Stability of sunflower 2S albumins and LTP to physiologically relevant in vitro gastrointestinal digestion

Berecz, Bernadett; Mills, E. N. Clare; Parádi, István; Láng, F.; Tamás, László; Shewry, Peter R.; Mackie, Alan

doi:10.1016/j.foodchem.2012.12.034

Cited by 25 publications

(20 citation statements)

References 28 publications

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Section: Discussionmentioning

confidence: 99%

“…The respective protein families, 2S albumins and LTPs, are commonly classified as particularly resistant against heat and protease treatment, given their closely packed molecular structure and stabilizing disulfide bonds [45,46]. A high stability against in vitro digestion has been described for 2S albumins and LTPs from several allergenic foods [23,25,49,50]. Concerning the digestion of hazelnut allergens, Vieths et al also observed a high resistance of the prolamin fraction, with retained IgE binding for proteins in the prolamin molecular size range [20], and Pfeifer et al recently reported that isolated Cor a 14 withstood simulated gastric and intestinal digestion [51].…”

Section: Differential Stability Of Allergen Super(families) Under Gasmentioning

confidence: 99%

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Gastrointestinal digestion of hazelnut allergens on molecular level: Elucidation of degradation kinetics and resistant immunoactive peptides using mass spectrometry

Korte

Bräcker

Brockmeyer

2017

Molecular Nutrition Food Res

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We present a comprehensive survey on the gastrointestinal digestion of a relevant allergenic food on level of the peptidome, including the first systematic characterization and quantification of degradation products. This provides information on the differential resistance of plant food allergens and their structural elements undergoing digestion and forms the basis for a deeper understanding of the molecular principles responsible for sensitization to food allergy.

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Section: Discussionmentioning

confidence: 99%

Section: Differential Stability Of Allergen Super(families) Under Gasmentioning

confidence: 99%

Gastrointestinal digestion of hazelnut allergens on molecular level: Elucidation of degradation kinetics and resistant immunoactive peptides using mass spectrometry

Korte

Bräcker

Brockmeyer

2017

Molecular Nutrition Food Res

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“…The presence of bands around 3 and 8 kDa demonstrated that there are some proteins resistant to these enzymes up to 8 h. In the Figure 5B the crude extract sample was crisp and incubated with trypsin/chymotrypsin. In this condition These resistant proteins have been reported as 2S albumins and are related in various species, including peanut, mustard, Brazil nut, sesame seed and sunflower (Murtagh et al, 2003;Moreno et al, 2005;Vissers et al, 2011;Orruno & Morgan, 2011;Sirvent et al, 2012;Berecz et al, 2013).…”

Section: Seed Extract Toasted Simulating Gastric and Intestinal Fluidmentioning

confidence: 93%

Anti-nutritional factors and digestibility of protein in Cayocar brasiliense seeds

et al. 2017

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The Brazilian Cerrado presents a wide variety of natural products, including the Pequi (Caryocar brasiliense). The important factor that determines the dietary and nutritional ideality of protein is degestitibility. This work aims to evaluate the protein digestibility of Pequi seeds and the presence of anti-nutritional factors. The protein Pequi almonds were extracted, toasted and untoasted. Evaluation digestibility was structurally characterized by SDS-PAGE 15%, which can be used to analyze simulated gastric fluid (SFG) and digestion in intestinal fluid (SFI) in the presence of pepsin and trypsin/chymotrypsin. The extract from Pequi almonds showed inhibitory activity and was not detected hemagglutination. The intensity of the bands according to 2S albumins, after heat treatment, did not decrease in comparison to the condition native, significantly. In the crisp crude extract, which was incubated under SGF and SIF, the intensity of the corresponding bands at 8 and 3 kDa was resistant to SGF and indigestible after 4 hours under SIF. The characterization of Pequi almonds demonstrated that the product of the crude extract has anti-nutritional factors, which were confirmed by evaluating digestibility.Keywords: Caryocar brasiliense; almonds; in vitro digestibility; 2S albumin; peptidase inhibitor; lectins.Practical Application: The study of anti-nutritional factors identification is very important because of its inactivation on food industry and it can also be used to avoid allergy due to them.

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“…There was a report of anaphylaxis to Helianthus pollen contaminated commercial peeled sunflower seeds in a patient sensitized to mugwort pollen, and another of oral allergy syndrome to sunflower seeds in a case of airborne allergy to pet food seed particles. Helianthus annuus belongs to the Asteraceae family and its pollen allergen component Hel a 4 is an Art v 1-like allergen [44][45][46] . In a recent case of anaphylaxis after consumption of sunflower seeds, in an adult patient with IgE sensitization to mugwort pollen, hypersensitivity to Hel a 3 LTP and defensin-like proteins, both crossreactive with Artemisia vulgaris pollen allergen components, were suspected as a cause of anaphylaxis 47 .…”

Section: Pollen Allergens In Foodsmentioning

confidence: 99%

The presence of aeroallergens in food products: a potential risk for the patient with allergic rhinitis

Popescu

Vieru

2018

Romanian Journal of Rhinology

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Clinical entities of food allergy in allergic rhinitis patients due to IgE-sensitization to cross-reactive aeroallergen and food allergen components are well described, but less data are available regarding allergic reactions to foods containing aeroallergens, either due to food contamination, such as oral mite anaphylaxis, or due to their natural presence in the edible products, such as pollen grains in honey and bee products. There are some potential risks for allergic rhinitis subjects due to ingestion of food products containing domestic mite, insect, fungal and pollen allergens. The knowledge of these risks is useful for the allergists and ENT specialists, especially in the context of climate changes with warmer periods facilitating mite growth in flours, and of increase use of phytotherapy and apitherapy products containing pollen grains.

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Stability of sunflower 2S albumins and LTP to physiologically relevant in vitro gastrointestinal digestion

Cited by 25 publications

References 28 publications

Gastrointestinal digestion of hazelnut allergens on molecular level: Elucidation of degradation kinetics and resistant immunoactive peptides using mass spectrometry

Gastrointestinal digestion of hazelnut allergens on molecular level: Elucidation of degradation kinetics and resistant immunoactive peptides using mass spectrometry

Anti-nutritional factors and digestibility of protein in Cayocar brasiliense seeds

The presence of aeroallergens in food products: a potential risk for the patient with allergic rhinitis

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