those with severe, persistent asthma are at greatest risk.

The diagnosis of sulfite-induced asthma is best made by blinded oral challenge with assessment of lung function.

Labeling regulations in the United States alert sulfite-sensitive individuals to the presence of sulfites in foods, which must then be avoided.

Development And Evolution Of Risk Assessment For Food Allergens, Rene W. R. Crevel, Joseph Baumert, Athanasia Baka, Geert Houben, André C. Knulst, Astrid Kruizinga, Stefano Luccioli, Stephen L. Taylor, Charlotte B. Madsen

Department of Food Science and Technology: Faculty Publications

The need to assess the risk from food allergens derives directly from the need to manage effectively this food safety hazard. Work spanning the last two decades dispelled the initial thinking that food allergens were so unique that the risk they posed was not amenable to established risk assessment approaches and methodologies. Food allergens possess some unique characteristics, which make a simple safety assessment approach based on the establishment of absolute population thresholds inadequate. Dose distribution modelling of MEDs permitted the quantification of the risk of reaction at the population level and has been readily integrated with consumption and contamination …

Translating Reference Doses Into Allergen Management Practice: Challenges For Stakeholders, René W. R. Crevel, Joseph Baumert, Stefano Luccioli, Athanasia Baka, Sue Hattersley, Jonathan O.B. Hourihane, Stefan Ronsmans, Frans Timmermans, Rachel Ward, Yong-Joo Chung

Department of Food Science and Technology: Faculty Publications

Risk assessment describes the impact of a particular hazard as a function of dose and exposure. It forms the foundation of risk management and contributes to the overall decision-making process, but is not its endpoint. This paper outlines a risk analysis framework to underpin decision-making in the area of allergen cross-contact. Specifically, it identifies challenges relevant to each component of the risk analysis: risk assessment (data gaps and output interpretation); risk management (clear and realistic objectives); and risk communication (clear articulation of risk and benefit). Translation of the outputs from risk assessment models into risk management measures must be informed …

Update Of The Who/Iuis Allergen Nomenclature Database Based On Analysis Of Allergen Sequences, C. Radauer, A. Nandy, F. Ferreira, Richard E. Goodman, J. N. Larsen, J. Lidholm, A. Pomés, M. Raulf-Heimsoth, P. Rozynek, W. R. Thomas, Heimo Breiteneder

Department of Food Science and Technology: Faculty Publications

The IUIS Allergen Nomenclature Sub-Committee, under the auspices of the World Health Organization and the International Union of Immunological Societies, maintains the systematic nomenclature of allergenic proteins and publishes a database of approved allergen names on its Web site, www.allergen.org. In this paper, we summarize updates of allergen names approved at the meetings of the committee in 2011 through 2013. These changes reflect recent progress in identification, cloning, and sequencing of allergens. The goals of this update were to increase consistency in the classification of allergens, isoallergens, and variants and in the incorporation of the evolutionary classification of proteins into …

Investigation Of Commercial Milk Enzyme-Linked Immunosorbent Assay (Elisa) Kits: Specificity And Utility For Residues Of Foods Subjected To Proteolysis During Processing, Katherine O. Ivens

Department of Food Science and Technology: Dissertations, Theses, and Student Research

Analytical methods, such as enzyme-linked immunosorbent assays (ELISA), are used to detect and quantify residues from allergenic sources in food products. However, ELISAs have not been validated for use in foods that have been exposed to proteolysis. This thesis explores the specificities, sensitivities, and capabilities of commercially-available milk ELISA kits for detecting milk residues in cheeses that have undergone varying degrees of proteolysis.

The specificity, accuracy, and consistency of twelve commercially-available milk ELISA kits for individual milk proteins and commonly used milk-derived ingredients, including α-,β-, and κ-casein, β-lactoglobulin, α-lactalbumin, non-fat dry milk, sodium caseinate, and whey protein concentrate were evaluated. …

Threshold Dose For Shrimp: A Risk Characterization Based On Objective Reactions In Clinical Studies, Julie A. Nordlee, Benjamin C. Remington, Barbara K. Ballmer-Weber, Samuel B. Lehrer, Joe L. Baumert, Steve L. Taylor

Department of Food Science and Technology: Faculty Publications

A DBPCFC [double-blind, placebo-controlled food challenge] of shrimp-allergic adults was conducted to obtain individual threshold doses. Results of this study and published research were combined and a population threshold for shrimp was determined from dose-distribution modeling. The shrimp-allergic population seems to have a higher threshold compared to other populations for other food allergens. Additional shrimp challenges should be done to confirm these initial results.

Challenges In Testing Genetically Modified Crops For Potential Increases In Endogenous Allergen Expression For Safety, Rakhi Panda, H. Ariyarathna, Plaimein Amnuaycheewa, Afua O. Tetteh, S. N. Pramod, Steve Taylor, B. K. Ballmer-Weber, Richard E. Goodman

Department of Food Science and Technology: Faculty Publications

Premarket, genetically modified (GM) plants are assessed for potential risks of food allergy. The major risk would be transfer of a gene encoding an allergen or protein nearly identical to an allergen into a different food source, which can be assessed by specific serum testing. The potential that a newly expressed protein might become an allergen is evaluated based on resistance to digestion in pepsin and abundance in food fractions. If the modified plant is a common allergenic source (e.g. soybean), regulatory guidelines suggest testing for increases in the expression of endogenous allergens. Some regulators request evaluating endogenous allergens for …

Severe Reactions To A Soy Containing Beverage In Peanut Allergic Individuals Not Avoiding Soy, Benjamin Remington, Julie A. Nordlee, John R. Bacon, Marc E. Dyer, Steve L. Taylor, Joe L. Baumert

Department of Food Science and Technology: Faculty Publications

Rationale: Three peanut-allergic individuals experienced severe reactions to a nationally distributed high-protein beverage in the same month. The major protein sources in the beverage were soy-based ingredients and cows’ milk. These individuals did not avoid soy in their diet and previously consumed various soy products without adverse reactions. Peanut contamination of the beverage was not detected by specific ELISA, so attention shifted to the soy ingredients. The research objective was to elucidate differences between the soy milk and soy protein isolate used in the beverage and other forms of soy safely consumed by these individuals.

Methods: Specific IgE levels from …

Measuring Parvalbumin Levels In Fish Muscle Tissue: Relevance Of Muscle Locations And Storage Conditions, Poi-Wah Lee, Julie A. Nordlee, Stef J. Koppelman, Joseph L. Baumert, Steve L. Taylor

Department of Food Science and Technology: Faculty Publications

Fish is an allergenic food capable of provoking severe anaphylactic reactions. Parvalbumin is the major allergen identified in fish and frog muscles. Antibodies against fish and frog parvalbumin have been used to quantify parvalbumin levels from fish. However, these antibodies react variably with parvalbumin from different fish species. Several factors might be responsible for this variation including instability of parvalbumin in fish muscle as a result of frozen storage and differential parvalbumin expression in muscles from various locations within the whole fish. We aimed to investigate whether these factors contribute to the previously observed variable immunoreactivity of the anti-parvalbumin antibodies. …

Parvalbumin In Fish Skin–Derived Gelatin: Is There A Risk For Fish Allergic Consumers?, S. J. Koppelman, J. A. Nordlee, P.-W. Lee, R. P. Happe, M. Hessing, R. Norland, T. Manning, R. Deschene, G. A. H. De Jong, S. L. Taylor

Department of Food Science and Technology: Faculty Publications

The major allergen parvalbumin was purified from cod muscle tissues, and polyclonal antibodies were raised toward it. The antibodies were tested for specificity, and an enzyme-linked immunosorbent assay (ELISA) was developed using these antibodies. The ELISA was applied to measure parvalbumin in cod skin, the starting material for fish gelatin made from deep sea, wild fish. The ELISA was sufficiently sensitive (LLOQ = 0.8 ng ml^–1 in extracts, corresponding to 0.02 μg of parvalbumin per g of tissue) and did not cross-react with common food constituents. Fish gelatin, wine, and beer, matrices for the potential use of this ELISA, …

Identification And Analysis Of The Ige Binding By Parvalbumin And Other Potential Allergens In Different Fish And Frog Species, P. Lee, J. A. Nordlee, S. J. Koppelman, J. L. Baumert, S. L. Taylor

Department of Food Science and Technology: Faculty Publications

Rationale: Serological cross-reactivity to different fish and frog species is common among fish-allergic individuals.We examined the intra- and inter-individual diversity in IgE responses of fish-allergic subjects to various fish and frog species and identified novel allergens besides parvalbumin.

Methods: Sera from 38 subjects with a clinical history of fish allergy were analyzed for IgE-binding profiles to crude extracts of 26 raw fish and frog species, and purified cod and carp parvalbumin using IgE-immunoblotting. Sera of 7 subjects showing similar IgE-binding profiles in the IgEimmmunoblotting were pooled to identify potential allergens in pilchard, herring, cod, cusk, and rainbow trout using two-dimensional …

Characterization Of Igg And Ige Binding To Parvalbumin Derived From Commercially Important Fish Species, P. Lee, J. A. Nordlee, S. J. Koppelman, J. L. Baumert, S. L. Taylor

Department of Food Science and Technology: Faculty Publications

Rationale: Parvalbumin is recognized as pan-allergen in fish and frog. However, previous studies demonstrated that the IgE- and IgG-binding patterns to parvalbumins vary depending on the fish species. We aimed to use 3 anti-parvalbumin IgG and human IgE to investigate the contributing factors for the binding differences.

Methods: Indirect enzyme-linked immunosorbent assay (ELISA) and IgG immunoblotting were used to determine the reactivity of the polyclonal anti-cod parvalbumin antibody and the commercially available, monoclonal anti-frog and anti-carp parvalbumin antibodies against raw muscle extracts of 25 fish species. Additionally, sera from 46 individuals with clinical history of fish allergy were analyzed for …

Suggested Improvements For The Allergenicity Assessment Of Genetically Modified Plants Used In Foods, Richard E. Goodman

Department of Food Science and Technology: Faculty Publications

Genetically modified (GM) plants are increasingly used for food production and industrial applications. As the global population has surpassed 7 billion and per capita consumption rises, food production is challenged by loss of arable land, changing weather patterns, and evolving plant pests and disease. Previous gains in quantity and quality relied on natural or artificial breeding, random mutagenesis, increased pesticide and fertilizer use, and improved farming techniques, all without a formal safety evaluation. However, the direct introduction of novel genes raised questions regarding safety that are being addressed by an evaluation process that considers potential increases in the allergenicity, toxicity, …

Evaluation And Comparison Of The Species-Specificity Of 3 Antiparvalbumin Igg Antibodies, Poi-Wah Lee, Julie A. Nordlee, Stef J. Koppelman, Joseph L. Baumert, Steve L. Taylor

Department of Food Science and Technology: Faculty Publications

Parvalbumin is a pan-allergen in fish and frogs that triggers IgE-mediated reactions in fish-allergic individuals. Previous studies demonstrated that antibodies raised against fish and frog parvalbumins displayed varying specificity for different fish species, and thus, the applicability of these antibodies for potential use in immunoassays to detect fish residues were limited. We aimed to determine the specificity of 3 IgG antibodies for various fish species. Indirect enzyme-linked immunosorbent assay (ELISA) and IgG-immunoblotting were used to compare the reactivity of the polyclonal anticod parvalbumin antibody and the commercially available, monoclonal antifrog and monoclonal anticarp parvalbumin antibodies against raw muscle extracts of …

Wild Buckwheat Is Unlikely To Pose A Risk To Buckwheat-Allergic Individuals, Julie A. Nordlee, Rakhi Panda, Joseph L. Baumert, Richard E. Goodman, Steve Taylor

Department of Food Science and Technology: Faculty Publications

Buckwheat (Fagopyrum esculentum) is a commonly allergenic food especially in Asia where buckwheat is more commonly consumed. Wild buckwheat (Polygonum convolvulus, recently changed to Fallopia convolvulus) is an annual weed prevalent in grain-growing areas of the United States. Wild buckwheat is not closely related to edible buckwheat although the seeds do have some physical resemblance. A large shipment of wheat into Japan was halted by the discovery of the adventitious presence of wild buckwheat seeds over possible concerns for buckwheat-allergic consumers. However, IgE-binding was not observed to an extract of wild buckwheat using sera from …

Purification Of Parvalbumin From Carp: A Protocol That Avoids Heat Treatment, Stef J. Koppelman, Roland A. Romijn, Harmen H. J. De Jongh, Julie A. Nordlee, Sander Piersma, Martin Hessing, Steve L. Taylor

Department of Food Science and Technology: Faculty Publications

Parvalbumin from carp, a major allergen,was purified to homogeneity using ion exchange chromatography and size exclusion chromatography (estimated purity > 95% to 98% based on SDS-PAGE and native PAGE) with a yield of 318 mg, and a number of basic biochemical characteristics were determined. The identity was confirmed by peptide-mass fingerprinting, and IgE-binding was demonstrated. The UV/Vis absorbance spectra were explained using the previously published amino acid sequences. Far UV-CD spectroscopy was used to confirm the folding character of parvalbumin. We conclude that parvalbumin from carp can be purified on a comparatively large (hundreds of milligrams) scale using a purification protocol …

Lupine Allergy: Not Simply Cross-Reactivity With Peanut Or Soy, Kim A. B. M. Peeters, Julie A. Nordlee, André H. Penninks, Lingyun Chen, Richard E. Goodman, Carla A. F. M. Bruijnzeel-Koomen, Sue L. Hefle, Steve L. Taylor, André C. Knulst

Department of Food Science and Technology: Faculty Publications

Background: Reports of lupine allergy are increasing as its use in food products increases. Lupine allergy might be the consequence of cross-reactivity after sensitization to peanut or other legumes or de novo sensitization. Lupine allergens have not been completely characterized. Objectives: We sought to identify allergens associated with lupine allergy, evaluate potential cross-reactivity with peanut, and determine eliciting doses (EDs) for lupine allergy by using double-blind, placebo-controlled food challenges. Methods: Six patients with a history of allergic reactions to lupine flour were evaluated by using skin prick tests, CAP tests, and double-blind, placebo-controlled food challenges. Three of these patients were …

Presentation Of Allergen In Different Food Preparations Affects The Nature Of The Allergic Reaction—A Case Series, K. E. C. Grimshaw, R. M. King, J. A. Nordlee, S. L. Hefle, John O. Warner, J. O.'B. Hourihane

Department of Food Science and Technology: Faculty Publications

Background: Characterization of fatal and nonfatal reactions to food indicates that the majority of reactions are due to the ingestion of prepared foods rather than the nonprocessed allergen. In an ongoing study that used a double-blind placebo-controlled food challenge to investigate peanut allergy and clinical symptoms, the observed reaction severity in four of the first six subjects was greater than anticipated. We hypothesized that this was due to differences in the composition of the challenge vehicle. Objective: The aim was to investigate whether the severity of observed challenge reactions would be repeated on rechallenge with a lower fat challenge vehicle. …

An Evaluation Of The Sensitivity Of Subjects With Peanut Allergy To Very Low Doses Of Peanut Protein: A Randomized, Double-Blind, Placebo-Controlled Food Challenge Study, Jonathan O'B. Hourihane, Sally A. Kilburn, Julie A. Nordlee, Susan L. Hefle, Steve L. Taylor, John O. Warner

Department of Food Science and Technology: Faculty Publications

The minimum dose of food protein to which subjects with food allergy have reacted in double-blind, placebo-controlled food challenges is between 50 and 100 mg. However, subjects with peanut allergy often report severe reactions after minimal contact with peanuts, even through intact skin. Objective: We sought to determine whether adults previously proven by challenge to be allergic to peanut react to very low doses of peanut protein. Methods: We used a randomized, double-blind, placebo-controlled food challenge of 14 subjects allergic to peanuts with doses of peanut ranging from 10 μg to 50 mg, administered in the form of a commercially …

Identification Of A Brazil-Nut Allergen In Transgenic Soybeans, Julie A. Nordlee, Steve L. Taylor, Jeffrey A. Townsend, Laurie A. Thomas, Robert K. Bush

Department of Food Science and Technology: Faculty Publications

Background: The nutritional quality of soybeans (Glycine max) is compromised by a relative deficiency of methionine in the protein fraction of the seeds. To improve the nutritional quality, methionine-rich 2S albumin from the Brazil nut (Bertholletia excelsa) has been introduced into transgenic soybeans. Since the Brazil nut is a known allergenic food, we assessed the allergenicity of the 2S albumin. Methods: The ability of proteins in transgenic and nontransgenic soybeans, Brazil nuts, and purified 2S albumin to bind to IgE in serum from subjects allergic to Brazil nuts was determined by radioallergosorbent tests (four subjects) and …

Allergenic Foods, Susan L. Hefle, Julie A. Nordlee, Steve L. Taylor

Department of Food Science and Technology: Faculty Publications

Virtually all food allergens are proteins, although only a small percentage of the many proteins in foods are allergens. Any food that contains protein has the potential to cause allergic reactions in some individuals. However, a few foods or food groups are known to cause allergies on a more frequent basis than other foods. At a 1995 consultation on food allergies sponsored by the Food and Agriculture Organization, a group of international experts confirmed that peanuts, soybeans, crustacea, fish, cow’s milk, eggs, tree nuts, and wheat are the most common allergenic foods. These foods are responsible for more than 90% …

A Sandwich Enzyme-Linked Immunosorbent Assay (Elisa) For The Quantitation Of Peanut In Foods, S. L. Taylor, J. A. Nordlee, S. L. Hefle

Department of Food Science and Technology: Faculty Publications

Peanuts are one of the most allergenic foods known. Strict avoidance of peanut by peanut-allergic individuals is difficult and often unsuccessful. Peanut proteins have previously been found in nonpeanut foodstuffs prepared on shared processing equipment, and such carryover contamination increases the risk of occurrence of allergic reactions. Immunoassays offer a specific, sensitive, and rapid technique to detect and quantitate small amounts of proteins in food systems.

A sandwich-type, enzyme-linked immunosorbent assay (ELISA) was developed for the detection of peanut protein in foods. Selected food samples were ground and extracts prepared by overnight extraction in 0.01 M phosphate buffered saline, followed …