Multi-spectroscopic and molecular modeling studies of bovine serum albumin interaction with sodium acetate food additive.

Author(s) Mohammadzadeh-Aghdash, H.; Dolatabadi, J.Ezzati Naz; Dehghan, P.; Panahi-Azar, V.; Barzegar, A.
Journal Food Chem
Date Published 2017 Aug 01

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 (1.09×10(3) at 310°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.

DOI 10.1016/j.foodchem.2017.01.149
Keywords Animals; Cattle; Food Additives; Models, Molecular; Molecular Docking Simulation; Serum Albumin, Bovine; Sodium Acetate; Spectrometry, Fluorescence
ISSN 0308-8146
Citation Food Chem. 2017;228:265269.

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