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大豆蛋白分离物-矢车菊素-3-半乳糖苷通过超声诱导自由基产生的物理化学性质。

Physicochemical properties of soy protein isolates-cyanidin-3-galactoside conjugates produced using free radicals induced by ultrasound.

机构信息

School of Pharmacy, Nanjing University of Chinese Medicine, Nanjing 210023, PR China.

College of Food Science and Light Industry, Nanjing Tech University, Nanjing 211816, PR China.

出版信息

Ultrason Sonochem. 2020 Jun;64:104990. doi: 10.1016/j.ultsonch.2020.104990. Epub 2020 Jan 28.

DOI:10.1016/j.ultsonch.2020.104990
PMID:32018136
Abstract

Free radicles produced by ultrasound were used to produce soy protein isolate (SPI)-cyanidin-3-galactoside conjugates. The conjugation between SPI and cyanidin-3-galactoside was confirmed by the increased ratio of bound polyphenol and the disappearance of cyanidin-3-galactoside's absorption peak in ultraviolet-visible spectrum. Conjugation with cyanidin-3-galactoside resulted in breakdown of SPI aggregate, which also led to a decrease in particle size and an increase in fluorescence intensity. Conjugation disrupted the hydrogen bonds of SPI as indicated by the lowest band intensity at 1646, 1533 and 3300-3450 cm on FTIR spectra. Conjugation also increased the electrostatic repulsion and decreased the hydrophobic interactions between SPI molecules. The SPI-cyanidin-3-galactoside conjugate had higher solubility and less aggregated structure in aqueous medium. The aqueous dispersions and solid powders of these conjugates had better thermal stability than that of SPI.

摘要

超声产生的自由基被用来制备大豆分离蛋白(SPI)-矢车菊素-3-半乳糖苷缀合物。SPI 与矢车菊素-3-半乳糖苷的缀合通过结合多酚比例的增加以及紫外可见光谱中矢车菊素-3-半乳糖苷吸收峰的消失得到证实。与矢车菊素-3-半乳糖苷的缀合导致 SPI 聚集物的分解,这也导致粒径减小和荧光强度增加。如傅里叶变换红外光谱中 1646、1533 和 3300-3450cm 处最低波段强度所示,缀合破坏了 SPI 的氢键。共轭还增加了 SPI 分子之间的静电排斥和减少了疏水相互作用。SPI-矢车菊素-3-半乳糖苷缀合物在水介质中具有更高的溶解度和更少的聚集结构。这些缀合物的水分散体和固体粉末比 SPI 具有更好的热稳定性。

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