糖化 α-乳白蛋白消化产物的分离及变应原性评价和变应原性肽的鉴定。
Isolation and allergenicity evaluation of glycated α-lactalbumin digestive products and identification of allergenic peptides.
机构信息
State Key Laboratory of Food Science and Technology, Nanchang University, Nanchang, Jiangxi 330047, China.
State Key Laboratory of Food Science and Technology, Nanchang University, Nanchang, Jiangxi 330047, China; National R&D Branch Center for Conventional Freshwater Fish Processing, Jiangxi Normal University, Nanchang, Jiangxi 330022, China; Engineering Research Center of Freshwater Fish High-value Utilization of Jiangxi Province, Jiangxi Normal University, Nanchang, Jiangxi 330022, China.
出版信息
Food Chem. 2022 Oct 1;390:133185. doi: 10.1016/j.foodchem.2022.133185. Epub 2022 May 10.
This study aimed to isolate and evaluate the allergenicity of glycated α-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.
本研究旨在分离和评估糖化α-乳白蛋白（ALA）消化产物的变应原性，并鉴定其变应原性肽。将天然、单独糖化和超声辅助糖化的 ALA（ALA-D、ALA-gal-D、100ALA-gal-D）的消化产物分离成三个部分（F1、F2 和 F3）。高分辨质谱显示，F2 和 F3 的消化抗性肽主要分布在氨基酸序列（AA）25-31、AA32-53、AA40-53、AA54-60、AA80-90、AA94-104。糖化 ALA 的三个部分的变应原性低于 ALA-D，表明 ALA 的糖化确实可以降低其消化后的变应原性。此外，高糖化度 ALA 分离得到的大多数部分具有最低的变应原性。合成肽的 IgG/IgE 结合能力表明，我们首次鉴定的 AA94-104 具有最强的变应原性，可能是潜在的变应原性肽。这将为基于鉴定的变应原性肽制备低变应原性产品提供理论依据。
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