In fluorescence titration, it was assumed that sub-fractions of molecules in FA had consistent fluorescence characteristics. Intensification of fluorescence intensity and the concentrations of [HL] was described linearly (Equation B5). (B5) where: indicated the maximum fluorescence intensity of peaks in EEM recorded at pH 7.0 F0 and normalized by concentration of sub-fractions of FA in the study; indicated the F fluorescence intensity during titration; indicated the fluorescence intensity at the end of Fend titration. From equation (B4) and (B5), (B6) Letting in combination with equation (B6), Equation (B7) can be obtained: f= (B7) Where: represents the fluorescence intensity of peaks in D-EEMs at acidic pH range of ∆F 7.5-11.5; represents the fraction of the initial EEM fluorescence that corresponding to the f binding fluorophores. and can be solved by plotting against 1/[H] using SigmaPlot f Ka2 F0/∆F 12.5 software.
In fluorescence titration, it was assumed that sub-fractions of molecules in FA had consistent fluorescence characteristics. Intensification of fluorescence intensity and the concentrations of [HL] was described linearly (Equation B5). (B5) where: F0 indicated the maximum fluorescence intensity of peaks in EEM recorded at pH 7.0 and normalized by concentration of sub-fractions of FA in the study; F indicated the fluorescence intensity during titration; Fend indicated the fluorescence intensity at the end of titration. From equation (B4) and (B5), (B6) Letting f= in combination with equation (B6), Equation (B7) can be obtained: (B7) Where: ∆F represents the fluorescence intensity of peaks in D-EEMs at acidic pH range of 7.5-11.5; f represents the fraction of the initial EEM fluorescence that corresponding to the binding fluorophores. f and Ka2 can be solved by plotting F0/∆F against 1/[H] using SigmaPlot 12.5 software.
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