College of Food Science and Engineering, Nanjing University of Finance and Economics, Nanjing 210023, Jiangsu, China.
College of Food Science and Engineering, Nanjing University of Finance and Economics, Nanjing 210023, Jiangsu, China.
Food Chem. 2024 Dec 1;460(Pt 2):140628. doi: 10.1016/j.foodchem.2024.140628. Epub 2024 Jul 26.
The study elucidates that the pH shifting treatment unfolds the conformation of soybean protein isolate (SPI), enabling it to intertwine with bacterial cellulose (BC) and form SPI/BC co-assemblies. Results from intrinsic fluorescence spectroscopy and surface hydrophobicity indicate that the SPI with pH shifting treatment shows a notable blue shift in maximum emission wavelength and increased surface hydrophobicity. It demonstrates that pH shifting treatment facilitates the unfolding of SPI's molecular conformation, promoting its entanglement with high aspect ratio BC. Particle size distribution and microstructural analysis further demonstrate that the pH shifting treatment facilitates the formation of SPI/BC co-assemblies. Evaluation of processing properties reveals that the SPI/BC co-assemblies exhibited exceptional gel and emulsification properties, with gel strength and emulsifying activity respectively six and two times higher than natural SPI. This enhancement is attributed to the thickening properties of BC with a high aspect ratio and the superior hydrophobicity of SPI in its molten globule state.
该研究阐明 pH 值转换处理可展开大豆分离蛋白（SPI）的构象，使其能够与细菌纤维素（BC）交织形成 SPI/BC 共组装体。内源荧光光谱和表面疏水性的结果表明，经过 pH 值转换处理的 SPI 表现出最大发射波长的明显蓝移和表面疏水性的增加。这表明 pH 值转换处理促进了 SPI 分子构象的展开，促进了其与高纵横比 BC 的缠结。粒度分布和微观结构分析进一步表明 pH 值转换处理有助于 SPI/BC 共组装体的形成。加工性能评估表明，SPI/BC 共组装体表现出优异的凝胶和乳化性能，凝胶强度和乳化活性分别比天然 SPI 高 6 倍和 2 倍。这种增强归因于高纵横比 BC 的增稠特性和处于熔融球蛋白状态的 SPI 的优越疏水性。
