期刊
FOOD CHEMISTRY
卷 228, 期 -, 页码 265-269出版社
ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2017.01.149
关键词
Sodium acetate; Bovine serum albumin; Fluorescence quenching; Molecular docking
资金
- Tabriz University of Medical Sciences, Tabriz, Iran [117]
Sodium acetate (SA) has been used as a highly effective protectant in food industry and the possible effect of this additive on the binding to albumin should be taken into consideration. Therefore, for the first time, the mechanism of SA interaction with bovine serum albumin (BSA) has been investigated by multi spectroscopic and molecular modeling methods under physiological conditions. Stern-Volmer fluorescence quenching analysis showed an increase in the fluorescence intensity of BSA upon increasing the amounts of SA. The high affinity of SA to BSA was demonstrated by a binding constant value (1.09 x 10(3) at 310 degrees K). The thermodynamic parameters indicated that hydrophobic binding plays a main role in the binding of SA to Albumin. Furthermore, the results of UV-vis spectra confirmed the interaction of this additive to BSA. In addition, molecular modeling study demonstrated that A binding sites of BSA play the main role in the interaction with acetate. (C) 2017 Elsevier Ltd. All rights reserved.
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