Fast Green FCF (FCF), Patent Blue V (PBV) and Acid Blue 1 (AB1) are used as food colorants. Multiple spectroscopic techniques were employed to probe in depth the affinity of FCF/PBV/AB1 with BSA in different pH and/or salt concentrations. The results showed that FCF/PBV/AB1 quenched the intrinsic fluorescence of BSA by a static process, and electrostatic force dominated the formation of BSA-FCF/PBV/AB1 complex which was confirmed by the effects of salt on their interactions. Subdomain IIA was the primary binding site for FCF/PBV/AB1 on BSA in the pH range of 5.5-7.4, while both Trp 212 and Trp 134 residues of BSA might be bound by FCF/PBV/AB1 at pH 4.8. The K values suggested that the binding ability of three food colorants with BSA was FCF>PBV>AB1. The results of UV-vis absorption, synchronous fluorescence, 3D fluorescence and FT-IR spectra proved that the structure of BSA altered by FCF/PBV/AB1.
Keywords: Acid Blue 1; Binding constant; Bovine serum albumin; Fast Green FCF; Patent Blue V; Spectroscopic techniques.
Copyright © 2015 Elsevier Ltd. All rights reserved.