The effect of roasting on peanut allergens’ digestibility, allergenicity, and structure

Zhou, Hongfei; Wu, Zhihua; Chang, Xuejiao; Yuan, Juanli; Li, Xin; Yang, Anshu; Tong, Ping

doi:10.1016/j.fbio.2021.101454

Cited by 15 publications

(13 citation statements)

References 47 publications

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“…Linear epitopes play an essential role in food allergens because they can still partially exist to bond with a specific antibody after food allergens have been digested by the human gastrointestinal tract. 34 In addition to linear epitopes, conformational epitopes play an important part in the allergenicity of an allergen. 35 Hence, four conformational mimotopes and nine linear mimotopes were predicted using bioinformatic tools.…”

Section: Discussionmentioning

confidence: 99%

Identification of linear epitopes and their major role in the immunoglobulin E-binding capacity of tropomyosin from Alectryonella plicatula

Han

et al. 2022

Food Funct.

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Section: Discussionmentioning

confidence: 99%

Identification of linear epitopes and their major role in the immunoglobulin E-binding capacity of tropomyosin from Alectryonella plicatula

Han

et al. 2022

Food Funct.

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“…29 The IgE binding capacity was estimated by an indirect competitive enzyme-linked immunosorbent assay (ELISA) with human antisera. 13 The 96-well microplate was percolated with nAra h 2 (100 μL per well, 0.25 μg/mL) overnight. Then, 60 μL of anti-Ara h 2 IgE (1:300 diluted human sera pooled) and 60 μL of Ara h 2 were added to the wells after blocking, and the plates incubated for 1 h. Unbound IgE was then removed from microplate wells; 100 μL of goat anti-human IgE-HRP conjugate (1:2000 diluted IgE conjugate) was added, and the mixture was incubated for 1 h. After the color development was terminated, the absorbance was determined at 450 nm by using a microplate reader (model 1860, Bio-Rad).…”

Section: ■ Materials and Methodsmentioning

confidence: 99%

“…12 Structural changes are significant factors that lead to allergic changes in peanut allergens. 13 Processing can reduce Ara h 2 allergenicity by changing its structure. After samples had been boiled at 100 °C for 20 min, the α-helical and random coil content in Ara h 2 decreased and the β-sheet and β-turn content increased.…”

Section: ■ Introductionmentioning

confidence: 99%

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Effect of Structural Targeted Modifications on the Potential Allergenicity of Peanut Allergen Ara h 2

Zhou

Ren

Zhang

et al. 2022

J. Agric. Food Chem.

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Protein structure affects allergenicity, and critical structural elements, especially conformational epitopes that determine allergenicity, have attracted a great deal of interest. In this study, we aimed to identify the localized structure that affects the potential allergenicity of protein by making targeted modifications of Ara h 2 and comparing the structure and allergenicity of mutants with those of the wide-type allergen. The structures of the allergen and its mutants were characterized by circular dichroism and ultraviolet absorption spectroscopy and simulated by molecular dynamics. The allergenicity was assessed by Western blotting, an indirect competitive enzyme-linked immunosorbent assay, a cell model, and a mouse model. Then, the structures that affect allergenicity were analyzed and screened. Our results showed that mutations in amino acids changed the nearby localized structure and the overall structures. The structural changes affected the IgE binding capacity of the allergen and reduced its potential allergenicity. The solvent accessible surface area (SASA) of aromatic residues was positively correlated with the IgE binding capacity. The integrity of the disulfide bond is also critical for the binding of IgE to allergens. Interestingly, different mutations induced similar electrostatic potential and allergenicity changes, such as localized structure R62DPYSPSQDPYSPS75. In conclusion, the disulfide bond and the SASA of aromatic residues are important for the allergenicity of Ara h 2. The localized structure R62DPYSPSQDPYSPS75 is also crucial for the allergenicity of Ara h 2.

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“…Liquid chromatography–mass spectrometry (LC-MS) was performed according to Zhou et al [ 27 ]. The mass spectrum parameters were as follows: (1) primary mass spectrometry: resolution = 70,000; AGC target = 3,000,000; maximum IT = 100 ms; scan range = 350 to 1800 m / z ; (2) secondary mass spectrometry: resolution = 17,500; AGC target = 50,000; maximum IT = 120 ms; topN = 20; collision energy = 30.…”

Section: Methodsmentioning

confidence: 99%

Lipid and Protein Oxidation of Brown Rice and Selenium-Rich Brown Rice during Storage

Zhang

Liu

2022

Foods

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Selenium-rich rice has become one of the effective ways to increase people’s selenium intake. Selenium-containing proteins have higher antioxidant properties, which may lead to selenium-rich brown rice (Se-BR) having better storage stability than ordinary brown rice (BR). By measuring the peroxidation value, fatty acid value, carbonyl value and protein secondary structure, it was found that Se-BR had higher oxidation resistance stability than BR. The biological function of the differential proteins (DEPs) between ordinary brown rice stored for 0 days (BR-0) and 180 days (BR-6) as well as Se-rich brown rice stored for 0 days (Se-0) and 180 days (Se-6) was investigated by using iTRAQ. A total of 237, 235, 113 and 213 DEPs were identified from group A (BR-0/BR-6), group B (Se-0/Se-6), group C (BR-0/Se-0) and group D (BR-6/Se-6), respectively. Kyoto Encyclopedia of Genes and Genomes analysis showed that the DEPs were mainly enriched in glucose metabolism, tricarboxylic acid cycle, fatty acid biosynthesis and degradation, glutathione metabolism, sulfur metabolism, peroxisome and other metabolic pathways. This study provides theoretical support for the study of protein oxidation kinetics and storage quality control of brown rice during storage.

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The effect of roasting on peanut allergens’ digestibility, allergenicity, and structure

Cited by 15 publications

References 47 publications

Identification of linear epitopes and their major role in the immunoglobulin E-binding capacity of tropomyosin from Alectryonella plicatula

Identification of linear epitopes and their major role in the immunoglobulin E-binding capacity of tropomyosin from Alectryonella plicatula

Effect of Structural Targeted Modifications on the Potential Allergenicity of Peanut Allergen Ara h 2

Lipid and Protein Oxidation of Brown Rice and Selenium-Rich Brown Rice during Storage

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