Journal
FOOD CHEMISTRY
Volume 136, Issue 2, Pages 442-449Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2012.09.026
Keywords
Amaranth; Human serum albumin; Fluorescence spectroscopy; Fourier-transform infrared spectroscopy; Interaction
Funding
- National Natural Science Foundation of China [31060210, 21167013]
- Supported Program of Science and Technology of Jiangxi Province [2009BNA09000, 2010BSA17400, 20112BBF60010]
- Natural Science Foundation of Jiangxi Province [20114BAB204019]
- State Key Laboratory of Food Science and Technology of Nanchang University [SKLF-KF-201203, SKLF-MB-201002]
- Foundation of Jiangxi Provincial Office of Education [GJJ11287]
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The mechanism of interaction between food dye amaranth and human serum albumin (HSA) in physiological buffer (pH 7.4) was investigated by fluorescence, UV-vis absorption, circular dichroism (CD), and Fourier transform infrared (FT-IR) spectroscopy. Results obtained from analysis of fluorescence spectra indicated that amaranth had a strong ability to quench the intrinsic fluorescence of HSA through a static quenching procedure. The negative value of enthalpy change and positive value of entropy change elucidated that the binding of amaranth to HSA was driven mainly by hydrophobic and hydrogen bonding interactions. The surface hydrophobicity of HSA increased after binding with amaranth. The binding distance between HSA and amaranth was estimated to be 3.03 nm and subdomain IIA (Sudlow site I) was the primary binding site for amaranth on HSA. The results of CD and FT-IR spectra showed that binding of amaranth to HSA induced conformational changes of HSA. (C) 2012 Elsevier Ltd. All rights reserved.
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