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Expression and characterization of a dye-decolorizing peroxidase from pseudomonas fluorescens Pf0-1

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2019
Expression_and_Characterization_pub_2019.pdf (2.047Mb)
Authors
Lončar, Nikola L.
Drašković, Natalija
Božić, Nataša
Romero, Elvira
Simić, Stefan
Opsenica, Igor
Vujčić, Zoran
Fraaije, Marco W.
Article (Published version)
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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 incre...ase 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.

Keywords:
Decolorization / DyP peroxidase / Oxidoreductase / Reactive dye
Source:
Catalysts, 2019, 9, 5
Publisher:
  • MDPI
Funding / projects:
  • Production, purification and characterization of enzymes and small molecules and their application as soluble or immobilized in food biotechnology, biofuels production and environmental protection (RS-172048)
Note:
  • Supplementary material: http://cherry.chem.bg.ac.rs/handle/123456789/3710

DOI: 10.3390/catal9050463

ISSN: 2073-4344

WoS: 000472678500072

Scopus: 2-s2.0-85066730056
[ Google Scholar ]
10
5
URI
https://cherry.chem.bg.ac.rs/handle/123456789/3709
Collections
  • Publikacije / Publications
  • Publikacije / Publications
Institution/Community
Hemijski fakultet
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 . .

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