STRUCTURAL INVESTIGATION OF THE INTERACTION BETWEEN BOVINE SERUM ALBUMIN AND ACID GELATIN IN WATER - Biochemistry and Biotechnology: Research and Development - page 73

Figure 9. Antonov et al. “Structural investigation of the interaction between bovine serum albumin and
acid gelatin in water”.
Figure 10. Antonov et al. “Structural investigation of the interaction between bovine serum albumin and
acid gelatin in water”.
3.4. Thermal Denaturation (DSC Measurements)
The DSC trace of thermal denaturation of BSA alone and in the presence of gelatin at
different q values at pH 5.4 is shown in Figure 10. The reversibility of the unfolding process
was checked by reheating the sample after it had been cooled to room temperature in the
calorimeter. If the BSA solution is heated up to 100 °C or higher denaturation is irreversible.
However, as judged by the area of DSC curve, the denaturation should be essentially
reversible, provided the first heating was not carried on above the temperature at which the
denaturation is effectively complete. Sturtevant and co-workers,[32-34] , Sanchez-Ruiz, [35]
and Galisteo et al [36] have shown that the usual thermodynamic evaluation methods are
applicable in cases where the irreversible steps do not take place during the time the protein
spends in the temperature range of DSC transition, but occur at somewhat higher
temperatures. It is thus permissible to apply equilibrium thermodynamics for the evaluation of
thermodynamic parameters as function of the BSA/gelatin weight ratio. The thermal scan of
for the BSA solution yields a symmetric peak (Figure 10). The calorimetric data were
analyzed using the MicroCal Origin software, according to the methodology recommended by
JUPAC [37] . The parameters obtained in this manner are collected in Table 1.