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Study on the interaction mechanism between (-)-epigallocatechin-3-gallate and myoglobin: Multi-spectroscopies and molecular simulation.
Bu, Ying; Fan, Maomei; Sun, Chaonan; Zhu, Wenhui; Li, Jianrong; Li, Xuepeng; Zhang, Yi.
Afiliación
  • Bu Y; College of Food Science, Fujian Agriculture and Forestry University, Engineering Research Centre of Fujian-Taiwan Special Marine Food Processing and Nutrition, Ministry of Education, Fuzhou, Fujian, China; College of Food Science and Engineering, Bohai University, Jinzhou, Liaoning, China. Electroni
  • Fan M; College of Food Science and Engineering, Bohai University, Jinzhou, Liaoning, China.
  • Sun C; College of Food Science and Engineering, Bohai University, Jinzhou, Liaoning, China.
  • Zhu W; College of Food Science and Engineering, Bohai University, Jinzhou, Liaoning, China. Electronic address: zhuwenhui@bhu.edu.cn.
  • Li J; College of Food Science and Engineering, Bohai University, Jinzhou, Liaoning, China.
  • Li X; College of Food Science and Engineering, Bohai University, Jinzhou, Liaoning, China.
  • Zhang Y; College of Food Science, Fujian Agriculture and Forestry University, Engineering Research Centre of Fujian-Taiwan Special Marine Food Processing and Nutrition, Ministry of Education, Fuzhou, Fujian, China. Electronic address: zyifst@163.com.
Food Chem ; 448: 139208, 2024 Aug 01.
Article en En | MEDLINE | ID: mdl-38608400
ABSTRACT
(-)-Epigallocatechin-3-gallate (EGCG) is remarkably efficacious in inhibiting the browning of red meat. We therefore propose a hypothesis that EGCG forms complexes with myoglobin, thereby stabilizing its structure and thus preventing browning. This study investigated the interaction mechanism between EGCG and myoglobin. EGCG induced static quenching of myoglobin. Noncovalent forces, including hydrogen bonds and van der Waals, primarily governing the interactions between myoglobin and EGCG. The interactions primarily disrupted myoglobin's secondary structure, thus significantly reducing surface hydrophobicity by 53% (P < 0.05). The modification augmented the solubility and thermal stability of myoglobin. The radius of gyration (Rg) value fluctuated between 1.47 and 1.54 nm, and the hydroxyl groups in EGCG formed an average of 2.93 hydrogen bonds with myoglobin. Our findings elucidated the formation of stable myoglobin-EGCG complexes and the myoglobin-EGCG interaction, thus confirming our initial hypothesis.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Catequina / Interacciones Hidrofóbicas e Hidrofílicas / Mioglobina Límite: Animals Idioma: En Revista: Food Chem Año: 2024 Tipo del documento: Article Pais de publicación: Reino Unido
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Catequina / Interacciones Hidrofóbicas e Hidrofílicas / Mioglobina Límite: Animals Idioma: En Revista: Food Chem Año: 2024 Tipo del documento: Article Pais de publicación: Reino Unido