Exploring the Binding Mechanism of Soybean Protein-Baicalein Including Changes in Protein Conformation and Function

Abstract

Abstract: To explore the binding mechanism of β-conglycinin (7S)/glycinin (11S) in soybean protein components with baicalein, and to investigate the changes of the conformation and functional properties of the complex. Fourier transform infrared spectroscopy indicated that baicalein induced the transformation of β-sheets into α-helices and random coils. Intrinsic fluorescence spectra confirmed that the addition of baicalein made the 7S、11S structure tighter. The reaction of baicalein with the protein proceeded spontaneously and quenched the protein fluorescence in a static manner. The 7S、11S proteins bound to baicalein by hydrogen bonds and hydrophobic interactions, respectively. The affinity of baicalein to 11S was higher than that of 7S by molecular docking. Scanning electron microscopy showed the microstructure difference between 7S、11S and complex. In addition, the surface hydrophobicity of 7S、11S decreased and the thermal stability and other functional properties of complex were improved after combining with baicalein.

Key words: β-conglycinin (7S), glycinin (11S), baicalein, binding mechanism, conformational change, functional properties

CLC Number:

TS.214.2

Xin-Yue YAN Jinjie Yang Babich Olga li yang. Exploring the Binding Mechanism of Soybean Protein-Baicalein Including Changes in Protein Conformation and Function[J]. FOOD SCIENCE, 0, (): 0-0.

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