Spectroscopic Analysis of Interaction between Bovine Serum Albumin and Anthocyanin

doi:10.7506/spkx1002-6630-201323002

Abstract

Abstract:

The interaction between anthocyanin and bovine serum albumin (BSA) was studied by UV-Vis, fluorescence and
Fourier transform infrared spectroscopy (FT-IR). The results suggested that anthocyanin had a strong ability to quench the
BSA fluorescence in a static mode. The binding constants (KA) and site numbers (n) obtained at different temperatures were
2.218 × 104, 1.084 (298 K); 1.770 × 104, 1.065 (306 K) and 1.706 × 104, 1.086 (310 K), respectively. According to the
thermodynamic parameters, electrostatic forces played a dominant role in the interaction between anthocyanin and BSA. The
distance between donor and acceptor in anthocyanin-BSA complex was calculated as 2.1 nm, based on the equations from
Förster nonradiative energy transfer theory. The synchronous fluorescence spectra revealed that anthocyanin interacted with
tryptophan residues in BSA, and the vicinity of tryptophan residues was more hydrophobic. The FT-IR spectra revealed that
conformational changes of BSA were caused by anthocyanin, thus leading to structural changes of α-helix.

Key words: anthocyanin, bovine serum albumin, fluorescence spectroscopy, UV-Vis spectroscopy, Fourier transform infrared spectroscopy

CLC Number:

TS201.4

YAO Hui-fang，JING Hao*. Spectroscopic Analysis of Interaction between Bovine Serum Albumin and Anthocyanin[J]. FOOD SCIENCE, 2013, 34(23): 6-10.

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