Functional and conformational changes to soy proteins accompanying anthocyanins: Focus on covalent and non-covalent interactions

Food Chemistry
Xiaonan SuiLianzhou Jiang

Abstract

The present study was aimed to evaluate the interaction between anthocyanins from black rice and soybean protein isolate (SPI) via non-covalent and covalent bindings and the impact of these interactions on the functional and conformational changes of soybean protein. The conformational changes of the protein structure with different concentrations of anthocyanins (0.05, 0.1%, and 0.2%) were analyzed using three-dimensional fluorescence and Fourier transform infrared spectroscopy. The anthocyanins were more likely to form covalent interactions with SPI instead of non-covalent interactions. The addition of anthocyanins changed the secondary structure of SPI with a decrease in β-sheets and an increase in β-turns and random coils. The emulsifying and foaming properties of SPI were improved after complexation with anthocyanins. This study might be useful for elucidating the mechanisms behind the binding of anthocyanins with SPI and the possible uses of SPI-anthocyanin complexes in food formulations.

Citations

Jun 13, 2018·Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry·Xuelian BaiHuawei Zhang
Dec 19, 2020·Journal of the Science of Food and Agriculture·Jingjing XuZhi Zheng
Dec 16, 2020·Annual Review of Food Science and Technology·Xiaonan SuiLianzhou Jiang
Oct 17, 2020·Food Science and Technology International = Ciencia Y Tecnología De Los Alimentos Internacional·Jia LiHaoran Zhang
May 17, 2021·Food Research International·Telmo FranciscoVictor de Freitas

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