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Breakthroughs in the discovery and use of different peroxidase isoforms of microbial origin

Peroxidases are classified as oxidoreductases and are the second largest class of enzymes applied in biotechnological processes. These enzymes are used to catalyze various oxidative reactions using hydrogen peroxide and other substrates as electron donors. They are isolated from various sources such...

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Autores principales: Twala, Pontsho Patricia, Mitema, Alfred, Baburam, Cindy, Feto, Naser Aliye
Formato: Online Artículo Texto
Lenguaje:English
Publicado: AIMS Press 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7595840/
https://www.ncbi.nlm.nih.gov/pubmed/33134747
http://dx.doi.org/10.3934/microbiol.2020020
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author Twala, Pontsho Patricia
Mitema, Alfred
Baburam, Cindy
Feto, Naser Aliye
author_facet Twala, Pontsho Patricia
Mitema, Alfred
Baburam, Cindy
Feto, Naser Aliye
author_sort Twala, Pontsho Patricia
collection PubMed
description Peroxidases are classified as oxidoreductases and are the second largest class of enzymes applied in biotechnological processes. These enzymes are used to catalyze various oxidative reactions using hydrogen peroxide and other substrates as electron donors. They are isolated from various sources such as plants, animals and microbes. Peroxidase enzymes have versatile applications in bioenergy, bioremediation, dye decolorization, humic acid degradation, paper and pulp, and textile industries. Besides, peroxidases from different sources have unique abilities to degrade a broad range of environmental pollutants such as petroleum hydrocarbons, dioxins, industrial dye effluents, herbicides and pesticides. Ironically, unlike most biological catalysts, the function of peroxidases varies according to their source. For instance, manganese peroxidase (MnP) of fungal origin is widely used for depolymerization and demethylation of lignin and bleaching of pulp. While, horseradish peroxidase of plant origin is used for removal of phenols and aromatic amines from waste waters. Microbial enzymes are believed to be more stable than enzymes of plant or animal origin. Thus, making microbially-derived peroxidases a well-sought-after biocatalysts for versatile industrial and environmental applications. Therefore, the current review article highlights on the recent breakthroughs in the discovery and use of peroxidase isoforms of microbial origin at a possible depth.
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spelling pubmed-75958402020-10-30 Breakthroughs in the discovery and use of different peroxidase isoforms of microbial origin Twala, Pontsho Patricia Mitema, Alfred Baburam, Cindy Feto, Naser Aliye AIMS Microbiol Review Peroxidases are classified as oxidoreductases and are the second largest class of enzymes applied in biotechnological processes. These enzymes are used to catalyze various oxidative reactions using hydrogen peroxide and other substrates as electron donors. They are isolated from various sources such as plants, animals and microbes. Peroxidase enzymes have versatile applications in bioenergy, bioremediation, dye decolorization, humic acid degradation, paper and pulp, and textile industries. Besides, peroxidases from different sources have unique abilities to degrade a broad range of environmental pollutants such as petroleum hydrocarbons, dioxins, industrial dye effluents, herbicides and pesticides. Ironically, unlike most biological catalysts, the function of peroxidases varies according to their source. For instance, manganese peroxidase (MnP) of fungal origin is widely used for depolymerization and demethylation of lignin and bleaching of pulp. While, horseradish peroxidase of plant origin is used for removal of phenols and aromatic amines from waste waters. Microbial enzymes are believed to be more stable than enzymes of plant or animal origin. Thus, making microbially-derived peroxidases a well-sought-after biocatalysts for versatile industrial and environmental applications. Therefore, the current review article highlights on the recent breakthroughs in the discovery and use of peroxidase isoforms of microbial origin at a possible depth. AIMS Press 2020-09-22 /pmc/articles/PMC7595840/ /pubmed/33134747 http://dx.doi.org/10.3934/microbiol.2020020 Text en © 2020 the Author(s), licensee AIMS Press This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0)
spellingShingle Review
Twala, Pontsho Patricia
Mitema, Alfred
Baburam, Cindy
Feto, Naser Aliye
Breakthroughs in the discovery and use of different peroxidase isoforms of microbial origin
title Breakthroughs in the discovery and use of different peroxidase isoforms of microbial origin
title_full Breakthroughs in the discovery and use of different peroxidase isoforms of microbial origin
title_fullStr Breakthroughs in the discovery and use of different peroxidase isoforms of microbial origin
title_full_unstemmed Breakthroughs in the discovery and use of different peroxidase isoforms of microbial origin
title_short Breakthroughs in the discovery and use of different peroxidase isoforms of microbial origin
title_sort breakthroughs in the discovery and use of different peroxidase isoforms of microbial origin
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7595840/
https://www.ncbi.nlm.nih.gov/pubmed/33134747
http://dx.doi.org/10.3934/microbiol.2020020
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