The heat-induced denaturation process of soy protein includes the changes in its secondary structure (i.e., the exposure of hydrophobic region to the surface) and the dissociation and reassociation between proteins. Upon heating, the protein aggregation driven by hydrophobic interaction exhibits the fluorescence quenching effect, which significantly lowers the quantum yield of fluorescence (Shen & Tang, 2012). As shown in Fig. 4, the blanching treatment resulted in an increase in the quantum yield of fluorescence, thus suggesting a relatively high extent of protein denaturation and exposure of tryptophan residues but a low fluorescence quenching effect in relation to the protein–solvent or protein–protein interactions. Therefore, the results demonstrate that in comparison with the traditional method, the blanching treatment leads to high protein denaturation and low quenching-effect interactions.