کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
7587948 | 1492081 | 2016 | 8 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Interactions of two food colourants with BSA: Analysis by Debye-Hückel theory
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کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی آنالیزی یا شیمی تجزیه
پیش نمایش صفحه اول مقاله
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چکیده انگلیسی
We have focused on exploring pH- and ionic strength-modulated binding of acid red 1 (AR1) and acid green 50 (AG50) with bovine serum albumin (BSA) by fluorescence, UV-vis absorption and FTIR spectra. The results implied that the quenching mechanism of BSA-AR1/AG50 system was a static quenching, electrostatic force dominated the formation of BSA-AR1/AG50 complex, and the binding affinity of AR1 was greater than that of AG50 on the subdomain IIA of BSA. Moreover, their true thermodynamic binding constant (Keq), true free energy change (ÎG0Iâ0), and effective charge (ZP) in the anion receptor pocket of BSA were calculated using Debye-Hückel limiting law. The local charge bound by AR1/AG50 rather than the overall or surface charge of BSA played a key role in determining their interaction strength. Besides, the thermal and structural stabilization of BSA was discussed by analyzing the changes of Tm and Hurea without/with the addition of AR1/AG50, respectively.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Food Chemistry - Volume 211, 15 November 2016, Pages 198-205
Journal: Food Chemistry - Volume 211, 15 November 2016, Pages 198-205
نویسندگان
Tian Li, Zhengjun Cheng, Lijun Cao, Xiaohui Jiang, Lei Fan,