caa a22 4500 605504571 CHVBK 20210128100617.0 cr unu---uuuuu 210128e20150301xx s 000 0 eng 10.1007/s00253-014-6060-5 doi (NATIONALLICENCE)springer-10.1007/s00253-014-6060-5 Not so monofunctional—a case of thermostable Thermobifida fusca catalase with peroxidase activity [Elektronische Daten] [Nikola Lončar, Marco Fraaije] Thermobifida fusca is a mesothermophilic organism known for its ability to degrade plant biomass and other organics, and it was demonstrated that it represents a rich resource of genes encoding for potent enzymes for biocatalysis. The thermostable catalase from T. fusca has been cloned and overexpressed in Escherichia coli with a yield of 400mg/L. Heat treatment of disrupted cells at 60°C for 1h resulted in enzyme preparation of high purity; hence, no chromatography steps are needed for large-scale production. Except for catalyzing the dismutation of hydrogen peroxide, TfuCat was also found to catalyze oxidations of phenolic compounds. The catalase activity was comparable to other described catalases while peroxidase activity was quite remarkable with a k obs of nearly 1000s−1 for catechol. Site directed mutagenesis was used to alter the ratio of peroxidase/catalase activity. Resistance to inhibition by classic catalase inhibitors and an apparent melting temperature of 74°C classifies this enzyme as a robust biocatalyst. As such, it could compete with other commercially available catalases while the relatively high peroxidase activity also offers new biocatalytic possibilities. Springer-Verlag Berlin Heidelberg, 2014 Thermobifida fusca nationallicence Catalase nationallicence Thermostable enzyme nationallicence Peroxidase nationallicence Oxidation nationallicence Lončar Nikola Molecular Enzymology Group, University of Groningen, Nijenborgh 4, 9747 AG, Groningen, The Netherlands aut Fraaije Marco Molecular Enzymology Group, University of Groningen, Nijenborgh 4, 9747 AG, Groningen, The Netherlands aut Applied Microbiology and Biotechnology Springer Berlin Heidelberg 99/5(2015-03-01), 2225-2232 0175-7598 99:5<2225 2015 99 253 https://doi.org/10.1007/s00253-014-6060-5 text/html Onlinezugriff via DOI BK010053 XK010053 XK010000 Metadata rights reserved Springer special CC-BY-NC licence nationallicence 1 research-article jats NATIONALLICENCE NATIONALLICENCE NL-springer NATIONALLICENCE 856 40 https://doi.org/10.1007/s00253-014-6060-5 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Lončar Nikola Molecular Enzymology Group, University of Groningen, Nijenborgh 4, 9747 AG, Groningen, The Netherlands aut NATIONALLICENCE 700 1- Fraaije Marco Molecular Enzymology Group, University of Groningen, Nijenborgh 4, 9747 AG, Groningen, The Netherlands aut NATIONALLICENCE 773 0- Applied Microbiology and Biotechnology Springer Berlin Heidelberg 99/5(2015-03-01), 2225-2232 0175-7598 99:5<2225 2015 99 253