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Updated: Feb 16, 2026

Covalent Immobilization of Proteins for the Single Molecule Force Spectroscopy
Published on: August 20, 2018
Functional and conformational changes to soy proteins accompanying anthocyanins: Focus on covalent and non-covalent
Xiaonan Sui1, Hongbo Sun2, Baokun Qi1
1College of Food Science, Northeast Agricultural University, Harbin 150030, China; National Research Center of Soybean Engineering and Technology, Harbin 150030, China.
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.
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