Assembly Behavior and Interaction between Fish Skin Gelatin and Polyphenols

被引:2
|
作者
Wang S. [1 ]
Zhao J. [1 ]
Dai Y. [1 ]
Gao J. [1 ]
Liang H. [2 ]
Li S. [1 ]
Zhou B. [1 ,3 ]
机构
[1] Key Laboratory of Fermentation Engineering, Ministry of Education, School of Food and Biological Engineering, Hubei University of Technology, Wuhan
[2] College of Food Science and Technology, Huazhong Agricultural University, Wuhan
[3] Cellular Regulation and Molecular Pharmaceutics-overseas Expertise Introduction Center for Discipline Innovation ("111 Center"), Wuhan
来源
Zhou, Bin (zhoubin4111@163.com) | 1600年 / Chinese Chamber of Commerce卷 / 42期
关键词
Fish skin gelatin; Fluorescence spectrum; Interaction; Isothermal titration calorimetry; Polyphenol;
D O I
10.7506/spkx1002-6630-20200702-033
中图分类号
学科分类号
摘要
In this current work, the interaction and assemble behavior between polyphenols with different structures and fish skin gelatin (GLA) were evaluated, which is expected to provide a scientific basis for the processing of aquatic products, the utilization of by-products and the exploration of novel food ingredients, and to provide a theoretical guidance for the application of polyphenol-protein complexes in food fields. Three kinds of polyphenols with different numbers of pyrogallol groups including tannic acid (TA), epigallocatechin gallate (EGCG) and gallic acid (GA) were selected for this study. The impact of polyphenol concentration and pH on the assembly behavior of GLA-polyphenol systems was evaluated based on turbidity and particle size. Fluorescence spectroscopy and isothermal titration calorimetry (ITC) were used to explore the interaction mechanism between polyphenols and GLA. The results showed that TA and EGCG could be assembled with GLA at a certain concentration to form polyphenol-GLA nanocomposites, whose transmittance could be reversibly tuned by changing the pH. Fluorescence spectroscopic analysis revealed that the formation of GLA-polyphenol complexes could statically quench the endogenous fluorescence of GLA. Isothermal titration calorimetry showed that the main forces of the interaction between TA and GLA were hydrogen bonds and van der Waals forces, while the interaction between EGCG and GLA was mainly driven by electrostatic interaction. © 2021, China Food Publishing Company. All right reserved.
引用
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页码:1 / 8
页数:7
相关论文
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