High-Oleic Peanuts Are Not Different from Normal Peanuts in Allergenic Properties

Chung, Si-Yin; Maleki, Soheila J.; Champagne, Elaine T.; Buhr, K. L.; Gorbet, D. W.

doi:10.1021/jf011132u

Cited by 22 publications

(31 citation statements)

References 28 publications

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“…During the roasting process, lipid oxidations with various biochemical reactions occur (Chung et al, 2002;Liu et al, 2011) aside from the Maillard reactions. Peanut is an oil plant with a lipid content of about 50% (Özcan, 2010).…”

Section: Discussionmentioning

confidence: 99%

Roasting and lipid binding provide allergenic and proteolytic stability to the peanut allergen Ara h 8

Petersen

Rennert

Kull

et al. 2013

Biological Chemistry

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Ara h 8 is the peanut allergen homologous to the birch pollen allergen Bet v 1. Because Bet v 1 has been shown to bind lipophilic ligands, the aim of this investigation was to determine the impact of lipid binding and roasting on the Ara h 8 structure and their influences on allergenicity. For the characterization of natural Ara h 8 (nAra h 8) from roasted and unroasted peanuts, circular dichroism spectroscopy, hydrophobic binding assay, immunohistochemistry, and immunoblot with sera of peanut allergic patients were performed and compared with results from recombinant Ara h 8 (rAra h 8) and Bet v 1. rAra h 8 displayed stronger hydrophobicity than rBet v 1. Patients' sera showed IgE reactivity with rAra h 8 and nAra h 8 from roasted peanuts, whereas fewer sera recognized nAra h 8 from unroasted peanuts. Simulated gastric digestion experiments demonstrated low proteolytic stability of rAra h 8, whereas the stability of nAra h 8 was increasingly higher in unroasted and roasted peanuts. The results demonstrate that IgE reactivity and thermal and proteolytic stability are reinforced in nAra h 8 after roasting, most likely due to Maillard reactions, lipid oxidations, and lipophilic associations. These aspects must be considered when estimating the allergenicity of Bet v 1-homologous proteins.

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Section: Discussionmentioning

confidence: 99%

Roasting and lipid binding provide allergenic and proteolytic stability to the peanut allergen Ara h 8

Petersen

Rennert

Kull

et al. 2013

Biological Chemistry

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“…Free amino groups of peanut bind to phosphate groups of phytic acids and contribute to complex formation. During roasting, these free amino groups may become unavailable and hence binding with the phosphate group of phytic acid becomes impossible [50,51].…”

Section: Treatment With Phytic Acidmentioning

confidence: 99%

Peanut proteins: Applications, ailments and possible remediation

Ghatak

Sen

2013

Journal of Industrial and Engineering Chemistry

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“…There were three runner-type peanut genotypes: Georgia Green, A100 and SunOleic 97R, and two Spanish type peanut genotypes: GT-C9 and GT-C20. SunOleic 97R, as a control, was only used in adducts and IgE binding assays [14]. To avoid the effects of different locations, all genotypes were grown in 2004, Bellflower Farm, Tifton, GA.…”

Section: Plant Materialsmentioning

confidence: 99%

“…IgE binding to peanuts was determined in an indirect ELISA as described [14]. Each sample was repeated 3 times (n = 3).…”

Section: Assay Of Ige Binding To Peanutsmentioning

confidence: 99%

See 1 more Smart Citation

Proteomic Analysis of Peanut Seed Storage Proteins and Genetic Variation in a Potential Peanut Allergen

Guo¹,

Liang²,

Chung³

et al. 2008

PPL

Self Cite

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Peanut allergy is one of the most severe food allergies. One effort to alleviate this problem is to identify peanut germplasm with lower levels of allergens which could be used in conventional breeding to produce a less allergenic peanut cultivar. In this study, we identified one peanut line, GT-C9, lacking several seed proteins, which were identified as Ara h 3 isoforms by peptide sequencing and named iso-Ara h 3. Total seed proteins were analyzed by one-dimensional (SDS-PAGE) and two-dimensional gel electrophoreses (2-D PAGE). The total protein extracts were also tested for levels of protein-bound end products or adducts such as advanced glycation end products (AGE) and N-(carboxymethyl) lysine (CML), and IgE binding. Peanut genotypes of GT-C9 and GT-C20 exhibited significantly lower levels of AGE adducts and of IgE binding. This potential peanut allergen iso-Ara h 3 was confirmed by peptide sequences and Western blot analysis using specific anti-Ara h 1, Ara h 2, and Ara h 3 antibodies. A full-length sequence of iso-ara h 3 (GenBank number DQ855115) was obtained. The deduced amino acid sequence iso-Ara h 3 (ABI17154) has the first three of four IgE-binding epitopes of Ara h 3. Anti-Ara h 3 antibodies reacted with two groups of protein peptides, one with strong reactions and another with weak reactions. These peptide spots with weak reaction on 2-D PAGE to anti-Ara h 3 antibodies are subunits or isoallergens of this potential peanut allergen iso-Ara h 3. A recent study suggested that Ara h 3 basic subunits may be more significant allergenicity than the acidic subunits.

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High-Oleic Peanuts Are Not Different from Normal Peanuts in Allergenic Properties

Cited by 22 publications

References 28 publications

Roasting and lipid binding provide allergenic and proteolytic stability to the peanut allergen Ara h 8

Roasting and lipid binding provide allergenic and proteolytic stability to the peanut allergen Ara h 8

Peanut proteins: Applications, ailments and possible remediation

Proteomic Analysis of Peanut Seed Storage Proteins and Genetic Variation in a Potential Peanut Allergen

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