TY  - JOUR
AU  - Lončar, Nikola L.
AU  - Drašković, Natalija
AU  - Božić, Nataša
AU  - Romero, Elvira
AU  - Simić, Stefan
AU  - Opsenica, Igor
AU  - Vujčić, Zoran
AU  - Fraaije, Marco W.
PY  - 2019
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3709
AB  - The consumption of dyes is increasing worldwide in line with the increase of population and demand for clothes and other colored products. However, the efficiency of dyeing processes is still poor and results in large amounts of colored effluents. It is desired to develop a portfolio of enzymes which can be used for the treatment of colored wastewaters. Herein, we used genome sequence information to discover a dye-decolorizing peroxidase (DyP) from Pseudomonas fluorescens Pf-01. Two genes putatively encoding for DyPs were identified in the respective genome and cloned for expression in Escherichia coli, of which one (Pf DyP B2) could be overexpressed as a soluble protein. Pf DyP B2 shows some typical features known for DyPs which includes the ability to convert dyes at the expense of hydrogen peroxide. Interestingly, t-butyl hydroperoxide could be used as an alternative substrate to hydrogen peroxide. Immobilization of Pf DyP B2 in calcium-alginate beads resulted in a significant increase in stability: Pf DyP B2 retains 80% of its initial activity after 2 h incubation at 50◦ C, while the soluble enzyme is inactivated within minutes. Pf DyP B2 was also tested with aniline and ethyl diazoacetate as substrates. Based on GC-MS analyses, 30% conversion of the starting material was achieved after 65 h at 30◦ C. Importantly, this is the first report of a DyP-catalyzed insertion of a carbene into an N-H bond.
PB  - MDPI
T2  - Catalysts
T1  - Expression and characterization of a dye-decolorizing peroxidase from pseudomonas fluorescens Pf0-1
VL  - 9
IS  - 5
DO  - 10.3390/catal9050463
ER  - 

@article{
author = "Lončar, Nikola L. and Drašković, Natalija and Božić, Nataša and Romero, Elvira and Simić, Stefan and Opsenica, Igor and Vujčić, Zoran and Fraaije, Marco W.",
year = "2019",
abstract = "The consumption of dyes is increasing worldwide in line with the increase of population and demand for clothes and other colored products. However, the efficiency of dyeing processes is still poor and results in large amounts of colored effluents. It is desired to develop a portfolio of enzymes which can be used for the treatment of colored wastewaters. Herein, we used genome sequence information to discover a dye-decolorizing peroxidase (DyP) from Pseudomonas fluorescens Pf-01. Two genes putatively encoding for DyPs were identified in the respective genome and cloned for expression in Escherichia coli, of which one (Pf DyP B2) could be overexpressed as a soluble protein. Pf DyP B2 shows some typical features known for DyPs which includes the ability to convert dyes at the expense of hydrogen peroxide. Interestingly, t-butyl hydroperoxide could be used as an alternative substrate to hydrogen peroxide. Immobilization of Pf DyP B2 in calcium-alginate beads resulted in a significant increase in stability: Pf DyP B2 retains 80% of its initial activity after 2 h incubation at 50◦ C, while the soluble enzyme is inactivated within minutes. Pf DyP B2 was also tested with aniline and ethyl diazoacetate as substrates. Based on GC-MS analyses, 30% conversion of the starting material was achieved after 65 h at 30◦ C. Importantly, this is the first report of a DyP-catalyzed insertion of a carbene into an N-H bond.",
publisher = "MDPI",
journal = "Catalysts",
title = "Expression and characterization of a dye-decolorizing peroxidase from pseudomonas fluorescens Pf0-1",
volume = "9",
number = "5",
doi = "10.3390/catal9050463"
}

Lončar, N. L., Drašković, N., Božić, N., Romero, E., Simić, S., Opsenica, I., Vujčić, Z.,& Fraaije, M. W.. (2019). Expression and characterization of a dye-decolorizing peroxidase from pseudomonas fluorescens Pf0-1. in Catalysts
MDPI., 9(5).
https://doi.org/10.3390/catal9050463

Lončar NL, Drašković N, Božić N, Romero E, Simić S, Opsenica I, Vujčić Z, Fraaije MW. Expression and characterization of a dye-decolorizing peroxidase from pseudomonas fluorescens Pf0-1. in Catalysts. 2019;9(5).
doi:10.3390/catal9050463 .

Lončar, Nikola L., Drašković, Natalija, Božić, Nataša, Romero, Elvira, Simić, Stefan, Opsenica, Igor, Vujčić, Zoran, Fraaije, Marco W., "Expression and characterization of a dye-decolorizing peroxidase from pseudomonas fluorescens Pf0-1" in Catalysts, 9, no. 5 (2019),
https://doi.org/10.3390/catal9050463 . .

TY  - DATA
AU  - Lončar, Nikola L.
AU  - Drašković, Natalija
AU  - Božić, Nataša
AU  - Romero, Elvira
AU  - Simić, Stefan
AU  - Opsenica, Igor
AU  - Vujčić, Zoran
AU  - Fraaije, Marco W.
PY  - 2019
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3710
PB  - MDPI
T2  - Catalysts
T1  - Supplementary data for the article: Lončar, N.; Drašković, N.; Božić, N.; Romero, E.; Simić, S.; Opsenica, I.; Vujčić, Z.; Fraaije, M. W. Expression and Characterization of a Dye-Decolorizing Peroxidase from Pseudomonas Fluorescens Pf0-1. Catalysts 2019, 9 (5). https://doi.org/10.3390/catal9050463
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3710
ER  - 

@misc{
author = "Lončar, Nikola L. and Drašković, Natalija and Božić, Nataša and Romero, Elvira and Simić, Stefan and Opsenica, Igor and Vujčić, Zoran and Fraaije, Marco W.",
year = "2019",
publisher = "MDPI",
journal = "Catalysts",
title = "Supplementary data for the article: Lončar, N.; Drašković, N.; Božić, N.; Romero, E.; Simić, S.; Opsenica, I.; Vujčić, Z.; Fraaije, M. W. Expression and Characterization of a Dye-Decolorizing Peroxidase from Pseudomonas Fluorescens Pf0-1. Catalysts 2019, 9 (5). https://doi.org/10.3390/catal9050463",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3710"
}

Lončar, N. L., Drašković, N., Božić, N., Romero, E., Simić, S., Opsenica, I., Vujčić, Z.,& Fraaije, M. W.. (2019). Supplementary data for the article: Lončar, N.; Drašković, N.; Božić, N.; Romero, E.; Simić, S.; Opsenica, I.; Vujčić, Z.; Fraaije, M. W. Expression and Characterization of a Dye-Decolorizing Peroxidase from Pseudomonas Fluorescens Pf0-1. Catalysts 2019, 9 (5). https://doi.org/10.3390/catal9050463. in Catalysts
MDPI..
https://hdl.handle.net/21.15107/rcub_cherry_3710

Lončar NL, Drašković N, Božić N, Romero E, Simić S, Opsenica I, Vujčić Z, Fraaije MW. Supplementary data for the article: Lončar, N.; Drašković, N.; Božić, N.; Romero, E.; Simić, S.; Opsenica, I.; Vujčić, Z.; Fraaije, M. W. Expression and Characterization of a Dye-Decolorizing Peroxidase from Pseudomonas Fluorescens Pf0-1. Catalysts 2019, 9 (5). https://doi.org/10.3390/catal9050463. in Catalysts. 2019;.
https://hdl.handle.net/21.15107/rcub_cherry_3710 .

Lončar, Nikola L., Drašković, Natalija, Božić, Nataša, Romero, Elvira, Simić, Stefan, Opsenica, Igor, Vujčić, Zoran, Fraaije, Marco W., "Supplementary data for the article: Lončar, N.; Drašković, N.; Božić, N.; Romero, E.; Simić, S.; Opsenica, I.; Vujčić, Z.; Fraaije, M. W. Expression and Characterization of a Dye-Decolorizing Peroxidase from Pseudomonas Fluorescens Pf0-1. Catalysts 2019, 9 (5). https://doi.org/10.3390/catal9050463" in Catalysts (2019),
https://hdl.handle.net/21.15107/rcub_cherry_3710 .

TY  - JOUR
AU  - Lončar, Nikola L.
AU  - Colpa, Dana I.
AU  - Fraaije, Marco W.
PY  - 2016
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2342
AB  - Dye-decolorizing peroxidases (DyPs) represent a new class of oxidative enzymes for which the natural substrates are largely unknown. To explore the biocatalytic potential of a DyP, we have studied the substrate acceptance profile of a robust DyP peroxidase, a DyP from Thermobifida fusca (TfuDyP). While previous work established that this bacterial peroxidase is able to act on a few reactive dyes and aromatic sulfides, this work significantly expands its substrate scope towards lignin related compounds, flavors, and various dyes. (C) 2016 Elsevier Ltd. All rights reserved.
PB  - Pergamon-Elsevier Science Ltd, Oxford
T2  - Tetrahedron
T1  - Exploring the biocatalytic potential of a DyP-type peroxidase by profiling the substrate acceptance of Thermobifida fusca DyP peroxidase
VL  - 72
IS  - 46
SP  - 7276
EP  - 7281
DO  - 10.1016/j.tet.2015.12.078
ER  - 

@article{
author = "Lončar, Nikola L. and Colpa, Dana I. and Fraaije, Marco W.",
year = "2016",
abstract = "Dye-decolorizing peroxidases (DyPs) represent a new class of oxidative enzymes for which the natural substrates are largely unknown. To explore the biocatalytic potential of a DyP, we have studied the substrate acceptance profile of a robust DyP peroxidase, a DyP from Thermobifida fusca (TfuDyP). While previous work established that this bacterial peroxidase is able to act on a few reactive dyes and aromatic sulfides, this work significantly expands its substrate scope towards lignin related compounds, flavors, and various dyes. (C) 2016 Elsevier Ltd. All rights reserved.",
publisher = "Pergamon-Elsevier Science Ltd, Oxford",
journal = "Tetrahedron",
title = "Exploring the biocatalytic potential of a DyP-type peroxidase by profiling the substrate acceptance of Thermobifida fusca DyP peroxidase",
volume = "72",
number = "46",
pages = "7276-7281",
doi = "10.1016/j.tet.2015.12.078"
}

Lončar, N. L., Colpa, D. I.,& Fraaije, M. W.. (2016). Exploring the biocatalytic potential of a DyP-type peroxidase by profiling the substrate acceptance of Thermobifida fusca DyP peroxidase. in Tetrahedron
Pergamon-Elsevier Science Ltd, Oxford., 72(46), 7276-7281.
https://doi.org/10.1016/j.tet.2015.12.078

Lončar NL, Colpa DI, Fraaije MW. Exploring the biocatalytic potential of a DyP-type peroxidase by profiling the substrate acceptance of Thermobifida fusca DyP peroxidase. in Tetrahedron. 2016;72(46):7276-7281.
doi:10.1016/j.tet.2015.12.078 .

Lončar, Nikola L., Colpa, Dana I., Fraaije, Marco W., "Exploring the biocatalytic potential of a DyP-type peroxidase by profiling the substrate acceptance of Thermobifida fusca DyP peroxidase" in Tetrahedron, 72, no. 46 (2016):7276-7281,
https://doi.org/10.1016/j.tet.2015.12.078 . .

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 . .

TY  - JOUR
AU  - Lončar, Nikola L.
AU  - Fraaije, Marco W.
PY  - 2015
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1682
AB  - Catalases represent a class of enzymes which has found its place among industrially relevant biocatalysts due to their exceptional catalytic rate and high stability. Textile bleaching prior to the dyeing process is the main application and has been performed on a large scale for the past few decades. Their limited substrate scope has not prevented the development of various other catalase-based applications. Newly developed approaches continue to exploit their excellent catalytic potential to degrade hydrogen peroxide while (per)oxidase activity of catalases is opening a new range of possibilities as well. This review provides an overview of applications that involve heme-containing catalases that have been demonstrated in recent years.
PB  - Springer, New York
T2  - Applied Microbiology and Biotechnology
T1  - Catalases as biocatalysts in technical applications: current state and perspectives
VL  - 99
IS  - 8
SP  - 3351
EP  - 3357
DO  - 10.1007/s00253-015-6512-6
ER  - 

@article{
author = "Lončar, Nikola L. and Fraaije, Marco W.",
year = "2015",
abstract = "Catalases represent a class of enzymes which has found its place among industrially relevant biocatalysts due to their exceptional catalytic rate and high stability. Textile bleaching prior to the dyeing process is the main application and has been performed on a large scale for the past few decades. Their limited substrate scope has not prevented the development of various other catalase-based applications. Newly developed approaches continue to exploit their excellent catalytic potential to degrade hydrogen peroxide while (per)oxidase activity of catalases is opening a new range of possibilities as well. This review provides an overview of applications that involve heme-containing catalases that have been demonstrated in recent years.",
publisher = "Springer, New York",
journal = "Applied Microbiology and Biotechnology",
title = "Catalases as biocatalysts in technical applications: current state and perspectives",
volume = "99",
number = "8",
pages = "3351-3357",
doi = "10.1007/s00253-015-6512-6"
}

Lončar, N. L.,& Fraaije, M. W.. (2015). Catalases as biocatalysts in technical applications: current state and perspectives. in Applied Microbiology and Biotechnology
Springer, New York., 99(8), 3351-3357.
https://doi.org/10.1007/s00253-015-6512-6

Lončar NL, Fraaije MW. Catalases as biocatalysts in technical applications: current state and perspectives. in Applied Microbiology and Biotechnology. 2015;99(8):3351-3357.
doi:10.1007/s00253-015-6512-6 .

Lončar, Nikola L., Fraaije, Marco W., "Catalases as biocatalysts in technical applications: current state and perspectives" in Applied Microbiology and Biotechnology, 99, no. 8 (2015):3351-3357,
https://doi.org/10.1007/s00253-015-6512-6 . .