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The Myceliophthora thermophila laccase was covalently immobilized on polymethacrylate-based polymers (Sepabeads EC-EP3 and Dilbeads NK) activated with epoxy groups. The enzyme immobilized on Sepabeads EC-EP3 exhibited notable activity (203 U/g) along with remarkably improved stability towards pH, temperature and storage time, but no increased resistance to organic solvents. In addition, the immobilized laccase also showed good operational stability, maintaining 84% of its initial activity after 17 cycles of oxidation of ABTS. The immobilized biocatalyst was applied to the decolorization of six synthetic dyes. Immobilized laccase retained 41% activity in the decolorization of Methyl Green in a fixed-bed reactor after five cycles. The features of these biocatalysts are very attractive for their application on the decolorization of dyes in the textile industry in batch and continuous fixed-bed bioreactors. To our knowledge, this is the first report on immobilization of laccase on Sepabeads carriers and its efficient dyes decolorization. ; We thank Drs. Moreno Daminati and Paolo Caimi (Resindion) and Vyasa Rajasekar (DilComplex) for providing us Sepabeads EC-EP3 and Dilbeads NK polymers, respectively. We are grateful to Ramiro Martínez (Novozymes A/S, Spain) for DeniLite II S samples. This material is based upon work founded by Spanish MEC (Projects VEM2004-08559 and CTQ2005-08925-C02-02/PPQ); European Union (Project NMP2-CT-2006-026456) and CSIC (Project 200580M121). Spanish MEC is also thanked for the post-doctoral fellowship (SB2004-0011) of Dr. A. Kunamneni and for the Ramon y Cajal contracts of Drs. S. Camarero and M. Alcalde. ; This material is based upon work financed by Spanish MEC (Projects VEM2004-08559 and CTQ2005-08925-C02-02/PPQ); European Union (Project NMP2-CT-2006-026456) and CSIC (Project 200580M121). Spanish MEC is also thanked for the post-doctoral fellowship (SB2004-0011) of Dr. A. Kunamneni and for the Ramon y Cajal contracts of Drs. S. Camarero and M. Alcalde. ; Peer reviewed

Unnatural selection: A fungal laccase was tailored by directed evolution to be active at neutral/alkaline pH. After five generations, the final mutant showed a broader pH profile while retaining 50 to 80 % of its activity at neutral pH. ; This study was based upon work funded by the EU Projects [NMP4‐SL‐2009–229255–3D‐Nanobiodevice, FP7‐KBBE‐2010–4–26537‐Peroxicats and COST Action CM0701] and a project of the Spanish Government [BIO2010–19697]. P.T.S. was supported by a grant from the "Comunidad de Madrid" and D.M.M. was supported by a JAE‐CSIC grant. ; Peer Reviewed