Interactions of two food colourants with BSA: Analysis by Debye-Hückel theory.
作者： Tian Li , Zhengjun Cheng , Lijun Cao , Xiaohui Jiang , Lei Fan
DOI: 10.1016/J.FOODCHEM.2016.05.053
关键词:
摘要: Abstract We have focused on exploring pH- and ionic strength-modulated binding of acid red 1 (AR1) green 50 (AG50) with bovine serum albumin (BSA) by fluorescence, UV–vis absorption FTIR spectra. The results implied that the quenching mechanism BSA-AR1/AG50 system was a static quenching, electrostatic force dominated formation complex, affinity AR1 greater than AG50 subdomain IIA BSA. Moreover, their true thermodynamic constant (Keq), free energy change (ΔG0I→0), effective charge (ZP) in anion receptor pocket BSA were calculated using Debye-Huckel limiting law. local bound AR1/AG50 rather overall or surface played key role determining interaction strength. Besides, thermal structural stabilization discussed analyzing changes Tm Hurea without/with addition AR1/AG50, respectively.
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