Stability evaluation of an immobilized enzyme system for inulin hydrolysis

Abstract

The stability of free and Amberlite-immobilized inulinase, aiming at inulin hydrolysis was evaluated. The apparent activation energy of the biotransformation decreased when the immobilized biocatalyst was used, suggesting diffusional limitations, despite a decrease in the optimal temperature for catalytic activity for the immobilized biocatalyst. Thermal deactivation, of both forms of the biocatalyst, was evaluated by the linear inverted model. Inulinase immobilization consistently enhanced half-life of the enzyme, which increased up to 6-fold, as compared to the free form. Mean enzymatic activity was computed for both forms of the biocatalyst, and evidenced a decrease of optimal temperature with increased incubation periods. The deactivation energies estimated by an Arrhenius plot, evidenced a decrease of roughly 20% when free inulinase was used. The immobilized biocatalyst was effectively reused in successive batch runs for the hydrolysis of a 5% inulin solution.