The effect of glucose (0–15 mass%) on the kinetics of bovine serum albumin (BSA) denatured aggregation at high concentration
in aqueous solution has been studied by differential scanning calorimetry. The observed denatured aggregation process was
irreversible and could be characterized by a denaturation temperature (Tm), apparent activation energy (Ea), the approximate order of reaction, and pre-exponential factor (A). As the glucose concentration increased from 0 to 15 mass%, Tm increased, Ea also increased from 514.59409±6.61489 to 548.48611±7.81302 kJ mol−1, and A/s−1 increased from 1.24239E79 to 5.59975E83. The stabilization increased with an increasing concentration of glucose, which was
attributed to its ability to alter protein denatured aggregation kinetics.
The kinetic analysis was carried out using a composite procedure involving the iso-conversional method and the master plots
method. The iso-conversional method indicated that denatured aggregation of BSA in the presence and absence of glucose should
conform to single reaction model. The master plots method suggested that the simple order reaction model best describe the
process. This study shows the combination of iso-conversional method and the master plots method can be used to quantitatively
model the denatured aggregation mechanism of the BSA in the presence and absence of glucose.