Effect of processing on soybean allergens and their allergenicity

Pi, Xiaowen; Sun, Yuxue; Fu, Guiming; Wu, Zhihua; Cheng, Jianjun

doi:10.1016/j.tifs.2021.10.006

Cited by 83 publications

(49 citation statements)

References 87 publications

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“…Soybean (Glycine max) is a good source of nutritional protein for animal and human consumption due to its high protein content (dry weight basis, 34.1-56.8%) [1], but it is one of eight major food allergens, affecting 1.4% of the referred population [2,3]. Generally, soybean allergy can cause allergic reactions, including rhinitis, urticarial, vomiting, shock and death, etc.…”

Section: Introductionmentioning

confidence: 99%

“…Generally, soybean allergy can cause allergic reactions, including rhinitis, urticarial, vomiting, shock and death, etc. [2]. Moreover, the LOAEL (the lowest amount of the allergenic food inducing allergic symptoms) is 5.3 mg of soybean proteins [4].…”

Section: Introductionmentioning

confidence: 99%

“…Moreover, the LOAEL (the lowest amount of the allergenic food inducing allergic symptoms) is 5.3 mg of soybean proteins [4]. Currently, many soybean allergens have been identified, including Gly m 1 to Gly m 8, P28, P34 and kunitz trypsin [2,5,6]. All soybean allergens account for approximately 65-80% of total soybean proteins and 30% of defatted soybean meal [7].…”

Section: Introductionmentioning

confidence: 99%

“…All soybean allergens account for approximately 65-80% of total soybean proteins and 30% of defatted soybean meal [7]. Gly m 4 (17 kDa), Gly m 5 (42-53 kDa, 57-76 kDa, 57-83 kDa), Gly m 6 (56, 54, 54, 64, and 59 kDa), P28 (28 kDa), P34 (30 kDa) are the major soybean allergens [2]. P34, P28 and Gly m 5 are derived from the 7S globulin, whereas Gly m 6 is from 11S globulin and Gly m 4 is a pathogenesis-related protein [2].…”

Section: Introductionmentioning

confidence: 99%

“…Boiling and autoclaving are common thermal technologies used to inactivate microorganism and anti-nutritional factors of food products with low cost and easy use [2,[8][9][10]. Many studies have demonstrated that the allergenicity of soybeans and peanuts were successfully reduced by boiling and autoclaving, respectively [6,[11][12][13][14].…”

Section: Introductionmentioning

confidence: 99%

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

Sun

Deng

et al. 2022

Foods

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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.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

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

Sun

Deng

et al. 2022

Foods

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Effects of faba bean protein isolate on rheological properties of pork myofibrillar protein gels and quality characteristics of pork low‐fat model sausages

Kim,

Chin

2024

J Sci Food Agric

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BackgroundThis study aimed to assess the effect of faba bean (Vicia faba L.) protein isolate (FBPI) on the rheological properties of pork myofibrillar protein gels (MPGs) and the quality characteristics of pork low‐fat model sausages (LFMSs).ResultsPork MPGs with 5 or 10 g kg−1 FBPI had higher cooking yield, gel strength, and viscosity compared with control. The addition of FBPI to MPGs increased the protein surface hydrophobicity and decreased sulfhydryl groups. Furthermore, adding FBPI to MPGs changed the protein profile and microstructure. The cooking loss and expressible moisture of LFMSs with 5, 10, or 15 g kg−1 FBPI were lower than those of control and showed similar results to those with 15 g kg−1 soy protein isolate (SPI). Hardness values of LFMSs with FBPI and SPI were no different, and were higher than those of control.ConclusionThe addition of FBPI potentially improves rheological properties of MPGs and the functional properties of LFMSs, including water‐holding capacity and textural properties.This article is protected by copyright. All rights reserved.

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Effect of transglutaminase crosslinking combined with lactic fermentation on the potential allergenicity and conformational structure of soy protein

Xing,

Yang,

Huang

et al. 2024

J Sci Food Agric

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BACKGROUNDFood allergies are a growing concern worldwide, with soy proteins being important allergens that are widely used in various food products. This study investigated the potential of transglutaminase (TGase) and lactic acid bacteria (LAB) treatments to modify the allergenicity and structural properties of soy protein isolate (SPI), aiming to develop safer soy‐based food products.RESULTSTreatment with TGase, LAB or their combination significantly reduced the antibody reactivity of β‐conglycinin and the immunoglobulin E (IgE) binding capacity of soy protein, indicating a decrease in allergenicity. TGase treatment led to the formation of high‐molecular‐weight aggregates, suggesting protein crosslinking, while LAB treatment resulted in partial protein hydrolysis. These structural changes were confirmed by Fourier transform infrared spectroscopy, which showed a decrease in β‐sheet content and an increase in random coil and β‐turn contents. In addition, changes in intrinsic fluorescence and ultraviolet spectroscopy were also observed. The alterations in protein interaction and the reduction in free sulfhydryl groups highlighted the extensive structural modifications induced by these treatments.CONCLUSIONThe synergistic application of TGase and LAB treatments effectively reduced the allergenicity of SPI through significant structural modifications. This approach not only diminished antibody reactivity of β‐conglycinin and IgE binding capacity of soy protein but also altered the protein's primary, secondary and tertiary structures, suggesting a comprehensive alteration of SPI's allergenic potential. These findings provide a promising strategy for mitigating food allergy concerns and lay the foundation for future research on food‐processing techniques aimed at allergen reduction. © 2024 Society of Chemical Industry.

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Effect of processing on soybean allergens and their allergenicity

Cited by 83 publications

References 87 publications

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

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

Effects of faba bean protein isolate on rheological properties of pork myofibrillar protein gels and quality characteristics of pork low‐fat model sausages

Effect of transglutaminase crosslinking combined with lactic fermentation on the potential allergenicity and conformational structure of soy protein

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