Isolation and allergenicity evaluation of glycated alpha-lactalbumin digestive products and identification of allergenic peptides

文献类型: 外文期刊

第一作者: Wang, Xu-Mei

作者: Wang, Xu-Mei;Tu, Zong-Cai;Hu, Yue-Ming;Wang, Hui;Tu, Zong-Cai;Ye, Yun-Hua;Tu, Zong-Cai;Ye, Yun-Hua;Liu, Guang-Xian

作者机构:

关键词: alpha-Lactalbumin; Glycation; In-vitro gastroduodenal digestion; UPLC HCD-MS/MS; Allergenicity; Allergenic peptides

期刊名称:FOOD CHEMISTRY ( 影响因子:9.231; 五年影响因子:8.795 )

ISSN: 0308-8146

年卷期: 2022 年 390 卷

页码:

收录情况: SCI

摘要: This study aimed to isolate and evaluate the allergenicity of glycated a-lactalbumin (ALA) digestive products and identify its allergenic peptides. The digestive products of native-, alone glycated- and ultrasound-assisted glycated ALA (ALA-D, ALA-gal-D, 100ALA-gal-D) were isolated into three fractions (F1, F2 and F3). High-resolution mass spectrometry showed that the digestion-resistant peptides of F2 and F3 mainly distributed in amino acid sequence (AA) 25-31, AA32-53, AA40-53, AA54-60, AA80-90, AA94-104. The allergenicity of the three fractions of glycated ALA was lower than that in ALA-D, indicating glycation of ALA could indeed reduce its allergenicity after digestion. Furthermore, most fractions isolated from high glycation-degree ALA had the lowest allergenicity. The IgG/IgE binding abilities of synthesized peptides indicated that AA94-104 firstly identified by us embodied the strongest allergenicity and might be the potential allergenic peptide. This will provide a theory for preparing hypoallergenic products based on the identified allergenic peptides.

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