Immobilization of commercial laccase onto green coconut fiber by adsorption and its application for reactive textile dyes degradation
authors Cristovao, RO; Tavares, APM; Brigida, AI; Loureiro, JM; Boaventura, RAR; Macedo, EA; Coelho, MAZ
nationality International
journal JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC
author keywords Commercial laccase; Dyes decolourization; Enzyme immobilization; Coconut fiber; Physical adsorption
keywords CANDIDA-ANTARCTICA; DIFFERENT SUPPORTS; MEDIATOR SYSTEM; LIPASE-B; ENZYMES; DECOLORIZATION; DECOLORATION; BEADS; DECOLOURIZATION; STABILIZATION
abstract An effort has been made to find a cheaper, easily available and simple alternative for the immobilization of enzymes and subsequent utilization at large scale in textile wastewater treatment. Commercial laccase was immobilized for the first time on an agroindustrial residue, green coconut fiber, by physical adsorption. The effect of the immobilization conditions (enzyme concentration, contact time and pH value) on the properties of the biocatalyst was determined. Then, the immobilized enzyme characterization was performed and kinetic parameters were obtained. Thermal and operational stabilities were improved compared with free commercial laccase showing its potential for continuous applications. Finally, the performance of immobilized laccase for the continuous degradation of various reactive textile dyes and of a mixture of them in batch reactors was evaluated. Two phenomena were observed: decolourization of the solutions due to dyes adsorption on the support and due to the enzyme action. A high decolourization percentage of practically all dyes in the first two cycles and an effective decolourization of the dye mixture were obtained, showing the suitability of the immobilized commercial laccase for continuous colour removal from textile industrial effluents. (C) 2011 Elsevier B.V. All rights reserved.
publisher ELSEVIER SCIENCE BV
issn 1381-1177
year published 2011
volume 72
issue 1-2
beginning page 6
ending page 12
digital object identifier (doi) 10.1016/j.molcatb.2011.04.014
web of science category Biochemistry & Molecular Biology; Chemistry, Physical
subject category Biochemistry & Molecular Biology; Chemistry
unique article identifier WOS:000293995300002
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