TY  - JOUR
AU  - Lončar, Nikola L.
AU  - Fraaije, Marco W.
PY  - 2015
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1664
AB  - 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 400 mg/L. Heat treatment of disrupted cells at 60 A degrees C for 1 h 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 1000 s(-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 A degrees 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.
PB  - Springer, New York
T2  - Applied Microbiology and Biotechnology
T1  - Not so monofunctional-a case of thermostable Thermobifida fusca catalase with peroxidase activity
VL  - 99
IS  - 5
SP  - 2225
EP  - 2232
DO  - 10.1007/s00253-014-6060-5
ER  - 

@article{
author = "Lončar, Nikola L. and Fraaije, Marco W.",
year = "2015",
abstract = "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 400 mg/L. Heat treatment of disrupted cells at 60 A degrees C for 1 h 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 1000 s(-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 A degrees 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.",
publisher = "Springer, New York",
journal = "Applied Microbiology and Biotechnology",
title = "Not so monofunctional-a case of thermostable Thermobifida fusca catalase with peroxidase activity",
volume = "99",
number = "5",
pages = "2225-2232",
doi = "10.1007/s00253-014-6060-5"
}

Lončar, N. L.,& Fraaije, M. W.. (2015). Not so monofunctional-a case of thermostable Thermobifida fusca catalase with peroxidase activity. in Applied Microbiology and Biotechnology
Springer, New York., 99(5), 2225-2232.
https://doi.org/10.1007/s00253-014-6060-5

Lončar NL, Fraaije MW. Not so monofunctional-a case of thermostable Thermobifida fusca catalase with peroxidase activity. in Applied Microbiology and Biotechnology. 2015;99(5):2225-2232.
doi:10.1007/s00253-014-6060-5 .

Lončar, Nikola L., Fraaije, Marco W., "Not so monofunctional-a case of thermostable Thermobifida fusca catalase with peroxidase activity" in Applied Microbiology and Biotechnology, 99, no. 5 (2015):2225-2232,
https://doi.org/10.1007/s00253-014-6060-5 . .