超声制备的蛋白质-多酚-多糖复合物稳定乳状液的机理:结构、功能特性和界面行为。

IF 9.7 1区 化学 Q1 ACOUSTICS
Yuyang Huang, Baoning Zheng, Bingyu Sun, Ying Zhu, Linlin Liu, Jiyuan Liu, Yixin Zhang, Yang Li, Xiuqing Zhu
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引用次数: 0

摘要

基于多酚和多糖通过氢键和疏水力等非共价相互作用调节蛋白质构象的机制,三元配合物的构建为开发高效的乳化基递送系统提供了一种有前途的策略。本研究以大豆分离蛋白(SPI)、(-)-表没食子儿茶素没食子酸酯(EGCG)和聚葡萄糖(PD)为原料,经超声处理制备SPI、SPI-EGCG、SPI-PD和SPI-EGCG-PD配合物。然后将这些配合物用于稳定乳液,并系统地研究了它们的结构特征、功能特性和界面行为。结果表明,超声处理后的蛋白二级结构与SPI及其复合物(SPI- egcg、SPI- pd、SPI- egcg - pd)相比发生了显著变化。其中α-螺旋和β-片的含量显著降低,而无规螺旋的含量显著增加。同时,它们的乳化能力和抗氧化活性也显著提高(p
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Mechanism of emulsion stabilized by an ultrasonically prepared protein-polyphenol-polysaccharide complex: structure, functional properties and interfacial behavior.

Based on the mechanism that polyphenols and polysaccharides can modulate protein conformation through non-covalent interactions such as hydrogen bonding and hydrophobic forces, the construction of ternary complexes offers a promising strategy for developing efficient emulsion-based delivery systems. This study employed soy protein isolate (SPI), (-)-epigallocatechin gallate (EGCG), and polydextrose (PD) as raw materials to fabricate SPI, SPI-EGCG, SPI-PD, and SPI-EGCG-PD complexes via ultrasonic treatment. These complexes were then used to stabilize emulsions, and their structural characteristics, functional properties, and interfacial behavior were systematically investigated. The results indicated that the protein secondary structure of the ultrasonicated samples underwent significant alterations compared to SPI and the complexes (SPI-EGCG, SPI-PD, SPI-EGCG-PD). Specifically, the contents of α-helix and β-sheet decreased significantly, while the content of random coils increased significantly. Also, their emulsifying capacity and antioxidant activity were both significantly enhanced (p < 0.05). The emulsion stabilized by the ultrasonically prepared SPI-EGCG-PD complex exhibited superior stability, as evidenced by the highest emulsion stability index (89.6 min), the smallest particle size (599.6 nm), the highest absolute ζ-potential value (-37.4 mV), the greatest interfacial adsorbed protein content (4.89 mg/mL), the best oxidative stability (5.31 μmol/L), the lowest interfacial tension (20.89 mN/m), and the best storage stability. This study elucidates the mechanism by which ultrasonic treatment promotes the synergistic adsorption of proteins, polyphenols, and polysaccharides. It further examines the role of the interfacial behavior of ultrasonicated proteins and their complexes in maintaining emulsion stability, thereby providing a theoretical foundation for developing highly stable delivery systems for bioactive substances.

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来源期刊
Ultrasonics Sonochemistry
Ultrasonics Sonochemistry 化学-化学综合
CiteScore
15.80
自引率
11.90%
发文量
361
审稿时长
59 days
期刊介绍: Ultrasonics Sonochemistry stands as a premier international journal dedicated to the publication of high-quality research articles primarily focusing on chemical reactions and reactors induced by ultrasonic waves, known as sonochemistry. Beyond chemical reactions, the journal also welcomes contributions related to cavitation-induced events and processing, including sonoluminescence, and the transformation of materials on chemical, physical, and biological levels. Since its inception in 1994, Ultrasonics Sonochemistry has consistently maintained a top ranking in the "Acoustics" category, reflecting its esteemed reputation in the field. The journal publishes exceptional papers covering various areas of ultrasonics and sonochemistry. Its contributions are highly regarded by both academia and industry stakeholders, demonstrating its relevance and impact in advancing research and innovation.
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