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Non-covalent interaction between lactoferrin and theaflavin: Focused on the structural changes, binding mechanism, and functional properties.
Liu, Xiaoze; Chen, Jingwen; Zhang, Wen; Lin, Xue; Fei, Tao; Liu, Zhonghua; Wang, Lu.
Afiliación
  • Liu X; School of Food Science and Engineering, Hainan University, Haikou 570228, PR China.
  • Chen J; School of Food Science and Engineering, Hainan University, Haikou 570228, PR China.
  • Zhang W; School of Food Science and Engineering, Hainan University, Haikou 570228, PR China.
  • Lin X; School of Food Science and Engineering, Hainan University, Haikou 570228, PR China; Key Laboratory of Food Nutrition and Functional Food of Hainan Province, Hainan University, Haikou 570228, PR China.
  • Fei T; School of Food Science and Engineering, Hainan University, Haikou 570228, PR China; Key Laboratory of Food Nutrition and Functional Food of Hainan Province, Hainan University, Haikou 570228, PR China.
  • Liu Z; Key Laboratory of Tea Science of Ministry of Education and National Research Center of Engineering Technology for Utilization of Functional Ingredients from Botanicals, Collaborative Innovation Centre of Utilisation of Functional Ingredients from Botanicals and Co-Innovation Center of Education Mini
  • Wang L; School of Food Science and Engineering, Hainan University, Haikou 570228, PR China; Key Laboratory of Tea Science of Ministry of Education and National Research Center of Engineering Technology for Utilization of Functional Ingredients from Botanicals, Collaborative Innovation Centre of Utilisation
Food Chem ; 461: 140835, 2024 Dec 15.
Article en En | MEDLINE | ID: mdl-39213731
ABSTRACT
In this study, non-covalent binding mechanism of lactoferrin (LaF)-theaflavin (TF) complex and its functional properties were investigated. Multi-spectroscopic analyses showed that the secondary structure of LaF was altered with increasing TF concentration. The non-covalent binding of TF to LaF resulted in a reduction in the content of the α-helix and ß-sheet, as well as a decrease in the fluorescence intensity of LaF. DSC result showed that non-covalent binding of TF improved thermal stability of LaF. Molecular dynamics simulations confirmed that the stable binding of LaF-TF was driven by hydrogen bonding and hydrophobic interactions. Additionally, non-covalent binding of TF increased the antioxidant capacity and emulsifying properties of LaF. Dynamic interfacial tension indicated that the strong interaction between LaF and TF reduced the interfacial tension, but improved the rheological properties of LaF. The functional characteristics of the non-covalent complex was effectively enhanced, paving the way for its potential use in the food industry.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Catequina / Biflavonoides / Simulación de Dinámica Molecular / Lactoferrina Idioma: En Revista: Food Chem Año: 2024 Tipo del documento: Article Pais de publicación: Reino Unido

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Catequina / Biflavonoides / Simulación de Dinámica Molecular / Lactoferrina Idioma: En Revista: Food Chem Año: 2024 Tipo del documento: Article Pais de publicación: Reino Unido