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Applications and immobilization strategies of the copper-centred laccase enzyme; a review

Laccase is a multi-copper enzyme widely expressed in fungi, higher plants, and bacteria which facilitates the direct reduction of molecular oxygen to water (without hydrogen peroxide production) accompanied by the oxidation of an electron donor. Laccase has attracted attention in biotechnological ap...

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Detalles Bibliográficos
Autores principales: Kyomuhimbo, Hilda Dinah, Brink, Hendrik G.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9898315/
https://www.ncbi.nlm.nih.gov/pubmed/36747551
http://dx.doi.org/10.1016/j.heliyon.2023.e13156
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author Kyomuhimbo, Hilda Dinah
Brink, Hendrik G.
author_facet Kyomuhimbo, Hilda Dinah
Brink, Hendrik G.
author_sort Kyomuhimbo, Hilda Dinah
collection PubMed
description Laccase is a multi-copper enzyme widely expressed in fungi, higher plants, and bacteria which facilitates the direct reduction of molecular oxygen to water (without hydrogen peroxide production) accompanied by the oxidation of an electron donor. Laccase has attracted attention in biotechnological applications due to its non-specificity and use of molecular oxygen as secondary substrate. This review discusses different applications of laccase in various sectors of food, paper and pulp, waste water treatment, pharmaceuticals, sensors, and fuel cells. Despite the many advantages of laccase, challenges such as high cost due to its non-reusability, instability in harsh environmental conditions, and proteolysis are often encountered in its application. One of the approaches used to minimize these challenges is immobilization. The various methods used to immobilize laccase and the different supports used are further extensively discussed in this review.
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spelling pubmed-98983152023-02-05 Applications and immobilization strategies of the copper-centred laccase enzyme; a review Kyomuhimbo, Hilda Dinah Brink, Hendrik G. Heliyon Review Article Laccase is a multi-copper enzyme widely expressed in fungi, higher plants, and bacteria which facilitates the direct reduction of molecular oxygen to water (without hydrogen peroxide production) accompanied by the oxidation of an electron donor. Laccase has attracted attention in biotechnological applications due to its non-specificity and use of molecular oxygen as secondary substrate. This review discusses different applications of laccase in various sectors of food, paper and pulp, waste water treatment, pharmaceuticals, sensors, and fuel cells. Despite the many advantages of laccase, challenges such as high cost due to its non-reusability, instability in harsh environmental conditions, and proteolysis are often encountered in its application. One of the approaches used to minimize these challenges is immobilization. The various methods used to immobilize laccase and the different supports used are further extensively discussed in this review. Elsevier 2023-01-25 /pmc/articles/PMC9898315/ /pubmed/36747551 http://dx.doi.org/10.1016/j.heliyon.2023.e13156 Text en © 2023 The Authors https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
spellingShingle Review Article
Kyomuhimbo, Hilda Dinah
Brink, Hendrik G.
Applications and immobilization strategies of the copper-centred laccase enzyme; a review
title Applications and immobilization strategies of the copper-centred laccase enzyme; a review
title_full Applications and immobilization strategies of the copper-centred laccase enzyme; a review
title_fullStr Applications and immobilization strategies of the copper-centred laccase enzyme; a review
title_full_unstemmed Applications and immobilization strategies of the copper-centred laccase enzyme; a review
title_short Applications and immobilization strategies of the copper-centred laccase enzyme; a review
title_sort applications and immobilization strategies of the copper-centred laccase enzyme; a review
topic Review Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9898315/
https://www.ncbi.nlm.nih.gov/pubmed/36747551
http://dx.doi.org/10.1016/j.heliyon.2023.e13156
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