2-2--azino-di-(3-ethylbenzothiazoline)-6-sulfonic-acid and malvidin-3-galactoside

This study investigates the effects of bovine serum albumin (BSA) on blueberry anthocyanins and their interaction. Findings showed that BSA could protect blueberry anthocyanins against degradation and retain their antioxidant activity at an ideal concentration of 0.15 mg/mL under three deteriorating treatments: illumination, vitamin C + illumination, and sucrose + illumination. The fluorescence and UV absorption spectra showed that malvidin-3-o-galactoside (M3G), the major monomer in blueberry anthocyanins, led to a static quenching of BSA and the binding site of M3G to BSA was approximately one. Further, the interaction was a spontaneous process with electrostatic interactions being the main force. CD spectra and synchronous fluorescence spectra presented alterations in the secondary structure and microenvironment of Trp and Tyr residues of BSA, respectively, upon interaction with M3G. Finally, molecular docking analysis showed that M3G mainly bound the II and III domains of BSA by hydrogen bonds and electrostatic interaction. In conclusion, our study highlights the protective effects of BSA on the stability and anti-oxidant activity of blueberry anthocyanins and their interaction analysis.

Topics: Anthocyanins; Antioxidants; Ascorbic Acid; Benzothiazoles; Binding Sites; Blueberry Plants; Circular Dichroism; Hydrogen Bonding; Light; Molecular Docking Simulation; Serum Albumin, Bovine; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet; Static Electricity; Sucrose; Sulfonic Acids; Thermodynamics; Tryptophan; Tyrosine