Influence of tea polyphenol and bovine serum albumin on tea cream formation by multiple spectroscopy methods and molecular docking
文献类型： 外文期刊
作者： Yu, Xia 1 ; Cai, Xinghong 2 ; Luo, Liyong 1 ; Wang, Jie 4 ; Ma, Mengjun 5 ; Wang, Min 2 ; Zeng, Liang 1 ;
作者机构： 1.Southwest Univ, Coll Food Sci, 2 Tiansheng Rd, Chongqing 400715, Peoples R China
2.Southwest Univ, Sch Mat & Energy, 2 Tiansheng Rd, Chongqing 400715, Peoples R China
3.Southwest Univ, Tea Res Inst, 2 Tiansheng Rd, Chongqing 400715, Peoples R China
4.Chongqing Acad Agr Sci, Tea Res Inst, Chongqing 402160, Peoples R China
5.Xianning Acad Agr Sci, 168 Hesheng Rd, Xianning Dist 437100, Hubei, Peoples R China
关键词： Tea polyphenols; Interaction; TOPSIS; Fluorescence spectroscopy; Molecular docking
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 sensory qualities and shelf life of tea beverage strongly affected by tea cream that forms by the interaction of polyphenols and protein. The study aimed to investigate the effects of the interactions between tea polyphenols (TPs) and bovine serum albumin (BSA) on tea cream formation at different concentrations. The tea cream formation increased with TPs and BSA concentration increased. The optimal concentration (TPs: 800 mg/L, BSA: 40 mg/L), for high clarities and contents of phytochemicals, was selected by the technique for order preference by similarity to ideal solution (C = 0.7572). The interaction mechanism of TPs-BSA was investigated by fluorescence spectroscopy, UV-visible absorption spectroscopy, synchronous fluorescence spectroscopy, and molecular docking. TPs interacted with BSA via static quenching process, affecting tryptophan and tyrosine residue microenvironment of BSA. Ester catechins had more binding affinity than non-ester catechins. Hydrogen bonds were the main interaction forces of TPs-BSA.
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