Study on the interaction between bovine serum albumin and starch nanoparticles prepared by isoamylolysis and recrystallization

The current study primarily investigated the interaction of bovine serum albumin (BSA) with starch nanoparticles (SNPs) prepared by isoamylolysis and recrystallization using UV-vis, fluorescence, transmission electron microscopy (TEM), Fourier transform infrared (FTIR) and circular dichroism (CD). The enhanced absorbance observed by UV-vis spectroscopy and decreased intensity of fluorescence spectroscopy suggested that BSA could bind to SNPs and form a BSA-SNP complex. The synchronous fluorescence spectra revealed that the emission maximum of Tyr residue (at Δλ=15nm) was red-shifted at the investigated concentrations range, indicating that the conformation of BSA was changed. Quenching parameters showed that the quenching effect of SNPs was static quenching. TEM images showed that the SNPs were surrounded by protein coronae, indicating that nanoparticle-protein complexes had formed. The FTIR and CD characterization indicated that the SNPs induced structural changes in the secondary structure of BSA.