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Expression and Characterization of a Dye-Decolorizing Peroxidase from Pseudomonas Fluorescens Pf0-1

Authors: Nikola Lončar; Natalija Draskovic; Natasa Bozic; Elvira Romero; Stefan Simić; Igor Opsenica; Zoran Vujčić; +1 Authors

Expression and Characterization of a Dye-Decolorizing Peroxidase from Pseudomonas Fluorescens Pf0-1

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 (PfDyP B2) could be overexpressed as a soluble protein. PfDyP 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 PfDyP B2 in calcium-alginate beads resulted in a significant increase in stability: PfDyP B2 retains 80% of its initial activity after 2 h incubation at 50 °

C, while the soluble enzyme is inactivated within minutes. PfDyP 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.

Countries
Serbia, Netherlands, Serbia
Subjects by Vocabulary

Microsoft Academic Graph classification: Population Pseudomonas fluorescens medicine.disease_cause chemistry.chemical_compound medicine Reactive dye education Hydrogen peroxide Escherichia coli Dye decolorizing peroxidase education.field_of_study biology Substrate (chemistry) biology.organism_classification Biochemistry chemistry biology.protein Peroxidase

Library of Congress Subject Headings: lcsh:Chemical technology lcsh:Chemistry lcsh:TP1-1185 lcsh:QD1-999

Keywords

Reactive dye, TP1-1185, OXIDATION, Catalysis, PF-5, Physical and Theoretical Chemistry, QD1-999, oxidoreductase, IDENTIFICATION, Chemical technology, Decolorization, HEME, decolorization, Chemistry, Oxidoreductase, reactive dye, DyP peroxidase, ENZYMES, LIGNIN

33 references, page 1 of 4

1. Fraaije, M.W.; Bloois, E.V. DyP-type peroxidases: A promising and versatile class of enzymes. Enzym. Eng. 2012, 1, 1-3. [CrossRef]

2. Colpa, D.I.; Fraaije, M.W.; van Bloois, E. DyP-type peroxidases: A promising and versatile class of enzymes. J. Ind. Microbiol. Biotechnol. 2014, 41, 1-7. [CrossRef] [PubMed] [OpenAIRE]

3. Loncˇar, N.; Colpa, D.I.; Fraaije, M.W. Exploring the biocatalytic potential of a DyP-type peroxidase by profiling the substrate acceptance of Thermobifida fusca DyP peroxidase. Tetrahedron 2016, 72, 7276-7281. [CrossRef] [OpenAIRE]

4. Liers, C.; Bobeth, C.; Pecyna, M.; Ullrich, R.; Hofrichter, M. DyP-like peroxidases of the jelly fungus Auricularia auricula-judae oxidize nonphenolic lignin model compounds and high-redox potential dyes. Appl. Microbiol. Biotechnol. 2010, 85, 1869-1879. [CrossRef]

5. Linde, D.; Ruiz-Duenas, F.J.; Fernandez-Fueyo, E.; Guallar, V.; Hammel, K.E.; Pogni, R.; Martinez, A.T. Basidiomycete DyPs: Genomic diversity, structural-functional aspects, reaction mechanism and environmental significance. Arch. Biochem. Biophys. 2015, 574, 66-74. [CrossRef]

6. Salvachua, D.; Prieto, A.; Martinez, A.T.; Martinez, M.J. Characterization of a novel dye-decolorizing peroxidase (DyP)-type enzyme from Irpex lacteus and its application in enzymatic hydrolysis of wheat straw. Appl. Environ. Microbiol. 2013, 79, 4316-4324. [CrossRef] [PubMed] [OpenAIRE]

7. Scheibner, M.; Hulsdau, B.; Zelena, K.; Nimtz, M.; de Boer, L.; Berger, R.G.; Zorn, H. Novel peroxidases of Marasmius scorodonius degrade beta-carotene. Appl. Microbiol. Biotechnol. 2008, 77, 1241-1250. [CrossRef] [OpenAIRE]

8. van Bloois, E.; Torres Pazmino, D.E.; Winter, R.T.; Fraaije, M.W. A robust and extracellular heme-containing peroxidase from Thermobifida fusca as prototype of a bacterial peroxidase superfamily. Appl. Microbiol. Biotechnol. 2010, 86, 1419-1430. [CrossRef] [OpenAIRE]

9. Habib, M.H.; Rozeboom, H.J.; Fraaije, M.W. Characterization of a new DyP-Peroxidase from the alkaliphilic cellulomonad, Cellulomonas bogoriensis. Molecules 2019, 24. [CrossRef] [OpenAIRE]

10. Colpa, D.I.; Loncˇar, N.; Schmidt, M.; Fraaije, M.W. Creating Oxidase-Peroxidase Fusion Enzymes as a Toolbox for Cascade Reactions. ChemBioChem 2017, 18, 2226-2230. [CrossRef] [OpenAIRE]

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citations
This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
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popularity
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
BIP!Popularity provided by BIP!
influence
This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
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impulse
This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
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