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A simple method for biocatalyst immobilization using PVA-based hydrogel particles

Fernandes, Pedro, Marques, Marco P.C., Carvalho, Filipe, Cabral, Joaquim M.S.
Journal of chemical technology and biotechnology 2009 v.84 no.4 pp. 561-564
beta-fructofuranosidase, biocatalysts, biotransformation, enzyme activity, extrusion, hydrocolloids, hydrolysis, immobilized enzymes, inulinase, pH, polyethylene glycol, sucrose
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.