Association Equilibrium of Methylene Blue by Spectral Titration and Chemometrics Analysis: A Thermodynamic Study

2009 ◽  
Vol 56 (3) ◽  
pp. 459-468 ◽  
Author(s):  
Jahan B. Ghasemi ◽  
M. Miladi
Keyword(s):  
Methylene Blue ◽  
Thermodynamic Study ◽  
Association Equilibrium ◽  
Spectral Titration

Removal of methylene blue from aqueous medium by citrate modified bagasse: Kinetic, Equilibrium and Thermodynamic study

2020 ◽  
Vol 11 ◽  
pp. 100463 ◽  
Author(s):  
Farid Mzee Mpatani ◽  
Aaron Albert Aryee ◽  
Alexander Nti Kani ◽  
Kang Wen ◽  
Evans Dovi ◽  
...  
Keyword(s):  
Methylene Blue ◽  
Aqueous Medium ◽  
Thermodynamic Study ◽  
Kinetic Equilibrium

Adsorption of methylene blue on chemically modified lychee seed biochar: Dynamic, equilibrium, and thermodynamic study

2020 ◽  
Vol 315 ◽  
pp. 113743 ◽  
Author(s):  
Sumanta Sahu ◽  
Souman Pahi ◽  
Sujata Tripathy ◽  
Satish Kumar Singh ◽  
Abhijit Behera ◽  
...  
Keyword(s):  
Methylene Blue ◽  
Dynamic Equilibrium ◽  
Thermodynamic Study ◽  
Chemically Modified

Thermodynamic Study of Methylene Blue Adsorption on Carbon Nanotubes Using Isothermal Titration Calorimetry: A Simple and Rigorous Approach

2017 ◽  
Vol 62 (2) ◽  
pp. 729-737 ◽  
Author(s):  
Paulo F. R. Ortega ◽  
João Paulo C. Trigueiro ◽  
Merly R. Santos ◽  
Ângelo M. L. Denadai ◽  
Luiz Carlos A. Oliveira ◽  
...  
Keyword(s):  
Carbon Nanotubes ◽  
Methylene Blue ◽  
Isothermal Titration Calorimetry ◽  
Thermodynamic Study ◽  
Titration Calorimetry ◽  
Methylene Blue Adsorption ◽  
Rigorous Approach

scholarly journals A Novel method for Thermodynamic Study on the Binding of Milk Carrier protein of BLG-A with Cr+3

2009 ◽  
Vol 11 (4) ◽  
pp. 24-29
Author(s):  
G. Behbehania ◽  
A. Divsalar ◽  
A. Saboury
Keyword(s):  
Binding Site ◽  
Equilibrium Constants ◽  
Thermodynamic Study ◽  
Titration Calorimetry ◽  
Carrier Protein ◽  
Novel Method ◽  
The Stability ◽  
New Equation ◽  
Β Lactoglobulin ◽  
Association Equilibrium

A Novel method for Thermodynamic Study on the Binding of Milk Carrier protein of BLG-A with Cr+3 Thermodynamics of the interaction between Cr3+ with β-lactoglobulin type A (BLG-A) was investigated at pH 7.0 and 37°C by isothermal titration calorimetry. A new method to follow the effect of Cr3+ on the stability of BLG-A was introduced. The new solvation model was used to reproduce the enthalpies of BLG-A+ Cr3+ interactions over the whole range of Cr3+ concentrations. The solvation parameters recovered from the new equation are attributed to the structural change of BLG-A and its biological activity. The results obtained indicate that there is a set of two identical binding sites for Cr3+ ions with positive cooperativity. The association equilibrium constants are 14.39 and 0.49 mM-1 for the first and second binding site, respectively. The enthalpy of binding for one mole of Cr+3 ion to one mole of the binding site on BLG-A (ΔH=104.60 kJ mol-1) is obtained.

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