纤维
大豆蛋白
层状结构
化学
结晶度
生物物理学
疏水效应
纤维素
化学工程
共价键
淀粉样蛋白(真菌学)
结晶学
生物化学
有机化学
生物
工程类
无机化学
作者
Qianxin Zhou,Songtao Lv,Wenqi Wang,Sha Zhu,Jianxia Xu,Mingming Zheng,Yingnan Liu,Yibin Zhou,Xiaonan Sui,Yaqing Xiao
标识
DOI:10.1016/j.carbpol.2024.121919
摘要
The differences in the gelling properties of soy protein isolate (SPI) and soy protein isolate amyloid fibrils (SAFs) as well as the role of cellulose nanocrystals (CNC) in regulating their gel behaviors were investigated in this study. The binding of CNC to β-conglycinin (7S), glycinin (11S), and SAFs was predominantly driven by non-covalent interactions. CNC addition reduced the particle size, turbidity, subunit segments, and crystallinity of SPI and SAFs, promoted the conversion of α-helix to β-sheet, improved the thermal stability, exposed more tyrosine and tryptophan residues, and enhanced the intermolecular interactions. A more regular and ordered lamellar network structure was formed in the SAFs-CNC composite gel, which could be conducive to the improvement of gel quality. This study would provide theoretical reference for the understanding of the regulatory mechanism of protein amyloid fibrils gelation as well as the high-value utilization of SAFs-CNC complex as a functional protein-based material or food ingredient in food field.
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