Immobilization of laccase on modified silica: Stabilization, thermal inactivation and kinetic behaviour in 1-ethyl-3-methylimidazolium ethylsulfate ionic liquid
authors Tavares, APM; Rodriguez, O; Fernandez-Fernandez, M; Dominguez, A; Moldes, D; Sanroman, MA; Macedo, EA
nationality International
journal BIORESOURCE TECHNOLOGY
author keywords Laccase; Ionic liquid; Stability; Thermal inactivation; Kinetic behaviour
keywords AQUEOUS-SOLUTIONS; BETA-GALACTOSIDASE; CATALYTIC-ACTIVITY; ENZYME-ACTIVITY; SUPPORTS; BIOCATALYSIS; PEROXIDASE; STABILITY; REMOVAL
abstract Laccase was immobilized on modified silica carrier. The immobilization conditions, pH and enzyme concentration were optimized. Operational stability of 10 reaction cycles showed that immobilized laccase in buffer was stable, presenting an activity loss <30%. Nevertheless, a high decrease >80% was obtained in ionic liquid (IL) solution. Activity of immobilized laccase was maintained when incubated in IL After 7 days of incubation, immobilized laccase lost 30-50% of its initial activity. Immobilization also improved thermal stability of laccase in the presence of IL. Enzyme kinetics was modelled with Michaelis-Menten model. The K-m value for free laccase increases significantly with the IL concentration. Slight differences were found in V-m, for free enzyme. Unusual kinetic behaviour was obtained for immobilized laccase in IL: Both V-m and K-m increased with IL concentration, resulting in increased catalytic efficiency of the immobilized enzyme in presence of IL. (C) 2013 Published by Elsevier Ltd.
publisher ELSEVIER SCI LTD
issn 0960-8524
year published 2013
volume 131
beginning page 405
ending page 412
digital object identifier (doi) 10.1016/j.biortech.2012.12.139
web of science category Agricultural Engineering; Biotechnology & Applied Microbiology; Energy & Fuels
subject category Agriculture; Biotechnology & Applied Microbiology; Energy & Fuels
unique article identifier WOS:000317024200053
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