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. 2022 Feb 7;11(3):479.
doi: 10.3390/foods11030479.

Characterization of the Reduced IgE Binding Capacity in Boiled and Autoclaved Soybeans through Proteomic Approaches

Xiaowen Pi  1 , Yuxue Sun  1   2 , Xiaomin Deng  1 , Dawei Xin  1 , Jianjun Cheng  1 , Mingruo Guo  1   3
Affiliations

Characterization of the Reduced IgE Binding Capacity in Boiled and Autoclaved Soybeans through Proteomic Approaches

Xiaowen Pi et al. Foods. .

Abstract

The study investigated the changes in IgE binding capacity, protein profiles and peptide compositions after soybeans were boiled and autoclaved. The results of ELISA showed that the IgE binding capacity of soybean was reduced by 69.3% and 88.9% after boiling and autoclaving, respectively. Above 43 and 10 kDa proteins disappeared in boiled and autoclaved soybeans from SDS-PAGE, respectively. A Venn diagram and heat map showed that there was no change in allergen types and a reduction in allergen contents in the boiled and autoclaved soybeans. The changes in peptide compositions were also observed in the boiled and autoclaved soybeans through Venn diagram, PCA and heat map. LC/MS-MS and peptide mapping analysis demonstrated that boiling and autoclaving masked many epitopes in Gly m 4 and Gly m 5, such as ALVTDADNVIPK, SVENVEGNGGPGTIKK and KITFLEDGETK of Gly m 4 and VEKEECEEGEIPRPRPRPQHPER of Gly m 5, resulting in a reduction of IgE binding capacity in the extracted proteins. By contrast, the exposure of many epitopes in Gly m 6 was observed in boiled and autoclaved soybeans, which might be mainly responsible for the existing IgE binding capacity in the treated soybean proteins. Interestingly, the IgE binding capacity of soybeans showed a positive correlation with the total contents and number of peptides in Gly m 4-Gly m 6.

Keywords: IgE binding capacity; allergen; autoclaving; boiling; peptide.

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Conflict of interest statement

Authors declare no conflict of interest.

Figures

Figure 1
Figure 1
Changes in IgE binding capacity of extracted proteins from raw, boiled and autoclaved soybeans. Means with different letters (a–c) indicate significantly different (p < 0.05).
Figure 2
Figure 2
Changes in protein profiles of extracted proteins from raw, boiled and autoclaved soybeans. (A) SDS-PAGE, M, standard proteins; lands M, 1, 2 and 3 represented extracted proteins from raw, boiled and autoclaved soybeans, respectively. (B) Venn diagrams. (C) heat map and cluster analysis, the deeper the red band, the higher the relative abundance of the protein, and the deeper the blue, the lower the relative abundance.
Figure 3
Figure 3
Changes in contents of identified allergens (Gly m 4-Gly m 6) in extracted proteins from raw, boiled and autoclaved soybeans.
Figure 4
Figure 4
Differences of peptide compositions in identified soybean allergens (Gly m 4−Gly m 6). (A) Venn diagrams. (B) PCA analysis. (C) heat map and cluster analysis, the deeper the red band, the higher the relative abundance of the protein, and the deeper the blue, the lower the relative abundance.
Figure 5
Figure 5
Changes in peptide map of Gly m 4-Gly m 6 in extracted proteins from raw (R1), boiled (B1) and autoclaved soybeans (A1). (A) peptide map of Gly m 4 (UniProtKB, P26987). (B) peptide map of Gly m 5, including beta-conglycinin alpha subunit 1 (UniProtKB, P0DO16), beta-conglycinin alpha’ subunit (P11827), beta-conglycinin beta subunit 1 (P25974) and beta-conglycinin beta subunit 2 (F7J077). (C) peptide map of Gly m 6, including Glycinin G1(P04776), G2 (P04405), G3 (P11828), G4 (P02858) and G5 (P04347). The relative abundance, amino acid coverage and overlap ratio was shown by the color depth, the width and length of each band, respectively.
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