Characterization of the protein structure of soymilk fermented by Lactobacillus and evaluation of its potential allergenicity based on the sensitized-cell model

Lu, Qiaoling; Zuo, LingLing; Wu, Zhihua; Li, Xin; Tong, Ping; Wu, Yong; Fan, Qiang; Chen, Hongbing; Yang, Anshu

doi:10.1016/j.foodchem.2021.130569

Cited by 41 publications

(26 citation statements)

References 38 publications

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“…In a KU812 cell model, Mut 1 showed a greatly weakened ability to induce the synthesis and release of allergenic cytokines. 30 In this study, the SASA of aromatic residues was found to be correlated with the IgE binding capacity. Two mutants, namely, Mut 1 and Mut 3, with small SASAs showed decreased allergenicity in all assessments.…”

Section: ■ Discussionmentioning

confidence: 62%

“…Mut 2 did not have substantial changes in various cytokines, indicating that the mutation scheme was not as effective as Mut 1 and Mut 3 in reducing sensitization. In a KU812 cell model, Mut 1 showed a greatly weakened ability to induce the synthesis and release of allergenic cytokines …”

Section: Discussionmentioning

confidence: 99%

“…Human basophil leukemia (KU812) cells were placed in fresh RPMI 1640 containing 15% fetal bovine serum (Wisent) and 1% penicillin/streptomycin and then cultured at 37 °C with 5% CO 2 . 30 Then, the cells (5 × 10 6 cells/mL) were preincubated with human sera pooled (30:1 v/v) for 24 h. Then, the Ara h 2 samples (45 μg/ mL) were added and incubated for 4 h. The contents of β-HEX, histamine, TNF-α, and IL-6 released from KU812 cells were measured by using a human β-HEX ELISA kit (Fusheng Industry Co., Shanghai, China), a human His ELISA kit (Fusheng Industry Co.), a human TNF-α ELISA kit (Neobioscience, Beijing, China), and a human IL-6 ELISA kit (Neobioscience), according to the manufacturer's recommendations.…”

Section: ■ Materials and Methodsmentioning

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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Section: ■ Discussionmentioning

confidence: 62%

Section: Discussionmentioning

confidence: 99%

Section: ■ Materials and Methodsmentioning

confidence: 99%

See 1 more Smart Citation

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.

Self Cite

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“…The immunoreactivity of β-conglycinin (7S) and glycinin (11S) in soymilk w reduced after fermentation with Enterococcus faecalis VB43 (Biscola et al, 2017). Soymilk fermented with a cocktail of L. brevis CICC 23,474 and L. brevis CICC 23,470 had lower antigenicity and potential allergenicity than the unfermented counterpart (Lu et al, 2022).…”

Section: Alleviating Allergenicitymentioning

confidence: 99%

Enzymatic Modification of Plant Proteins for Improved Functional and Bioactive Properties

Olatunde

Owolabi²,

Fadairo³

et al. 2022

Food Bioprocess Technol

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Plant-based proteins have shown great potential as an alternative substitute for animal proteins to meet the increasing global demand. Nevertheless, several limitations mitigate plant-based protein application and utilization. As a panacea to meeting the market demand, it is imperative to modify plant-based proteins to produce improved quality and technofunctionalities compared to conventional animal protein ingredients. Enzymatic, chemical, and physical modi cations have been used for plant-based proteins, which has shown exciting results in improving their techno-functional properties, digestibility, and inherent allergenicity. Among these modi cation methods, the low cost, limited time, high sensitivity, and high reproducibility give enzymatic modi cation leverage over chemical and physical methods. This review gave a concise summary of the advantages and disadvantages of enzymatic modi cations. The e cacy of enzymatic modi cation in producing protein ingredients from plant sources with improved techno-functional properties, digestibility, and alleviated allergenicity was discussed. Furthermore, the application of enzymatic modi cation in the production of bioactive compounds with health-bene cial properties adds in no small measure to the novelty of this review.

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“…Studies have shown that fermentation can reduce food allergens through hydrolysis (8), while improving nutritional and physicochemical characteristics of foods (9,10). Reduction of protein allergens through fermentation has been reported for milk (11,12), peanuts (13), soybeans (14,15), and wheat (16,17). Also, their nutritional properties were notably improved following fermentation, such as increasing the contents of free amino acids in milk (18), as well as improving the levels of phenolic compounds, bioactive peptides, and free amino acids in cereals (19).…”

Section: Introductionmentioning

confidence: 98%

A Combined Proteomic and Metabolomic Strategy for Allergens Characterization in Natural and Fermented Brassica napus Bee Pollen

et al. 2022

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Bee pollen is consumed for its nutritional and pharmacological benefits, but it also contains hazardous allergens which have not been identified. Here, we identified two potential allergens, glutaredoxin and oleosin-B2, in Brassica napus bee pollen using mass spectrometry-based proteomics analyses, and used bioinformatics to predict their antigenic epitopes. Comparison of fermented (by Saccharomyces cerevisiae) and unfermented bee pollen samples indicated that glutaredoxin and oleosin-B2 contents were significantly decreased following fermentation, while the contents of their major constituent oligopeptides and amino acids were significantly increased based on metabolomics analyses. Immunoblot analysis indicated that the IgE-binding affinity with extracted bee pollen proteins was also significantly decreased after fermentation, suggesting a reduction in the allergenicity of fermented bee pollen. Furthermore, fermentation apparently promoted the biosynthesis of L-valine, L-isoleucine, L-tryptophan, and L-phenylalanine, as well as their precursors or intermediates. Thus, fermentation could potentially alleviate allergenicity, while also positively affecting nutritional properties of B. napus bee pollen. Our findings might provide a scientific foundation for improving the safety of bee pollen products to facilitate its wider application.

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Characterization of the protein structure of soymilk fermented by Lactobacillus and evaluation of its potential allergenicity based on the sensitized-cell model

Cited by 41 publications

References 38 publications

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

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

Enzymatic Modification of Plant Proteins for Improved Functional and Bioactive Properties

A Combined Proteomic and Metabolomic Strategy for Allergens Characterization in Natural and Fermented Brassica napus Bee Pollen

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