Table 2. Thermodynamic parameters obtained from ITC titration of natural β-lactoglobulin and its mutants with DSM at 293 K.
N, stoichiometry; K d, dissociation constant; ΔH a, enthalpy change; ΔS a, entropy change. The errors shown are the errors of fitting the data to the one set of binding sites model.
| Natural (pH 7.5) | FAF (pH 7.5) | FAW (pH 7.5) | FAF (pH 8.5) | |
|---|---|---|---|---|
| N | 0.91 ± 0.08 | 0.94 ± 0.06 | 0.92 ± 0.05 | 1.21 ± 0.08 |
| K d (µM) | 55 ± 9 | 43 ± 6 | 31 ± 6 | 39 ± 5 |
| ΔH a (cal mol−1) | −1298 ± 145 | −1634 ± 133 | −1792 ± 137 | −614 ± 53 |
| ΔS a (cal mol−1 K−1) | 15.0 | 14.4 | 14.5 | 18.1 |
| TΔS a (cal mol−1) | 4395.0 | 4219.2 | 4248.5 | 5303.3 |