Antigenicity of the proteins in soy lecithin and soy oil in soybean allergy

Awazuhara, Hiroko; Kawai, Hideki; M, Baba; Matsui, T; Komiyama, Atsushi

doi:10.1046/j.1365-2222.1998.00431.x

Cited by 68 publications

(53 citation statements)

References 16 publications

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“…The method of Awazuhara et al [4], with slight modification, was used for the isolation of proteins from soy lecithin. For a typical isolation, 4.0 g of lecithin was homogenized in 24 ml of n-hexane-isopropyl alcohol-deionized water (3:2:1) by vortexing or shaking.…”

Section: Methodsmentioning

confidence: 99%

“…The 39-kD protein was identified as a soy glycinin based on immunoblotting with a glycinin monoclonal antibody. Awazuhara et al [4]investigated proteins in soy lecithin and oil and found 28 and 0.04 ppm, respectively, in these materials. Numerous protein bands from 14 to 70 kD were observed on Coomassie-stained SDS-PAGE gels.…”

Section: Introductionmentioning

confidence: 99%

“…While the amount of protein found in soy lecithin is relatively low (typically 100–500 ppm), IgE-binding proteins are among those present in this material [4, 5]. These proteins represent a potential concern because soy protein is classified as a major allergenic food, along with eggs, cow’s milk, peanuts, wheat and fish [6, 7].…”

Section: Introductionmentioning

confidence: 99%

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Identification of IgE-Binding Proteins in Soy Lecithin

Gu¹,

Beardslee

Zeece³

et al. 2001

Int Arch Allergy Immunol

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Background: Soy lecithin is widely used as an emulsifier in processed foods, pharmaceuticals and cosmetics. Soy lecithin is composed principally of phospholipids; however, it has also been shown to contain IgE-binding proteins, albeit at a low level. A few clinical cases involving allergic reactions to soy lecithin have been reported. The purpose of this investigation is to better characterize the IgE-binding proteins typically found in lecithin. Methods: Soy lecithin proteins were isolated following solvent extraction of lipid components and then separated on sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). The separated lecithin proteins were immunoblotted with sera from soy-sensitive individuals to determine the pattern of IgE-binding proteins. The identity of IgE-reactive bands was determined from their N-terminal sequence. Results: The level of protein in six lecithin samples obtained from commercial suppliers ranged from 100 to 1,400 ppm. Lecithin samples showed similar protein patterns when examined by SDS-PAGE. Immunoblotting with sera from soy-sensitive individuals showed IgE binding to bands corresponding to 7, 12, 20, 39 and 57 kD. N-terminal analysis of these IgE-binding bands resulted in sequences for 3 components. The 12-kD band was identified as a methionine-rich protein (MRP) and a member of the 2S albumin class of soy proteins. The 20-kD band was found to be soybean Kunitz trypsin inhibitor. The 39-kD band was matched to a soy protein with unknown function. Conclusions: Soy lecithin contains a number of IgE-binding proteins; thus, it might represent a source of hidden allergens. These allergens are a more significant concern for soy-allergic individuals consuming lecithin products as a health supplement. In addition, the MRP and the 39-kD protein identified in this study represent newly identified IgE-binding proteins.

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Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Identification of IgE-Binding Proteins in Soy Lecithin

Gu¹,

Beardslee

Zeece³

et al. 2001

Int Arch Allergy Immunol

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“…A small number of studies describe the immunochemical characterisation of non-refined (Awazuhara et al, 1998;Paschke et al, 2001) and N/RBD oils (Zitouni et al, 2001;Errahali et al, 2002;Montagnon et al, 2003). The observed binding pattern in non-refined oils (Paschke, 2001) was similar to that of N/RBD oils with 2 binding activities at 28 kDa and 56 kDa described by the French authors (Zitouni et al, 2001;Errahali et al, 2002;Montagnon et al, 2003).…”

Section: Immunochemical Methodologiesmentioning

confidence: 99%

Opinion of the Panel on dietetic products, nutrition and allergies [NDA] related to a notification from Cognis, ADM and Cargill on natural mixed tocopherols (E306), natural D‐alpha tocopherol, natural D‐alpha tocopherol acetate and natural D‐alpha tocopherol succinate from soybean sources pursuant to Article 6, paragraph 11 of Directive 2000/13/EC

Products¹

2007

EFS2

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SUMMARYSoy is a common dietary constituent and allergic reactions to soy proteins are well described. Soy allergy prevalence studies are lacking, estimated prevalences are about 0.5% in the general population with about 3-6% of allergic children being allergic to soy proteins. Clinical reactions are similar to those observed with other major food allergens, such as milk, egg or peanut and include systemic anaphylaxis.The application covers natural mixed tocopherols (vitamin E, E306) and a range of D-alpha tocopherols derived from vegetable oil (soybean oil). Natural mixed tocopherols are mainly used as antioxidants in fatty foods at a concentration of about 50 mg/kg (referring to the fat fraction of the specific food). This corresponds to an intake of about 0.03µg soy protein assuming a fat intake of 60-80 g/day (3-4 mg tocopherols). Natural mixed tocopherols are also used as dietary supplements. Natural mixed tocopherols and D-alpha tocopherols under consideration are derived from soybean oil deodorised distillates.The applicant has conducted analytical studies which have improved sensitivity and specificity of protein analysis. In a clinical study in 32 soy allergic patients, none reacted during skin testing to tocopherols and 31 did not reveal any adverse allergic reaction to a maximum dose of 500 mg mixed tocopherols. One patient reported oral allergy symptoms. The Panel considers that this clinical study is insufficient to predict the likelihood that the product may trigger an allergic reaction in susceptible individuals.Considering the information provided by the applicant regarding the starting material, the subsequent production process, and the demonstration of low residual protein content, the Panel considers that it is unlikely that natural mixed tocopherol/D-alpha tocopherols from soybean sources will trigger a severe allergic reaction in susceptible individuals.

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“…However, a small number of studies describe the immunochemical characterisation of nonrefined (Awazuhara et al, 1998;Paschke, 2001) and N/RBD oils (Zitouni, 2001;Errahali, 2002;Montagnon, 2003). The observed binding pattern in non-refined oils (Paschke, 2001) was similar to that of N/RBD oils with 2 binding activities at 28 kDa and 56 kDa described by the French authors (Zitouni, 2001;Errahali, 2002;Montagnon, 2003).…”

Section: Immunochemical Methodologiesmentioning

confidence: 99%

Opinion of the NDA Panel related to a notification from Raisio Life Sciences on plant stanol esters produced from soybean oil sterols pursuant to Article 6 paragraph 11 of Directive 2000/13/EC

2005

EFSA Journal

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Antigenicity of the proteins in soy lecithin and soy oil in soybean allergy

Abstract: Proteins present in soy lecithin and soy oil have little antigenicity with regard to soybean allergy.

Cited by 68 publications

References 16 publications

Identification of IgE-Binding Proteins in Soy Lecithin

Identification of IgE-Binding Proteins in Soy Lecithin

Opinion of the NDA Panel related to a notification from Raisio Life Sciences on plant stanol esters produced from soybean oil sterols pursuant to Article 6 paragraph 11 of Directive 2000/13/EC

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