Development of protein-polyphenol particles to stabilize high internal phase Pickering emulsions by polyphenols' structure

被引:51
作者
Chen, Yang [1 ]
Yao, Mengying [2 ]
Peng, Su [1 ]
Fang, Yajing [1 ]
Wan, Liting [1 ]
Shang, Wenting [1 ]
Xiang, Dong [1 ]
Zhang, Weimin [1 ,3 ,4 ]
机构
[1] Hainan Univ, Sch Food Sci & Engn, Key Lab Food Nutr & Funct Food Hainan Prov, Haikou 570228, Peoples R China
[2] Publ Inspect & Testing Ctr Gongan Cty, Jingzhou 434300, Peoples R China
[3] Hainan Inst Food Control, Key Lab Trop Fruits & Vegetables Qual & Safety Sta, Haikou 570228, Peoples R China
[4] Hainan Univ, Sch Food Sci & Engn, 58 Renmin Rd, Haikou 570228, Peoples R China
基金
中国国家自然科学基金;
关键词
Bovine serum albumin; Non-covalent interaction; High internal phase Pickering emulsion; Hydrogen bond; Oil -water interface; NANOPARTICLES; BINDING;
D O I
10.1016/j.foodchem.2023.136773
中图分类号
O69 [应用化学];
学科分类号
081704 ;
摘要
Protein-polyphenol colloidal particles are promising stabilizers for high internal phase Pickering emulsions (HIPPEs). However, the relationship between the structure of the polyphenols and its ability to stabilize HIPPEs has not been studied thus far. In this study, bovine serum albumin (BSA)-polyphenols (B-P) complexes were prepared, and their ability to stabilize HIPPEs was investigated. The polyphenols were bound to BSA via noncovalent interactions. Optically isomeric polyphenols formed similar bonds with BSA, whereas a greater number of trihydroxybenzoyl groups or hydroxyl groups in the dihydroxyphenyl moieties of polyphenols increased the B-P interactions. Polyphenols also reduced the interfacial tension and enhanced the wettability at the oil-water interface. The HIPPE stabilized by BSA-tannic acid complex exhibited the highest stability among the B-P complexes and resisted demixing and aggregation during centrifugation. This study promotes the potential applications of polyphenol-protein colloidal particles-stabilized HIPPEs in the food industry.
引用
收藏
页数:12
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