caa a22 4500 605503664 CHVBK 20210128100612.0 cr unu---uuuuu 210128e20150201xx s 000 0 eng 10.1007/s00253-014-6346-7 doi (NATIONALLICENCE)springer-10.1007/s00253-014-6346-7 An updated view on horseradish peroxidases: recombinant production and biotechnological applications [Elektronische Daten] [Florian Krainer, Anton Glieder] 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. The Author(s), 2015 Horseradish peroxidase nationallicence Plant peroxidase nationallicence Recombinant protein production nationallicence Diagnostics nationallicence Biosensor nationallicence Indole-3-acetic acid nationallicence Cancer treatment nationallicence Krainer Florian Institute of Molecular Biotechnology, NAWI Graz, Graz University of Technology, Petersgasse 14, 8010, Graz, Austria aut Glieder Anton Institute of Molecular Biotechnology, NAWI Graz, Graz University of Technology, Petersgasse 14, 8010, Graz, Austria aut Applied Microbiology and Biotechnology Springer Berlin Heidelberg 99/4(2015-02-01), 1611-1625 0175-7598 99:4<1611 2015 99 253 https://doi.org/10.1007/s00253-014-6346-7 text/html Onlinezugriff via DOI BK010053 XK010053 XK010000 Metadata rights reserved Springer special CC-BY-NC licence nationallicence 1 review-article jats NATIONALLICENCE NATIONALLICENCE NL-springer NATIONALLICENCE 856 40 https://doi.org/10.1007/s00253-014-6346-7 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Krainer Florian Institute of Molecular Biotechnology, NAWI Graz, Graz University of Technology, Petersgasse 14, 8010, Graz, Austria aut NATIONALLICENCE 700 1- Glieder Anton Institute of Molecular Biotechnology, NAWI Graz, Graz University of Technology, Petersgasse 14, 8010, Graz, Austria aut NATIONALLICENCE 773 0- Applied Microbiology and Biotechnology Springer Berlin Heidelberg 99/4(2015-02-01), 1611-1625 0175-7598 99:4<1611 2015 99 253