The kinetics of protein thermal transition is of a significant interest from the standpoint of medical treatment. The effect of sucrose (0–15 mass%) on bovine serum albumin denatured aggregation kinetics at high concentration was studied by the iso-conversional method and the master plots method using differential scanning calorimetry. The observed aggregation was irreversible and conformed to the simple order reaction. The denaturation temperature (Tm), the kinetic triplets all increased as the sucrose concentration increased, which indicated the remarkable stabilization effect of sucrose. The study purpose is to provide new opportunities in exploring aggregation kinetics mechanisms in the presence of additive.