Impact of food processing on the structural and allergenic properties of food allergens

Mills, E.N. Clare; Sancho, Ana I.; Rigby, Neil M.; Jenkins, John A.; Mackie, Alan

doi:10.1002/mnfr.200800236

Cited by 188 publications

(158 citation statements)

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“…Food processing may deeply affect the protein structure depending on the intrinsic characteristics of the protein, the severity of the treatment applied, and the environment where it takes place. In particular, thermal processing has the potential to modify the structure, solubility, and immunochemical reactivity of allergen proteins, affecting the conformation, epitope antigenicity, and hydrophobicity [21,30,31].…”

Section: Varietal Diversity Andmentioning

confidence: 99%

“…In addition, the conformational changes of the protein allergen structure occurring during the thermal process result in the formation of protein aggregates or oligomers, with decreased protein solubility [20,21]. In this regard, numerous methods to detect allergens contamination and/or to assess in vitro the allergenicity of specific ingredients rely on protein extraction systems.…”

Section: Introductionmentioning

confidence: 99%

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Effects of the Varietal Diversity and the Thermal Treatment on the Protein Profile of Peanuts and Hazelnuts

Angelis

Bavaro

Monaci

et al. 2018

Journal of Food Quality

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Several bu er compositions were compared for their e ciency in protein extraction from both raw and roasted peanut and hazelnut samples, the nal goal being to understand the modi cation of protein solubility upon roasting and maximize the extraction yield. Denaturant conditions provided by urea-TBS bu er resulted in satisfactory extraction yields for both peanut and hazelnut samples, before and after the thermal treatment. In addition, di erent varieties of peanuts and hazelnuts were characterized to highlight the extent of variability in the protein pro le accounted by the varietal factor and eventual di erential resistance among cultivars to protein modi cation induced by the thermal processing. e protein pro le was characterized by gel electrophoresis, and speci c bands were analyzed by micro-HPLC-MS/MS coupled to software-based protein identi cation. No signi cant di erence was observed for the investigated hazelnut cultivars, namely, Campana, Romana, and Georgia, whereas interesting features were presented for the peanut varieties Virginia, Zambia, and China. In particular, Zambia variety lacked two bands of approximately 36 and 24 kDa that were visible in Virginia and China varieties, which could suggest a lower allergenic potential of this particular variety which deserves to be further investigated before drawing nal conclusions.

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Section: Varietal Diversity Andmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Effects of the Varietal Diversity and the Thermal Treatment on the Protein Profile of Peanuts and Hazelnuts

Angelis

Bavaro

Monaci

et al. 2018

Journal of Food Quality

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“…A common feature of most legume allergens is their relative resistance to thermal, chemical, and proteolytic degradation (Lalles and Peltre, 1996;Mills et al, 2009 After harsh industrial processing involving mechanical, high-pressure homogenisation and lyophilisation and thermal (200 °C for 30 minutes) treatments, α-, β-, and δ-conglutin were still able to release stable IgE-binding peptides (Sirtori et al, 2010). However, the in vitro IgE-binding of lupin was reduced when an instantaneous controlled pressure drop was applied to lupin cotyledons (Guillamon et al, 2008).…”

Section: Effects Of Food Processing On Allergenicitymentioning

confidence: 99%

Scientific Opinion on the evaluation of allergenic foods and food ingredients for labelling purposes

Products¹

2014

EFS2

101

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Following a request from the Food Safety Authority of Ireland, the EFSA Panel on Dietetic Products, Nutrition and Allergies (NDA Panel) was asked to deliver a scientific opinion on the evaluation of allergenic foods and food ingredients for labelling purposes. In view of the request, the NDA Panel decided to update its previous opinions relative to food ingredients or substances with known allergenic potential listed in Annex IIIa of 2003/89/EC, as amended. These include cereals containing gluten, milk and dairy products, eggs, nuts, peanuts, soy, fish, crustaceans, molluscs, celery, lupin, sesame, mustard and sulphites. The opinion relates to immunoglobulin (Ig)E-and non-IgE-mediated food allergy, to coeliac disease and to adverse reactions to sulphites in food, and it does not address non-immune-mediated adverse reactions to food. It includes information on the prevalence of food allergy in unselected populations, proteins identified as food allergens, cross-reactivities, the effects of food processing on the allergenicity of foods and ingredients, methods for the detection of allergens and allergenic foods, doses observed to trigger adverse reactions in sensitive individuals and risk assessment methodologies that have been used to derive individual and population thresholds for selected allergenic foods. The present opinion relates to immunoglobulin (Ig)E-and non-IgE-mediated food allergy, to coeliac disease and to adverse reactions to sulphites in food, and it does not address non-immune-mediated adverse reactions to food. For each food ingredient or substance listed in Annex IIIa, it includes information on the prevalence of food allergy in unselected populations, on proteins identified as food allergens, on cross-reactivities, on the effects of food processing on the allergenicity of foods and ingredients, on methods for the detection of allergens and allergenic foods, and on doses observed to trigger adverse reactions in sensitive individuals.Immune-mediated adverse reactions to foods manifest with clinical signs and symptoms of variable severity and duration, which may affect different organs and systems. Anaphylactic reactions to food are IgE mediated and may occur at any age. Non-IgE-mediated food allergy includes a wide range of diseases, including protein-induced enterocolitis and eosinophilic oesophagitis.A careful family and clinical history are the basis for diagnosis of food allergy. Food diaries, skin prick tests (SPTs), allergen-specific IgE measurements, food elimination diets and food challenges are part of the standard protocol for the diagnosis of food allergy. A positive SPT indicates sensitisation to the tested food, but it is not diagnostic of food allergy. Allergen-specific serum IgE antibodies similarly denote sensitisation to a particular food, but they are not diagnostic without a clinical history or food challenge. The use of atopy patch tests for the diagnosis of food allergy is controversial. Other available tests have no current role in the diagnosis of food allergy. Diag...

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“…Food processing may destroy existing IgEbinding epitopes on a protein or conversely generate (neoallergen formation) new ones as a result of changes in protein conformation (Mills et al, 2009;Sathe et al, 2005). These changes may affect allergic sensitization to food proteins and the elicitation of allergic reactions in sensitized individuals.…”

Section: Assessing the Effect Of Processing On Allergenicity Of Food mentioning

confidence: 99%

Use of a rat basophil leukemia (RBL) cell-based immunological assay for allergen identification, clinical diagnosis of allergy, and identification of anti-allergy agents for use in immunotherapy

Sun

Zhou

Zhou³

et al. 2014

Journal of Immunotoxicology

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(2015) Use of a rat basophil leukemia (RBL) cell-based immunological assay for allergen identification, clinical diagnosis of allergy, and identification of anti-allergy agents for use in immunotherapy, Journal of Immunotoxicology, 12:2, 199-205, DOI: 10.3109/1547691X.2014 AbstractFood allergy is an important public health problem that affects an estimated 8% of young children and 2% of adults. With an increasing interest in genetically-engineered foods, there is a growing need for development of sensitive and specific tests to evaluate potential allergenicity of foods and novel proteins as well as to determine allergic responses to ensure consumer safety. This review covers progress made in the field of development of cell models, specifically that involving a rat basophil leukemia (RBL) cell-based immunoassay, for use in allergen identification, diagnosis, and immunotherapy. The RBL assay has been extensively employed for determining biologically relevant cross-reactivities of food proteins, assessing the effect of processing on the allergenicity of food proteins, diagnosing allergic responses to whole-food products, and identifying anti-allergy food compounds. From the review of the literature, one might conclude the RBL cell-based assay is a better test system when compared to wild-type mast cell and basophil model systems for use in allergen identification, diagnosis, and analyses of potential immunotherapeutics. However, it is important to emphasize that this assay will only be able to identify those allergens to which the human has already been exposed, but will not identify a truly novel allergen, i.e. one that has never been encountered as in its preferred (humanized) configuration.

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Impact of food processing on the structural and allergenic properties of food allergens

Cited by 188 publications

References 51 publications

Effects of the Varietal Diversity and the Thermal Treatment on the Protein Profile of Peanuts and Hazelnuts

Effects of the Varietal Diversity and the Thermal Treatment on the Protein Profile of Peanuts and Hazelnuts

Scientific Opinion on the evaluation of allergenic foods and food ingredients for labelling purposes

Use of a rat basophil leukemia (RBL) cell-based immunological assay for allergen identification, clinical diagnosis of allergy, and identification of anti-allergy agents for use in immunotherapy

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