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纤维素纳米晶介导的大豆分离蛋白原纤维凝胶网络结构的重塑机制。

Remodeling mechanism of gel network structure of soy protein isolate amyloid fibrils mediated by cellulose nanocrystals.

机构信息

Key Laboratory of Jianghuai Agricultural Product Fine Processing and Resource Utilization of Ministry of Agriculture and Rural Affairs, State Key Laboratory of Tea Plant Biology and Utilization, School of Tea and Food Science & Technology, Anhui Agricultural University, Hefei, 230036, China.

Key Laboratory of Jianghuai Agricultural Product Fine Processing and Resource Utilization of Ministry of Agriculture and Rural Affairs, State Key Laboratory of Tea Plant Biology and Utilization, School of Tea and Food Science & Technology, Anhui Agricultural University, Hefei, 230036, China.

出版信息

Carbohydr Polym. 2024 May 15;332:121919. doi: 10.1016/j.carbpol.2024.121919. Epub 2024 Feb 9.

DOI:10.1016/j.carbpol.2024.121919
PMID:38431397
Abstract

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.

摘要

本研究考察了大豆分离蛋白(SPI)和大豆分离蛋白原纤维(SAFs)的胶凝性质差异,以及纤维素纳米晶体(CNC)在调节其凝胶行为中的作用。CNC 与β-伴球蛋白(7S)、伴大豆球蛋白(11S)和 SAFs 的结合主要由非共价相互作用驱动。CNC 的添加降低了 SPI 和 SAFs 的粒径、浊度、亚基片段和结晶度,促进了α-螺旋向β-折叠的转化,提高了热稳定性,暴露出更多的酪氨酸和色氨酸残基,增强了分子间相互作用。在 SAFs-CNC 复合凝胶中形成了更规则和有序的层状网络结构,这有助于改善凝胶质量。本研究将为理解蛋白质原纤维凝胶化的调节机制以及 SAFs-CNC 复合物作为功能性蛋白质基材料或食品成分在食品领域中的高值利用提供理论参考。

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