College of Food Science, Northeast Agricultural University, Harbin, 150030, China.
Department of Chemical Physics, University of Science and Technology of China, Hefei, 230026, China.
Biomaterials. 2022 Apr;283:121455. doi: 10.1016/j.biomaterials.2022.121455. Epub 2022 Mar 5.
Soy protein-derived amyloid fibrils (SAFs) held desirable features, and with rational tailoring of physical structures, their techno-functions could be further improved. Here, we report a strategy for tailoring SAFs to form hydrogels with appealing mechanical properties as mediated by (-)-epigallocatechin-3-gallate (EGCG). The SAFs-EGCG complexes are characterized by measuring changes in gelling properties, identifying interfacing residues, and understanding the molecular geometry of complexes. EGCG is found to cleave rigid SAFs and induce the formation of large branched chains, which are essential for forming gel-like structures. Results in this study show that SAFs-EGCG complexes and their digesta are non-toxic in human cell lines, and these complexes are superior in inhibiting the growth of Escherichia coli and Staphylococcus aureus. This study provides new insights into remodeling structures and steering techno-functions of SAFs through interaction with EGCG, and will serve as a basis for EGCG as a potent remodeling agent of food protein-derived fibrils.
大豆蛋白衍生的淀粉样纤维（SAFs）具有理想的特性，通过合理调整物理结构，可以进一步提高其技术功能。在这里，我们报告了一种通过（-）-表没食子儿茶素没食子酸酯（EGCG）来调整 SAF 形成具有吸引力的机械性能的水凝胶的策略。通过测量胶凝特性的变化、确定界面残基以及了解复合物的分子几何形状来对 SAF-EGCG 复合物进行表征。发现 EGCG 可以切割刚性 SAF 并诱导形成大的支链，这对于形成凝胶状结构是必不可少的。本研究结果表明，SAF-EGCG 复合物及其消化产物在人细胞系中没有毒性，并且这些复合物在抑制大肠杆菌和金黄色葡萄球菌的生长方面表现出色。这项研究为通过与 EGCG 相互作用重塑 SAF 结构和控制其技术功能提供了新的见解，并将为 EGCG 作为一种有效的食品蛋白衍生纤维重塑剂奠定基础。
