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A simple method for biocatalyst immobilization using PVA‐based hydrogel particles
Author(s) -
Fernandes Pedro,
Marques Marco P.C.,
Carvalho Filipe,
Cabral Joaquim M.S.
Publication year - 2009
Publication title -
journal of chemical technology and biotechnology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.64
H-Index - 117
eISSN - 1097-4660
pISSN - 0268-2575
DOI - 10.1002/jctb.2080
Subject(s) - inulinase , biocatalysis , chemistry , polyethylene glycol , yield (engineering) , extrusion , hydrolysis , peg ratio , michaelis–menten kinetics , immobilized enzyme , chromatography , invertase , biotransformation , chemical engineering , sucrose , materials science , enzyme assay , organic chemistry , enzyme , catalysis , composite material , ionic liquid , finance , economics , engineering
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 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 °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