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超声辅助组装β-乳球蛋白和绿原酸形成非共价纳米复合物:制备、表征及潜在生物学功能。

Ultrasound-assisted assembly of β-lactoglobulin and chlorogenic acid for non covalent nanocomplex: fabrication, characterization and potential biological function.

机构信息

Zhejiang Provincial Key Lab for Biological and Chemical Processing Technologies of Farm Product, School of Biological and Chemical Engineering, Zhejiang University of Science and Technology, Hangzhou, Zhejiang 310023, China.

College of Grain Science and Technology, Shenyang Normal University, Shenyang 110034, China.

出版信息

Ultrason Sonochem. 2022 May;86:106025. doi: 10.1016/j.ultsonch.2022.106025. Epub 2022 May 5.

DOI:10.1016/j.ultsonch.2022.106025
PMID:35533432
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC9092509/
Abstract

It is essential to understand the ultrasound-induced changes in assembly of proteins and polyphenols into non covalent nanocomplex. β-Lactoglobulin (LG) and chlorogenic acid (CA) with various biological activities can be combined to form food-grade nanocomplexes. This study systematically explored the role of high-intensity ultrasound pretreatment on the binding mechanisms of LG and CA, and the potential biological function for embedding curcumin (Cur). The scanning electron microscopy (SEM) revealed that ultrasound treatment could destroy the structure of LG, and the particle size of the protein was reduced to<50 nm. The change in secondary structure of the protein by ultrasound treatment could be revealed by the fourier transform infrared (FTIR) and fluorescence spectra. Besides, it was found that LG and CA were combined to form a complex under the hydrophobic interaction, and CA was bound in the internal cavity of LG with a relatively extended conformation. The result demonstrated that the ratio of Cur embedded in the ultrasonic sample could be effectively increased by 7% - 10%, the particle size in the emulsion was smaller, and the dispersion was more stable. This work contributes to the development of protein-polyphenol functional emulsion systems with the ability to deliver Cur.

摘要

了解超声诱导蛋白质和多酚组装成非共价纳米复合物的变化是至关重要的。具有各种生物活性的β-乳球蛋白(LG)和绿原酸(CA)可以结合形成食品级纳米复合物。本研究系统地探讨了高强度超声预处理对 LG 和 CA 结合机制的作用,以及嵌入姜黄素(Cur)的潜在生物学功能。扫描电子显微镜(SEM)显示,超声处理可以破坏 LG 的结构,使蛋白质的粒径减小到<50nm。傅里叶变换红外(FTIR)和荧光光谱可以揭示超声处理引起的蛋白质二级结构变化。此外,发现 LG 和 CA 是通过疏水相互作用结合形成复合物的,CA 以相对伸展的构象结合在 LG 的内部腔中。结果表明,通过超声处理,嵌入到样品中的 Cur 比例可以有效增加 7%-10%,乳液中的颗粒更小,分散更稳定。这项工作有助于开发具有递送 Cur 能力的蛋白质-多酚功能乳液系统。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c1ea/9092509/9dc245a7a3c5/gr7.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c1ea/9092509/024c3c6848b5/ga1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c1ea/9092509/03934f589c32/gr1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c1ea/9092509/c449d348a485/gr2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c1ea/9092509/77098f3ab51d/gr3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c1ea/9092509/6942f68f40f6/gr4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c1ea/9092509/4234d52c8d2d/gr5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c1ea/9092509/2604f10f2ea2/gr6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c1ea/9092509/9dc245a7a3c5/gr7.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c1ea/9092509/024c3c6848b5/ga1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c1ea/9092509/03934f589c32/gr1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c1ea/9092509/c449d348a485/gr2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c1ea/9092509/77098f3ab51d/gr3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c1ea/9092509/6942f68f40f6/gr4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c1ea/9092509/4234d52c8d2d/gr5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c1ea/9092509/2604f10f2ea2/gr6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c1ea/9092509/9dc245a7a3c5/gr7.jpg

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