ArticleEuropean journal of nutrition2013
Effect of Maillard reaction on biochemical properties of peanut 7S globulin (Ara h 1) and its interaction with a human colon cancer cell line (Caco-2).
Article in European journal of nutrition, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 42 citations in OpenAlex.
- Structural Property, Immunoreactivity and Gastric Digestion Characteristics of Glycated Parvalbumin from Mandarin Fish (Foods (Basel, Switzerland) · 2022Article
- Comprehensive Analysis of the Structure and Allergenicity Changes of Seafood Allergens Induced by Non-Thermal Processing: A Review.Molecules (Basel, Switzerland) · 2022Review
- In Silico Analysis and Functional Characterization of Antimicrobial and Insecticidal Vicilin from Moth Bean (Molecules (Basel, Switzerland) · 2022Article
- Are Physicochemical Properties Shaping the Allergenic Potency of Plant Allergens?Clinical reviews in allergy & immunology · 2022Review
- Supercritical COJDS communications · 2021Article
- Circulating antibodies against age-modified proteins in patients with coronary atherosclerosis.Scientific reports · 2020Article
- Effects of different thermal processing methods on the structure and allergenicity of peanut allergen Ara h 1.Food science & nutrition · 2018Article
- Food Processing: The Influence of the Maillard Reaction on Immunogenicity and Allergenicity of Food Proteins.Nutrients · 2017Review
- Enhanced Approaches for Identifying Amadori Products: Application to Peanut Allergens.Journal of agricultural and food chemistry · 2016Article
- The molecular basis of peanut allergy.Current allergy and asthma reports · 2014Article
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
purposeThe purpose of this study was to determine the influence of Maillard reaction (MR, glycation) on biochemical and biological properties of the major peanut allergen Ara h 1.
methodsThree different time/temperature conditions of treatment were applied (37, 60, and 145 °C). The extent of MR was assessed by SDS-PAGE, loss of free amino groups, fluorescence intensity, content of bound sugar and fructosamine. The Caco-2 model system was applied to study effects of hydrolysed and non-hydrolysed Ara h 1 on proliferation and interleukin-8 (IL-8) secretion from Caco-2 cells.
resultsWe demonstrated significant differences in the biochemical properties of Ara h 1 glycated at different time/temperature conditions. Glycation of Ara h 1 at 37 °C was shown to cause least biochemical changes, not limiting pepsin hydrolysis. Loss of free amino groups, increase of fluorescence and brown colour of Ara h 1 glycated at 60 and 145 °C indicated advanced and final stages of MR. Non-treated Ara h 1 inhibited Caco-2 cell proliferation and stimulated IL-8 secretion. This effect was less pronounced for glycated Ara h 1. Incubation of Caco-2 cells with non-hydrolysed Ara h 1, glycated at the temperature of 37 and 60 °C, did not stimulate IL-8 secretion.
conclusionEach applied time/temperature-treatment combination caused different biochemical changes of Ara h 1, underlining diversity of formed MRPs. MR, independently of temperature/time conditions, reduced the pro-inflammatory properties of native Ara h 1, reflected in stimulation of IL-8 secretion from intestinal epithelial cells.
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