Modulation of soy protein immunoreactivity by different matrix structures of lactic acid bacterium-induced soy protein gels: Epitope destruction during in vitro gastroduodenal digestion and absorption

[Display omitted] •LAB-fermented SPI had various matrix structures at varied protein concentrations.•FSPI gels had lower immunoreactivity than FSPI-NG at 0–30 min of duodenal digestion.•Transepithelial study showed FSPI-gel induced stimulation of interferon-γ production.•FSPI-gel promoted the epitop...

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Published in:Food research international 2023-11, Vol.173 (Pt 1), p.113281-113281, Article 113281
Main Authors: Wang, Yaqiong, Fu, Yumeng, Li, Wei, Simpson, Benjamin K., Rui, Xin
Format: Article
Language:English
Subjects:
Digestion
Epitopes
Epitopes - chemistry
Globulins - chemistry
Glycine max - chemistry
Humans
IgE reactivity
In vitro dynamic gastroduodenal digestion
Lactic acid bacteria
Soy protein gel
Soybean Proteins - chemistry
Transepithelial transport
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Summary:[Display omitted] •LAB-fermented SPI had various matrix structures at varied protein concentrations.•FSPI gels had lower immunoreactivity than FSPI-NG at 0–30 min of duodenal digestion.•Transepithelial study showed FSPI-gel induced stimulation of interferon-γ production.•FSPI-gel promoted the epitope degradation of the six major allergens during digestion.•Glycinin/β-conglycinin inner epitope were preferentially degraded during digestion. Soy allergy is a common health problem. Food structure may change the gastroduodenal digestion and absorption of soy proteins, thus leading to the modulation of the immunoreactivity of soy proteins. In this study, lactic acid bacterium (LAB)-fermented soy protein isolates (FSPIs) were prepared at four concentrations (0.2 %–5.0 %, w/v) to present various matrix structures (nongel, NG; weak gel, WG; medium gel, MG; and firm gel, FG) and subjected to in vitro dynamic gastroduodenal digestion model. The results of sandwich enzyme-linked immunosorbent and human serum IgE binding capacity assays demonstrated that FSPI gels, especially the FSPI-MG/WG digestates obtained at the early and medium stages of duodenal digestion (D-5 and D-30), possessed greater potency in immunoreactivity reduction than FSPI-NG and reduced to 1.9 %–68.3 %. The transepithelial transport study revealed that the immunoreactivity of FSPI-MG/WG D-5 and D-30 digestates decreased through the stimulation of interferon-γ production and the induction of dominant Th1/Th2 differentiation. Peptidomics and bioinformatics analyses illustrated that compared with FSPI-NG, the FSPI-gel structure promoted the epitope degradation of the major allergens glycinin G2/G5, β-conglycinin α/β subunit, P34, lectin, trypsin inhibitor, and basic 7S globulin. Spatial structure analysis showed that FSPI-gel elicited an overall promotion in the degradation of allergen epitopes located in interior and exterior regions and was dominated by α-helix and β-sheet secondary structures, whereas FSPI-MG/WG promoted the degradation of epitopes located in the interior region of glycinin/β-conglycinin and exterior region of P34/basic 7S globulin. This study suggested that the FSPI-gel structure is a promising food matrix for decreasing the allergenic potential of allergenic epitopes during gastroduodenal digestion and provided basic information on the production of hypoallergenic soy products.
ISSN:0963-9969
1873-7145
DOI:10.1016/j.foodres.2023.113281