Multispectroscopic studies on the interaction of 2-tert-butylhydroquinone (TBHQ), a food additive, with bovine serum albumin

被引：174

作者：

Shahabadi, Nahid ^{[1
]}

Maghsudi, Maryam ^{[1
]}

Kiani, Zahra ^{[1
]}

Pourfoulad, Mehdi ^{[1
]}

机构：

[1] Razi Univ, Dept Chem, Fac Sci, Kermanshah, Iran

来源：

FOOD CHEMISTRY | 2011年 / 124卷 / 03期

关键词：

TBHQ; BSA; Fluorescence quenching; Circular dichroism; FT-IR; FLUORESCENCE; BINDING; SPECTROSCOPY; PROTEINS;

D O I：

10.1016/j.foodchem.2010.07.079

中图分类号：

O69 [应用化学];

学科分类号：

081704 ;

摘要：

The interaction of 2-tert-butylhydroquinone (TBHQ) and bovine serum albumin (BSA) was investigated by spectrophotometry, spectrofluorimetry, circular dichroism (CD) and FT-IR techniques. The experimental results indicated that the quenching mechanism of BSA by TBHQ was a static procedure. Various binding parameters were evaluated. The negative value of Delta H, positive value of Delta S and the negative value of Delta G indicated that hydrophobic and hydrogen bonding interactions play major roles in the binding of TBHQ and BSA. Based on Forster's theory of non-radiation energy transfer, the binding distance, r, between the donor (BSA) and acceptor (TBHQ) was evaluated. The results of CD, UV-vis and FT-IR spectroscopy showed that the binding of TBHQ to BSA induced conformational changes in BSA. (C) 2010 Elsevier Ltd. All rights reserved.

引用

页码：1063 / 1068

页数：6

共 35 条

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