Thermal Study of a Newly Synthesized Cu(II) Complex Binding to Bovine 𝛽-Lactoglobulin

Table 1

Binding parameters for BLG + Cu(II) complex interaction recovered from (1) and (2) at different temperatures of 298 and 310 K. 𝑝=1 indicates that the binding is noncooperative in the four binding sites. The negative values of 𝛿^𝜃𝐴 or 𝛿^𝜃𝐵 indicate that the low and high concentrations of Cu(II) complex destabilize the BLG structure. The interaction is strong as indicated by equilibrium association constants. The interaction is entropy driven, indicating that the hydrophobic forces are dominant in this interaction.

Parameters	𝑇=298 K	𝑇=310 K
𝐾𝑎/Lmol^−1	3.92×10^4±42	1.07×10^5±42
𝑔	4	4
𝑝	1.00±0.01	1.00±0.01
𝛿^𝜃𝐴	−3.49±0.11	−9.95±0.15
𝛿^𝜃𝐵	−5.47±0.11	−22.02±0.16
Δ𝐻/kJmol^−1	19.23±0.05	53.82±0.25
Δ𝐺/kJmol^−1	−26.38±0.04	−28.88±0.08
Δ𝑆/kJmol^−1K^−1	0.15±0.01	0.27±0.02