The interaction between tannic acid and soy protein isolate was examined at a molecular level by the means of fluorescence, ultraviolet-visible and circular dichroism spectra. The results suggested that tannic acid had a strong ability to quench the intrinsic fluorescence of soy protein isolate. When the concentration of tannic acid was below 6×10-6 mol/L (mass fraction 5.1% based on soy protein isolate), the quenching mechanism was mainly a static quenching. In contrast, when the concentration of tannic acid was above 6×10-6 mol/L, the quenching mechanism included both static and dynamic quenching. Hydrophobic force played a major role in the binding of tannic acid and soy protein isolate, and led the microenvironment of tryptophan and tyrosine residues of soy protein isolate more hydrophilic, but had no significant effect on the secondary structures of soy protein isolate. |