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

表位 化学 静水压力 酶水解 抗原 水解 体外 生物化学 分子质量 蛋白质二级结构 蛋白质三级结构 色谱法 抗体 消化(炼金术) 乳清蛋白 蛋白质结构 食品科学 四级结构
作者
Mengyao Li,Qingqing Zhao,Guanhao Bu,Songye Shi,Tingwei Zhu,Yixuan Chen,Jinrong Zhu
出处
期刊:Lebensmittel-Wissenschaft & Technologie [Elsevier BV]
卷期号:236: 118682-118682
标识
DOI:10.1016/j.lwt.2025.118682
摘要

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.
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