โ Scribed by Pedro Fernandes; Marco P.C. Marques; Filipe Carvalho; Joaquim M.S. Cabral
No coin nor oath required. For personal study only.
BACKGROUND: The aim of this study was to evaluate the feasibility of enzyme immobilization in PVA particles through extrusion of LentiKat^ยฎ^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 ยฐC was observed. A 1.8โfold increase in the apparent K~M~ (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 ยฐC, following 20 repeated, consecutive batches.
CONCLUSION: The results obtained highlight the potential of PVAโbased particles obtained through extrusion into PEG for the production of suitable biocatalysts for application in largeโscale processes. Copyright ยฉ 2008 Society of Chemical Industry
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