Thermodynamic study on the interaction of catechin with Jack bean urease

In this work complexation process between catechin and urease is examined using Isothermal Titration Calorimetry(ITC),The,at pH 7at 27°C in tris buffer.The enthalpies of urease +catechin interaction are reported and analysed in term of the Hill equation model.The thermodynamic parameters, enthalpy changes (ΔH) and entropy changes(ΔS) were calculated.These data suggested that hydrophobic interaction was the predominant intermolecular forces stabilizing the complex.,It was found that urease has two positively cooperative binding site for catechin. Ka values show catechin in the second binding sites has higher affinity for binding than the first binding sites.

Keywords:

urease , catechin , Isothermal Titration Calorimetry , folding.