Effects of high hydrostatic pressure combined with enzymatic hydrolysis on the allergenicity, structural properties, and antigenic epitopes of soybean glycinin

In this study, we systematically investigated the effects of high hydrostatic pressure-assisted enzymatic hydrolysis (HHP-E) on the allergenicity, structural properties, and antigenic epitopes of soybean glycinin (11S). The results showed that after 600 MPa pressure combined with enzymatic treatment (H600-E), the allergenicity of 11S decreased by 34.54%, and the allergenicity decreased by 76.68% and 71.43% after simulated digestion in adults (120 min) and infants (60 min), respectively. Spectral analysis revealed that the contents of β-sheets and random coils in the secondary structure of 11S decreased after H600-E treatment and in vitro digestion, and that the tertiary structure changed significantly. Mass spectrometry analysis revealed that after H600-E treatment, 29 dominant linear epitopes of 11S were degraded, and another six linear epitopes were further degraded after simulated digestion. These results indicated that HHP-E treatment can reduce the allergenicity of the 11S protein by altering its conformation and destroying antigenic epitopes. • HHP-E treatment significantly reduced the allergenicity of soybean glycinin. • The structures of 11S were changed after HHP-E treatment and in vitro digestion. • The antigenic epitopes were destroyed after HHP-E treatment and simulated digestion.

Authors

Institutions

Publication Details

Journal
LWT
Published
2025-10-31
DOI
https://doi.org/10.1016/j.lwt.2025.118682
Primary Topic
Food Allergy and Anaphylaxis Research
Type
article
Field-Weighted Citation Impact
0.00
Controls
|||
ALL TIME
JAN
FEB
MAR
APR
MAY
JUN
JUL
AUG
SEP
OCT
article

Effects of high hydrostatic pressure combined with enzymatic hydrolysis on the allergenicity, structural properties, and antigenic epitopes of soybean glycinin

Yixuan Chen, Tingwei Zhu, Guanhao Bu, Songshan Shi et al.
LWT
Food Allergy and Anaphylaxis Research
article

Effects of high hydrostatic pressure combined with enzymatic hydrolysis on the allergenicity, structural properties, and antigenic epitopes of soybean glycinin

Yixuan Chen, Tingwei Zhu, Guanhao Bu, Songshan Shi, Mengyao Li, Qingqing Zhao, Jinrong Zhu
article en

Abstract

In this study, we systematically investigated the effects of high hydrostatic pressure-assisted enzymatic hydrolysis (HHP-E) on the allergenicity, structural properties, and antigenic epitopes of soybean glycinin (11S). The results showed that after 600 MPa pressure combined with enzymatic treatment (H600-E), the allergenicity of 11S decreased by 34.54%, and the allergenicity decreased by 76.68% and 71.43% after simulated digestion in adults (120 min) and infants (60 min), respectively. Spectral analysis revealed that the contents of β-sheets and random coils in the secondary structure of 11S decreased after H600-E treatment and in vitro digestion, and that the tertiary structure changed significantly. Mass spectrometry analysis revealed that after H600-E treatment, 29 dominant linear epitopes of 11S were degraded, and another six linear epitopes were further degraded after simulated digestion. These results indicated that HHP-E treatment can reduce the allergenicity of the 11S protein by altering its conformation and destroying antigenic epitopes. • HHP-E treatment significantly reduced the allergenicity of soybean glycinin. • The structures of 11S were changed after HHP-E treatment and in vitro digestion. • The antigenic epitopes were destroyed after HHP-E treatment and simulated digestion.

LWTVol. 236
Henan University of Technology (CN)
Openalex Percentile: Top 60%
Food Allergy and Anaphylaxis Research
AI Navigator

Ask Laika to Summarize, Analyze, and Connect papers live on the map.

Summarize Papers & Methodologies

Extract key findings, datasets, and comparative methods across publications.

Benchmark Rankings & Visual Analytics

Rank top research institutions, authors, funders, topics, and journals by Field-Weighted Citation Impact (FWCI) and paper volume with instant charts.

Connect Distant Disciplines

Bridge topological clusters on the map to find hidden collaborative intersections.