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      Laccase: a multi‐purpose biocatalyst at the forefront of biotechnology

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      1 , 1 ,
      Microbial Biotechnology
      John Wiley and Sons Inc.

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          Summary

          Laccases are multicopper containing enzymes capable of performing one electron oxidation of a broad range of substrates. Using molecular oxygen as the final electron acceptor, they release only water as a by‐product, and as such, laccases are eco‐friendly, versatile biocatalysts that have generated an enormous biotechnological interest. Indeed, this group of enzymes has been used in different industrial fields for very diverse purposes, from food additive and beverage processing to biomedical diagnosis, and as cross‐linking agents for furniture construction or in the production of biofuels. Laccases have also been studied intensely in nanobiotechnology for the development of implantable biosensors and biofuel cells. Moreover, their capacity to transform complex xenobiotics makes them useful biocatalysts in enzymatic bioremediation. This review summarizes the most significant recent advances in the use of laccases and their future perspectives in biotechnology.

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          Most cited references102

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          Multicopper Oxidases and Oxygenases.

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            Laccases: blue enzymes for green chemistry.

            Laccases are oxidoreductases belonging to the multinuclear copper-containing oxidases; they catalyse the monoelectronic oxidation of substrates at the expense of molecular oxygen. Interest in these essentially "eco-friendly" enzymes--they work with air and produce water as the only by-product--has grown significantly in recent years: their uses span from the textile to the pulp and paper industries, and from food applications to bioremediation processes. Laccases also have uses in organic synthesis, where their typical substrates are phenols and amines, and the reaction products are dimers and oligomers derived from the coupling of reactive radical intermediates. Here, we provide a brief discussion of this interesting group of enzymes, increased knowledge of which will promote laccase-based industrial processes in the future.
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              Laccase: new functions for an old enzyme

              A. Mayer (2002)
              Laccases occur widely in fungi; they have been characterized less frequently in higher plants. Here we have focused on more recent reports on the occurrence of laccase and its functions in physiological development and industrial utility. The reports of molecular weights, pH optima, and substrate specificity are extremely diverse. Conclusive proof of the occurrence of laccase in a tissue must demonstrate that the enzyme be able to oxidize quinol with concomitant uptake of oxygen. Laccase is involved in the pigmentation process of fungal spores, the regeneration of tobacco protoplasts, as fungal virulence factors, and in lignification of cell walls and delignification during white rot of wood. Commercially, laccases have been used to delignify woody tissues, produce ethanol, and to distinguish between morphine and codeine. A very wide variety of bioremediation processes employ laccase in order to protect the environment from damage caused by industrial effluents. Research in recent years has been intense, much of it elicited by the wide diversity of laccases, their utility and their very interesting enzymology.
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                Author and article information

                Contributors
                malcalde@icp.csic.es
                Journal
                Microb Biotechnol
                Microb Biotechnol
                10.1111/(ISSN)1751-7915
                MBT2
                Microbial Biotechnology
                John Wiley and Sons Inc. (Hoboken )
                1751-7915
                03 October 2016
                November 2017
                : 10
                : 6 , Thematic Issue: From complex waste to plastic value ( doiID: 10.1111/mbt2.2017.10.issue-6 )
                : 1457-1467
                Affiliations
                [ 1 ] Department of Biocatalysis Institute of Catalysis CSIC Cantoblanco 28049 Madrid Spain
                Author notes
                [*] [* ]For correspondence. E‐mail malcalde@ 123456icp.csic.es ; Tel. +34 91 585 4806; Fax +34 91 585 4760.
                Article
                MBT212422
                10.1111/1751-7915.12422
                5658592
                27696775
                fff66b0f-1936-4305-a2eb-4762aa0c8487
                © 2016 The Authors. Microbial Biotechnology published by John Wiley & Sons Ltd and Society for Applied Microbiology.

                This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.

                History
                : 28 June 2016
                : 12 September 2016
                : 15 September 2016
                Page count
                Figures: 2, Tables: 1, Pages: 11, Words: 8110
                Funding
                Funded by: EU
                Award ID: FP7‐KBBE‐2013‐7‐613549‐INDOX
                Award ID: FP7‐People‐2013‐ITN‐607793
                Funded by: COST Action CM1303 Systems Biocatalysis
                Funded by: Spanish Government
                Award ID: BIO2013‐43407‐R‐DEWRY
                Categories
                Minireview
                Minireviews
                Custom metadata
                2.0
                mbt212422
                November 2017
                Converter:WILEY_ML3GV2_TO_NLMPMC version:5.2.1 mode:remove_FC converted:27.10.2017

                Biotechnology
                Biotechnology

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