Multispectroscopic studies on the interaction of maltol, a food additive, with bovine serum albumin

被引：166

作者：

Zhang, Guowen ^{[1
]}

Ma, Yadi ^{[1
]}

Wang, Lin ^{[1
]}

Zhang, Yepeng ^{[1
]}

Zhou, Jia ^{[1
]}

机构：

[1] Nanchang Univ, State Key Lab Food Sci & Technol, Nanchang 330047, Jiangxi, Peoples R China

来源：

FOOD CHEMISTRY | 2012年 / 133卷 / 02期

基金：

中国国家自然科学基金;

关键词：

Maltol; Bovine serum albumin; Fluorescence quenching; Binding site; Circular dichroism; SPECTROSCOPIC METHODS; BINDING-SITES; DRUG; ALPINETIN;

D O I：

10.1016/j.foodchem.2012.01.014

中图分类号：

O69 [应用化学];

学科分类号：

081704 ;

摘要：

The interaction between maltol, a food additive, and bovine serum albumin (BSA) under simulated physiological conditions was investigated by fluorescence, UV-Vis absorption, circular dichroism (CD) and Fourier transform infrared (FT-IR) spectroscopy. The results suggested that the fluorescence quenching of BSA by maltol was a static procedure forming a maltol-BSA complex. The positive values of enthalpy change and entropy change indicated that hydrophobic interactions played a predominant role in the interaction of maltol with BSA. The competitive experiments of site markers revealed that the binding of maltol to BSA mainly took place in subdomain IlA (Sudlow site l). The binding distance between maltol and BSA was 3.01 nm based on the Forster theory of non-radioactive energy transfer. Moreover, the results of UV-Vis, synchronous fluorescence, CD and FT-IR spectra demonstrated that the microenvironment and the secondary structure of BSA were changed in the presence of maltol. (C) 2012 Elsevier Ltd. All rights reserved.

引用

页码：264 / 270

页数：7

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