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An updated view on horseradish peroxidases: recombinant production and biotechnological applications

Horseradish peroxidase has been the subject of scientific research for centuries. It has been used exhaustively as reporter enzyme in diagnostics and histochemistry and still plays a major role in these applications. Numerous studies have been conducted on the role of horseradish peroxidase in the p...

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Detalles Bibliográficos
Autores principales: Krainer, Florian W., Glieder, Anton
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Berlin Heidelberg 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4322221/
https://www.ncbi.nlm.nih.gov/pubmed/25575885
http://dx.doi.org/10.1007/s00253-014-6346-7
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author Krainer, Florian W.
Glieder, Anton
author_facet Krainer, Florian W.
Glieder, Anton
author_sort Krainer, Florian W.
collection PubMed
description Horseradish peroxidase has been the subject of scientific research for centuries. It has been used exhaustively as reporter enzyme in diagnostics and histochemistry and still plays a major role in these applications. Numerous studies have been conducted on the role of horseradish peroxidase in the plant and its catalytic mechanism. However, little progress has been made in its recombinant production. Until now, commercial preparations of horseradish peroxidase are still isolated from plant roots. These preparations are commonly mixtures of various isoenzymes of which only a small fraction has been described so far. The composition of isoenzymes in these mixed isolates is subjected to uncontrollable environmental conditions. Nowadays, horseradish peroxidase regains interest due to its broad applicability in the fields of medicine, life sciences, and biotechnology in cancer therapy, biosensor systems, bioremediation, and biocatalysis. These medically and commercially relevant applications, the recent discovery of new natural isoenzymes with different biochemical properties, as well as the challenges in recombinant production render this enzyme particularly interesting for future biotechnological solutions. Therefore, we reviewed previous studies as well as current developments with biotechnological emphasis on new applications and the major remaining biotechnological challenge—the efficient recombinant production of horseradish peroxidase enzymes.
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spelling pubmed-43222212015-02-13 An updated view on horseradish peroxidases: recombinant production and biotechnological applications Krainer, Florian W. Glieder, Anton Appl Microbiol Biotechnol Mini-Review Horseradish peroxidase has been the subject of scientific research for centuries. It has been used exhaustively as reporter enzyme in diagnostics and histochemistry and still plays a major role in these applications. Numerous studies have been conducted on the role of horseradish peroxidase in the plant and its catalytic mechanism. However, little progress has been made in its recombinant production. Until now, commercial preparations of horseradish peroxidase are still isolated from plant roots. These preparations are commonly mixtures of various isoenzymes of which only a small fraction has been described so far. The composition of isoenzymes in these mixed isolates is subjected to uncontrollable environmental conditions. Nowadays, horseradish peroxidase regains interest due to its broad applicability in the fields of medicine, life sciences, and biotechnology in cancer therapy, biosensor systems, bioremediation, and biocatalysis. These medically and commercially relevant applications, the recent discovery of new natural isoenzymes with different biochemical properties, as well as the challenges in recombinant production render this enzyme particularly interesting for future biotechnological solutions. Therefore, we reviewed previous studies as well as current developments with biotechnological emphasis on new applications and the major remaining biotechnological challenge—the efficient recombinant production of horseradish peroxidase enzymes. Springer Berlin Heidelberg 2015-01-11 2015 /pmc/articles/PMC4322221/ /pubmed/25575885 http://dx.doi.org/10.1007/s00253-014-6346-7 Text en © The Author(s) 2015 https://creativecommons.org/licenses/by/4.0/ Open Access This article is distributed under the terms of the Creative Commons Attribution License which permits any use, distribution, and reproduction in any medium, provided the original author(s) and the source are credited.
spellingShingle Mini-Review
Krainer, Florian W.
Glieder, Anton
An updated view on horseradish peroxidases: recombinant production and biotechnological applications
title An updated view on horseradish peroxidases: recombinant production and biotechnological applications
title_full An updated view on horseradish peroxidases: recombinant production and biotechnological applications
title_fullStr An updated view on horseradish peroxidases: recombinant production and biotechnological applications
title_full_unstemmed An updated view on horseradish peroxidases: recombinant production and biotechnological applications
title_short An updated view on horseradish peroxidases: recombinant production and biotechnological applications
title_sort updated view on horseradish peroxidases: recombinant production and biotechnological applications
topic Mini-Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4322221/
https://www.ncbi.nlm.nih.gov/pubmed/25575885
http://dx.doi.org/10.1007/s00253-014-6346-7
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