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

Ultrasound-assisted assembly of β-lactoglobulin and chlorogenic acid for non covalent nanocomplex: fabrication, characterization and potential biological function.
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用于非共价纳米复合物的β-乳球蛋白和绿原酸的超声辅助组装:制造、表征和潜在的生物学功能

DOI:
10.1016/j.ultsonch.2022.106025
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发表时间:
2022-05
影响因子:
8.4
通讯作者:
Gong, Jinyan
Gong, Jinyan
中科院分区:
化学1区
文献类型:
--
作者:
Liu, Jiayuan;Song, Gongshuai;Yuan, Yawen;Zhou, Like;Wang, Danli;Yuan, Tinglan;Li, Ling;He, Guanghua;Yang, Qingyu;Xiao, Gongnian;Gong, Jinyan

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用超声波研究了LG与CA的相互作用。超声波可以破坏LG的二级结构。超声波促进了LG与CA的结合,与CA结合可以显著改善LG的理化性能。LG和LG- ca可以作为传递载体进一步传递Cur.有必要了解超声诱导的蛋白质和多酚组装成非共价纳米复合物的变化。具有多种生物活性的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。本研究系统探讨了高强度超声预处理对LG和CA结合机制的影响,以及姜黄素(curcumin, Cur)包埋的潜在生物学功能。扫描电镜(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<50 nm。利用傅里叶变换红外光谱和荧光光谱分析了超声处理后蛋白质二级结构的变化。此外,发现LG和CA在疏水相互作用下结合形成配合物,CA结合在LG的内腔中,构象相对延伸。结果表明,超声样品中Cur的包埋率可有效提高7% ~ 10%,乳液中的粒径更小,分散更稳定。这项工作有助于开发具有传递Cur能力的蛋白质-多酚功能乳液体系。
The interaction between LG and CA by ultrasound was studied. Ultrasound can destroy the secondary structure of LG. Ultrasound promotes the combination of LG and CA. Combining with CA can significantly improve the physical and chemical properties of LG. LG and LG-CA can be used as delivery carriers to further deliver Cur. 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.
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