Ultrasound-assisted assembly of β-lactoglobulin and chlorogenic acid for non covalent nanocomplex: fabrication, characterization and potential biological function
Jiayuan Liu, Gongshuai Song, Yawen Yuan, Like Zhou, Danli Wang, Tinglan Yuan +5 more
Ultrasonics Sonochemistry
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.
Extracted Claims
4 claims extracted from this paper into the knowledge graph
ultrasound treatment destroys structure of β-lactoglobulin
“ultrasound treatment could destroy the structure of LG, and the particle size of the protein was reduced to<50 nm.”
hydrophobic interaction binds β-lactoglobulin and chlorogenic acid
“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.”
ultrasound treatment reduces particle size of β-lactoglobulin
“ultrasound treatment could destroy the structure of LG, and the particle size of the protein was reduced to<50 nm.”