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

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...

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Detalles Bibliográficos
Autores principales: Mate, Diana M., Alcalde, Miguel
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5658592/
https://www.ncbi.nlm.nih.gov/pubmed/27696775
http://dx.doi.org/10.1111/1751-7915.12422
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author Mate, Diana M.
Alcalde, Miguel
author_facet Mate, Diana M.
Alcalde, Miguel
author_sort Mate, Diana M.
collection PubMed
description 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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spelling pubmed-56585922017-11-01 Laccase: a multi‐purpose biocatalyst at the forefront of biotechnology Mate, Diana M. Alcalde, Miguel Microb Biotechnol Minireviews 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. John Wiley and Sons Inc. 2016-10-03 /pmc/articles/PMC5658592/ /pubmed/27696775 http://dx.doi.org/10.1111/1751-7915.12422 Text en © 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 (http://creativecommons.org/licenses/by/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
spellingShingle Minireviews
Mate, Diana M.
Alcalde, Miguel
Laccase: a multi‐purpose biocatalyst at the forefront of biotechnology
title Laccase: a multi‐purpose biocatalyst at the forefront of biotechnology
title_full Laccase: a multi‐purpose biocatalyst at the forefront of biotechnology
title_fullStr Laccase: a multi‐purpose biocatalyst at the forefront of biotechnology
title_full_unstemmed Laccase: a multi‐purpose biocatalyst at the forefront of biotechnology
title_short Laccase: a multi‐purpose biocatalyst at the forefront of biotechnology
title_sort laccase: a multi‐purpose biocatalyst at the forefront of biotechnology
topic Minireviews
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5658592/
https://www.ncbi.nlm.nih.gov/pubmed/27696775
http://dx.doi.org/10.1111/1751-7915.12422
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