Thermodynamic Studies on the Interaction of Cobalt with Alpha‐Amylase

Abstract

The interaction of α‐amylase from Bacillus amyloliquefaciens with divalent cobalt ion was studied by equilibrium dialysis and isothermal titration microcalorimetry methods at 27 °C in neutral solution at pH = 7.0. A new equation with a useful graphical method, very similar to the Scatchard plot was introduced to obtain a dissociation equilibrium constant using microcalorimetric data. The constant is remarkably like that obtained from a normal Scatchard plot, which uses equilibrium dialysis data. The enzyme activity increased significantly with an increasing concentration of cobalt; however, the temperature of denaturation of the enzyme decreased.

A review on the ligand binding studies by isothermal titration calorimetry

“…By a double reciprocal linear plot of 1/q vs. 1/[L], two important thermodynamic parameters of ΔH and K can be (4) and (5) have been used extensively in the enzyme inhibition [33,35,50], metal [6,71] and sugar binding to proteins studies [48,50]. For the total heat of reaction (q) due to the isothermal titration of macromolecule by solution containing the two ligands I and X, equation (3) should be written with two terms as follows [72]:…”

“…Thermodynamic analysis of the observed heat effects that permits quantitative characterization of the energetic processes is associated with the binding reaction. ITC gives invaluable information about biomacromolecule-ligand interaction [6][7][8][9][10][11][12][13][14][15][16][17][18][19][20][21][22][23], protein denaturation [24][25][26][27][28], allosteric transition [29][30], enzyme inhibition [31][32][33][34][35], quality, safety and shelf-life of materials and material stability [36][37][38][39][40][41]. Different methods have been reported for data analysis of ligand binding study by ITC [42][43][44][45][46][47][48][49][50][51][52]…”

A Thermodynamic Study on the Binding of Cobalt Ion with Myelin Basic Protein

“…One of the most powerful techniques useful to obtain additional information about the structure of proteins in biophysical chemistry field is Isothermal Titration Calorimetry (ITC). [1][2][3][4] ITC gives invaluable information about biomacromolecule-ligand interaction, [5][6][7][8][9][10][11][12][13][14][15][16][17][18][19][20][21][22] protein denaturation. [23][24][25][26][27] During the last six years we attempt to study the metal ion binding study on different proteins.…”

Application of a new method for data analysis of isothermal titration calorimetry in the interaction between human serum albumin and Ni2+

“…A thermodynamic analysis of the observed heat effects permits a quantitative characterization of the energetic processes associated with the binding reaction [4]. ITC gives valuable information on biomacromolecule-ligand interaction [5][6][7], allosteric transition [8], protein denaturation [9][10][11], enzyme inhibition [12,13], quality, safety and the shelf-life of materials and material stability [14][15][16][17].…”