Controlling the Surface Chemistry of Multiwalled Carbon Nanotubes for the Production of Highly Efficient and Stable Laccase-Based Biocatalysts
authors Silva, CG; Tavares, APM; Drazic, G; Silva, AMT; Loureiro, JM; Faria, JL
nationality International
journal CHEMPLUSCHEM
author keywords biocatalysis; enzymes; immobilization; nanotubes; surface chemistry
keywords COMMERCIAL LACCASE; IMMOBILIZATION; OXIDATION; FUNCTIONALIZATION; SELECTIVITY; PEROXIDASE; STABILITY; CATALYSIS; PROTEINS
abstract Laccase was immobilized over multiwalled carbon nanotubes (MWCNTs) with diameters ranging from 10 to 100 nm and different surface chemical groups. Oxygen-containing groups were introduced selectively or removed by liquid-phase oxidation and thermal treatments. The effect of pH on the immobilization efficiency and catalytic activity of laccase has been evaluated. Pristine MWCNTs show excellent immobilization capacity (100%) and high enzyme activity, but low thermal stability (at 50 degrees C) owing to weak interaction (mostly hydrophobic) be-tween laccase and the support. Immobilization capacity and catalytic activity of laccase on the modified MWCNTs were related to the surface electric charge of both the support and the enzyme. MWCNTs oxidized with HNO3 and posteriorly heated at 400 degrees C, mostly presenting hydroxyl surface groups, provided the best compromise between laccase activity and thermal stability, which has been attributed to the formation of hydrogen bonds between the support and the enzyme.
publisher WILEY-V C H VERLAG GMBH
issn 2192-6506
year published 2014
volume 79
issue 8
beginning page 1116
ending page 1122
digital object identifier (doi) 10.1002/cplu.201402054
web of science category Chemistry, Multidisciplinary
subject category Chemistry
unique article identifier WOS:000340508000007
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journal analysis (jcr 2017):
journal impact factor 3.205
5 year journal impact factor 2.867
category normalized journal impact factor percentile 62.865
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