化学
纤维素
细菌纤维素
荧光
化学工程
大豆蛋白
荧光光谱法
粒子(生态学)
粒径
多糖
生物物理学
有机化学
生物化学
物理化学
物理
海洋学
量子力学
工程类
生物
地质学
作者
Xinbo Zhuang,Sunhui Yan,Cheng Luo,Jiaoqiong Liu,Yinji Chen,Qiang Liu,Guanghong Zhou,Chao Ding
标识
DOI:10.1016/j.foodchem.2024.140628
摘要
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.
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