Soy protein isolate-(-)-epigallocatechin gallate conjugate: Covalent binding sites identification and IgE binding ability evaluation
文献类型： 外文期刊
作者： Zhou, Si-Duo 1 ; Huang, Lu 2 ; Meng, Ling 2 ; Lin, Yan-Fei 2 ; Xu, Xiao 2 ; Dong, Ming-Sheng 2 ;
作者机构： 1.Qilu Univ Technol, Shandong Food Ferment Ind Res & Design Inst, Shandong Prov Key Lab Food & Fermentat Engn, Shandong Acad Sci, Jinan 250013, Peoples R China
2.Nanjing Agr Univ, Coll Food Sci & Technol, 1 Weigang Rd, Nanjing 210095, Jiangsu, Peoples R China
3.Jiangsu Acad Agr Sci, Inst Ind Crops, Nanjing 210014, Peoples R China
关键词： (-)-Epigallocatechin gallate; Soy protein isolate; Conjugate; Covalent binding sites
期刊名称：FOOD CHEMISTRY （ 影响因子：7.514； 五年影响因子：7.516 ）
ISSN： 0308-8146
年卷期： 2020 年 333 卷
页码：
收录情况： SCI
摘要： The conjugate prepared from (-)-epigallocatechin gallate (EGCG) and soy protein isolate (SPI) under alkaline and aerobic conditions was analyzed using a Nano-LC-Q-Orbitrap-MS/MS technique. The sulfhydryl and free amino groups of SPI were involved in covalent binding. Fifty-one peptides were conjugated with EGCG. Fifty-nine modified sites were identified, located on Cys, His, Arg, and Lys, respectively. It is the first time to confirm that each of the two phenolic rings of EGCG contained a reactive site that bound to an amino acid residue. The amino acid residue reactivity, amino acid sequence and composition affected the EGCG binding site in SPI. Lys and Arg residues are the most likely sites for modification, and modification appears to reduce IgE binding. This study is helpful to elucidate the pattern of covalent binding of polyphenols to proteins in food systems and provides a theoretical basis for the directional modification of soy proteins with polyphenols.
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