Quantitative and kinetic analyses of peanut allergens as affected by food processing

Meng, Shi; Li, Jiaxu; Chang, Sam K. C.; Maleki, Soheila J.

doi:10.1016/j.fochx.2019.100004

Cited by 17 publications

(45 citation statements)

References 34 publications

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“…[7] All peanut proteins (Ara h 1, 2, 3, and 6) are water-soluble proteins. [23] It can be hypothesized that Ara h 1 and 3 are subjected to degradation by lysosomal proteases, which results in the degradation of IgE binding epitopes and subsequently in reduced IgE binding, whereas Ara h 2 and 6 are less degraded by lysosomal proteases. This hypothesis is supported by Smit et al who investigated the processing of peanut allergens in dendritic cells.…”

Section: Discussionmentioning

confidence: 99%

Digestion and Transport across the Intestinal Epithelium Affects the Allergenicity of Ara h 1 and 3 but Not of Ara h 2 and 6

Smits

Nooijen

Redegeld

et al. 2021

Molecular Nutrition Food Res

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Scope No accepted and validated methods are currently available which can accurately predict protein allergenicity. In this study, the role of digestion and transport on protein allergenicity is investigated. Methods and results Peanut allergens (Ara h 1, 2, 3, and 6) and a milk allergen (β‐lactoglobulin) are transported across pig intestinal epithelium using the InTESTine model and afterward basophil activation is measured to assess the (remaining) functional properties. Additionally, allergens are digested by pepsin prior to epithelial transport and their allergenicity is assessed in a human mast cell activation assay. Remarkably, transported Ara h 1 and 3 are not able to activate basophils, in contrast to Ara h 2 and 6. Digestion prior to transport results in a significant increase in mast cell activation of Ara h 1 and 3 dependent on the length of digestion time. Activation of mast cells by Ara h 2 and 6 is unaffected by digestion prior to transport. Conclusions Digestion and transport influences the allergenicity of Ara h 1 and 3, but not of Ara h 2 and 6. The influence of digestion and transport on protein allergenicity may explain why current in vitro assays are not predictive for allergenicity.

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Section: Discussionmentioning

confidence: 99%

Digestion and Transport across the Intestinal Epithelium Affects the Allergenicity of Ara h 1 and 3 but Not of Ara h 2 and 6

Smits

Nooijen

Redegeld

et al. 2021

Molecular Nutrition Food Res

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“…( 76 ), allergen Glycyrrhiza uralensis ( 64 ), hazelnut allergens ( 78 ), olive pollen allergens ( 2 ), raw and roasted peanut allergens ( 71 ), N-glycoforms of soybean allergenic glycoproteins ( 91 ), allergens from seeds of Ginkgo biloba ( 80 ), and almond and hazelnut allergens from roasted nut ( 20 ). Immunological analysis such as immunoblotting was also applied after SDS-PAGE separation e.g., to egg yolk allergens ( 26 ), peanut allergens ( 92 ), Carya illinoinensis (Wangenh.) allergen ( 93 ), Gly m 4, a soybean allergen ( 21 ), citrus fruit allergens ( 94 ), and tree nuts ( 95 ).…”

Section: Methods For the Detection And Analysis Of Allergensmentioning

confidence: 99%

Review of New Trends in the Analysis of Allergenic Residues in Foods and Cosmetic Products

Tuzimski

Petruczynik

2020

Journal of AOAC INTERNATIONAL

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Background Allergies represent an important health problem in industrialized countries. Allergen sensitization is an important risk factor for the development of allergic diseases; thus, the identification of an individual’s allergen sensitization is essential for the diagnosis and treatment of diseases. Objective This review compares different modern methods applied for the analysis of allergens in various matrices (from 2015 to the end of September 2019). Conclusions Immunological methods are still most frequently used for detection of allergens. These methods are sensitive, but the lack of specificity and cross-reaction of some antibodies can still be a relevant source of errors. DNA-based methods are fast and reliable for determination of protein allergens, but the epitopes of protein allergens with posttranslational modifications and their changes, originated during various processing, cannot be identified through the use of this method. Methods based on application of biosensors are very rapid and easy to use, and can be readily implemented as screening methods to monitor allergens. Recent developments of new high-resolution MS instruments are encouraging and enable development in the analysis of allergens. Fast, very sensitive, reliable, and accurate detection and quantification of allergens in complex samples can be used in the near future. Mass spectrometry coupled with LC, GC, or electrophoretic methods bring additional advances in allergen analysis. The use of LC-MS or LC-MS/MS for the quantitative detection of allergens in various matrices is at present gaining acceptance as a protein-based confirmatory technique over the routinely performed enzyme-linked immunosorbent assays.

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“…Relative to the research reports on the effects of food processing on peanut allergens, the processing effects on wheat allergens have been modestly studied (Blanc et al, 2011;Meng et al, 2019;Zhang et al, 2019). Wheat food products are made using two general types of processing methods to create commonly consumed foods (Table 1):…”

Section: Impact Of Food Processing On Wheat Allergenicity: Evidence From the Literaturementioning

confidence: 99%

Creating hypo‐/nonallergenic wheat products using processing methods: Fact or fiction?

Gao

Jorgensen

Raghunath

et al. 2021

Comp Rev Food Sci Food Safe

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Wheat allergy is a potentiallylife-threatening disease that affects millions of people around the world. Food processing has been shown to influence the allergenicity of wheat and other major foods. However, a comprehensive review evaluating whether or not food processing can be used to develop hypo-/nonallergenic wheat products is unavailable. There were three objectives for this study: (1) to critically evaluate the evidence on the effect of fermentation, thermal processing, and enzyme or acid hydrolysis on wheat allergenicity so as to identify the potential for and challenges of using these methods to produce hypo-/nonallergenic wheat products; (2) to identify the molecular effects of food processing needed to create such products; and (3) to map the concept questions for future research and development to produce hypo-/nonallergenic wheat products. We performed literature research using PubMed and Google Scholar databases with various combinations of keywords to generate the data to accomplish these objectives. We found that: (1) food processing significantly modulates wheat allergenicity; while some methods can reduce or even abolish the allergenicity, others can create mega allergens; and (2) fermentation and enzymatic hydrolysis hold the most potential to create novel hypo-/nonallergenic wheat products; however, preclinical validation and human clinical trials are currently lacking. We also identify five specific research concepts to advance the research to enable the creation of hypo-/nonallergenic wheat products for application in food, medical, and cosmetic industries.

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Quantitative and kinetic analyses of peanut allergens as affected by food processing

Cited by 17 publications

References 34 publications

Digestion and Transport across the Intestinal Epithelium Affects the Allergenicity of Ara h 1 and 3 but Not of Ara h 2 and 6

Digestion and Transport across the Intestinal Epithelium Affects the Allergenicity of Ara h 1 and 3 but Not of Ara h 2 and 6

Review of New Trends in the Analysis of Allergenic Residues in Foods and Cosmetic Products

Creating hypo‐/nonallergenic wheat products using processing methods: Fact or fiction?

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