Journal
BIORESOURCE TECHNOLOGY
Volume 101, Issue 22, Pages 8541-8548Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.biortech.2010.06.042
Keywords
Laccase; Enzyme immobilization; Degradation of aromatic compounds; Mesostructured silica; Naphthalene
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The oxidation of naphthalene by immobilized laccase from Trametes versicolor has been performed using diverse immobilization strategies on mesostructured silica materials. Laccase was immobilized by physical adsorption on several SBA-15 with different textural properties and by covalent attachment on functionalized SBA-15 prepared by co-condensation method (direct synthesis). The adsorption of laccase was partially reversible and showed some degree of lixiviation. However, covalently attached laccase to aminopropyl and aminobutyl functionalized SBA-15 exhibited important activity for the degradation of naphthalene with, respectively, 35% and 39%wt of removal in 5 h. The aminopropyl biocatalyst retained higher activity after repeated uses than the corresponding aminobutyl. (C) 2010 Elsevier Ltd. All rights reserved.
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