Chemical and thermal stability of ferulic acid esterase-III from Aspergillus niger

Abstract

The stability of ferulic acid esterase III (FAE-III) from Aspergillus niger was examined using chemical and thermal denaturation. Thermal denaturation was irreversible and the loss of activity was dependent on pH. At 60°C and pH 6.0, the rate constant of unfolding was 0.76 10 −3/s, and the change in free energy of irreversible inactivation, ΔG*, was 101.9 kJ/mol. Sinapic acid, a product of the reaction of methyl sinapate with FAE-III, reduced the rate of unfolding (0.66 10 −3/s at 0.1 mM sinapic acid). Chemical denaturation was performed using guanidine hydrochloride. FAE-III was very sensitive to this denaturant, and the midpoint of unfolding was 1.38 M guanidine hydrochloride at 30°C, pH 6.0. The stability of FAE-III is compared to other enzymes.