• inulinase;
  • sucrose hydrolysis;
  • polyvinyl alcohol;
  • LentiKat®Liquid;
  • PEG 600


BACKGROUND: The aim of this study was to evaluate the feasibility of enzyme immobilization in PVA particles through extrusion of LentiKat®Liquid in polyethylene glycol. Inulinase, with invertase activity for sucrose hydrolysis, was used as model system.

RESULTS: Inulinase was effectively immobilized in PVA particles. The pH optimum of the enzyme activity was broadened for lower pH values. Mechanical instability of the PVA under prolonged incubation above 55 °C was observed. A 1.8-fold increase in the apparent KM (Michaelis constant) suggests diffusion limitations as a result of immobilization. The immobilized biocatalyst exhibited considerable operational stability, since a decrease of roughly 10% in the product yield after 24 h biotransformation runs was observed in trials performed at 50 °C, following 20 repeated, consecutive batches.

CONCLUSION: The results obtained highlight the potential of PVA-based particles obtained through extrusion into PEG for the production of suitable biocatalysts for application in large-scale processes. Copyright © 2008 Society of Chemical Industry