Influence of peanut matrix on stability of allergens in gastric‐simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion‐resistant peptides

Prodić, Ivana; Stanić-Vučinić, Dragana; Apostolović, Danijela; Mihailović, Jelena; Radibratović, Milica; Radosavljević, Jelena; Burazer, Lidija; Milčić, Miloš K.; Smiljanić, Katarina; Hage, Marianne van; Veličković, Tanja Ćirković

doi:10.1111/cea.13113

Cited by 43 publications

(56 citation statements)

References 30 publications

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“…The Ara h 3 isoforms were even identified in raw and roasted peanut after 120 min digestion processing by mass spectrometry. This finding coincides with the previous report that Ara h 3 contains a core region predicted to be preserved upon digestive enzyme attack in the gastrointestinal tract (Koppelman et al, 2010;Prodic et al, 2018a).…”

Section: Discussionsupporting

confidence: 93%

“…Purified Ara h 1 and Ara h 2 were more resistant to digestive enzymes and heat than the untreated allergens (Maleki, Chung, Champagne, & Raufman, 2003). Compared to these existing works (Mandalari et al, 2014;Moreno, 2007;Prodic et al, 2018b), the whole peanut matrix which contains around 20% protein, 50% lipids and dietary fibre may affect allergen conformation during heating and digestibility during the digestion process. It can be seen in the comparison of thermally processed peanuts that not all food allergens are resistant to heating.…”

Section: Discussionmentioning

confidence: 96%

“…Most of that related to the effects of processing or gastrointestinal digestion on immunoreactivity focused on purified peanut allergens or peanut extracts. Regardless of different digestion model, Ara h 2/6 showed higher pepsin resistance compared to Ara h 1 and Ara h 3 (Apostolovic et al, 2016;Prodic et al, 2018a). However, the effect of thermal processing on the digestion and immunogenic potential of allergenic proteins in whole peanut matrix is poorly investigated so far.…”

Section: Introductionmentioning

confidence: 99%

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In vitro digestibility and immunoreactivity of thermally processed peanut

Rao

Tian

et al. 2018

Food and Agricultural Immunology

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Food processing affects the bioavailability and immunoreactivity of allergens. However, there was a lack of the combined study of the influence of the processing and gastrointestinal digestion on peanut matrix. Digestibility of peanut matrices was assessed by using an in vitro digestion model and monitored by SDS-PAGE, immunoblotting with polyclonal antibody and serum from peanut-allergic patients. The IgE-binding ability of digested samples will be assessed by immunoassay. Peanut proteins were digested by pepsin after only 2 min which was accompanied by a loss of high molecular weight proteins and enrichment in polypeptides with molecular weight lower than 10 kDa. Ara h 1 and Ara h 3 were partly proteolysis, and Ara h 2/6 containing a digestion-resistant fragment. All soluble fractions after 120 min gastric digestion reduced a higher IgE-binding ability than that after 10 min. Our findings provide a more realistic picture, considering the role of food processing and food matrix. ARTICLE HISTORY

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Section: Discussionsupporting

confidence: 93%

Section: Discussionmentioning

confidence: 96%

Section: Introductionmentioning

confidence: 99%

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In vitro digestibility and immunoreactivity of thermally processed peanut

Rao

Tian

et al. 2018

Food and Agricultural Immunology

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“…Peanut allergens Ara h 1, Ara h 2, and, Ara h 3 are considered as major peanut allergens, and they also comprise the major proportion of peanut protein (Koppelman et al, 2001;Wu et al, 2016). Now days, Ara h 6 is also thought of as a major peanut allergen because of its similarity to Ara h 2 and recognition by serum IgE from allergic individuals (Koppelman, Hefle, Taylor, & De Jong, 2010;Kukkonen, Pelkonen, Mäkinen-Kiljunen, Voutilainen, & Mäkelä, 2015;Prodic et al, 2018). Besides the major/potent peanut allergens, research indicates that some other minor allergens can also potentially cause life-threatening symptoms, while other allergens may only cause oral symptoms (Arkwright, Summers, Riley, Alsediq, & Pumphrey, 2013;Mittag et al, 2004;Petersen et al, 2014).…”

Section: Molecular Characteristics Of Peanut Allergensmentioning

confidence: 99%

Peanut Allergy: Characteristics and Approaches for Mitigation

Shah

Shi

Ashley

et al. 2019

Comp Rev Food Sci Food Safe

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Peanut allergy has garnered significant attention because of the high sensitization rate, increase in allergy, and severity of the reaction. Sufficiently reliable therapies and efficient mitigating techniques to combat peanut allergy are still lacking. Current management relies on avoiding peanuts and nuts and seeds with homologous proteins, although adverse events mostly occur with accidental ingestion. There is a need for hypoallergenic peanut products to protect sensitized individuals and perhaps serve as immunotherapeutic products. Alongside traditional practices of thermal and chemical treatment, novel processing approaches such as high‐pressure processing, pulsed ultraviolet light, high‐intensity ultrasound, irradiation, and pulsed electric field have been performed toward reducing the immunoreactivity of peanut. Covalent and noncovalent chemical modifications to proteins also have the tendency to alter peanut allergenicity. Enzymatic hydrolysis seems to be the most advantageous technique in diminishing the allergenic potential of peanut. Furthermore, the combined processing approach (hurdle technologies) such as enzymatic hydrolysis followed by, or in conjunction with, roasting, high pressure and heat, ultrasound with enzymatic treatment, or germination have shown a significant reduction of peanut immunoreactivity and may emerge as useful techniques in reducing the allergenicity of peanut and other foods. This study represents our current knowledge about the alterations in allergenic properties of peanut via different processing mechanisms as well as evaluating its future potential, geographical based data on increasing sensitization, clinical relevance, eliciting dose, and current management of peanut allergy. Furthermore, the molecular characteristics and clinical relevance of peanut allergens have been discussed.

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“…Also in this issue of the Journal, Prodic et al have examined the digestion products of the major peanut allergens and assessed their potential to elicit an IgE response. The Ara h 2 and Ara h 6 proteins remained largely intact.…”

mentioning

confidence: 99%