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Published on: July 15, 2019
Interactions and binding mechanisms of soy protein isolate with theasinensin A in different pH conditions by
Haoyu Zhang1, Weiqi Xu1, Yulu Wang1
1College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, Jiangsu, China.
Abstract:
Soy protein isolate (SPI) may interact with polyphenols, but pH influences the interaction. Theasinensin A (TSA), a dimer of epigallocatechin gallate, has enhanced functional properties, while its combinations with SPI have been paid little attention. Therefore, their interactions under different pH (4.5, 7.0 and 9.5) were investigated for the first time in this study. UV-vis absorption spectral results indicated that the combinations altered the microenvironment of SPI. Fluorescence results revealed that Ka value was the highest at pH 9.5 (3.92 × 106 L/mol), and the quenching mechanism was predominately static. Hydrogen bonds played a key role under varying pH. The combinations modified the secondary structure of SPI, α-helix content increasing from 6.31% to 8.75% at pH 4.5 after binding, while rose from 6.16% to 7.78% at pH 7.0. The outcome of molecular docking proved the presence of interactions. This work provided the theoretical basis for application of SPI-TSA complexes.
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