Mechanism on the Allergenicity Changes of alpha-Lactalbumin Treated by Sonication-Assisted Glycation during In Vitro Gastroduodenal Digestion
文献类型： 外文期刊
作者： Wang, Xu-Mei 1 ; Tu, Zong-Cai 1 ; Ye, Yun-Hua 2 ; Liu, Guang-Xian 4 ; Wang, Hui 1 ; Hu, Yue-Ming 1 ;
作者机构： 1.Nanchang Univ, State Key Lab Food Sci & Technol, Nanchang 330047, Jiangxi, Peoples R China
2.Jiangxi Normal Univ, Natl R&D Branch Ctr Convent Freshwater Fish Proc, Nanchang 330022, Jiangxi, Peoples R China
3.Jiangxi Normal Univ, Engn Res Ctr Freshwater Fish High Value Utilizat, Nanchang 330022, Jiangxi, Peoples R China
4.Jiangxi Acad Agr Sci, Inst Food Sci & Technol, Nanchang 330200, Jiangxi, Peoples R China
关键词： alpha-lactalbumin; sonication-assisted glycation; allergenicity; high-resolution mass spectrometry; gastroduodenal digestion
期刊名称：JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY （ 影响因子：5.279； 五年影响因子：5.269 ）
ISSN： 0021-8561
年卷期： 2021 年 69 卷 24 期
页码：
收录情况： SCI
摘要： Physical-assisted chemical modification is effective to reduce the allergenicity of alpha-lactalbumin (ALA). However, there are few in-depth studies on the allergenicity changes of physical-assisted chemical-modified ALA during digestion. The effect of gastroduodenal digestion on the allergenicity changes of ALA treated by sonication-assisted glycation was assessed. Digestion of both ALA and its glycated forms generated peptide fractions, and intact undigested glycated ALA in the hydrolysates still covalently bound to D-galactose. High-resolution mass spectrometry revealed that a higher glycation degree was discovered in sonication-preprocessed ALA compared to native ALA. Enzyme-linked immunosorbent assay and basophil degranulation showed that sonication-assisted glycation could significantly reduce ALA allergenicity. The allergenicity of both gastric and gastroduodenal hydrolysates was further increased, and the hydrolysates of sonication-assisted glycated ALA showed the lowest allergenicity. The reason could be the shielding effect of the linear epitope found to be caused by a higher glycation degree; although linear epitopes were exposed, D-galactose covalently bound to intact undigested glycated ALA in the hydrolysates retained its masking role. These results indicated that sonication-assisted glycation could be a promising method to prepare immunotherapeutic agents for allergen immunotherapy to achieve the purpose of allergy desensitization.
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