Characterization of Two Hydrogen Peroxide Resistant Peroxidases from <i>Rhodococcus opacus</i> 1CP
The dye-decolorizing peroxidases (DyP) are a family of heme-dependent enzymes present on a broad spectrum of microorganisms. While the natural function of these enzymes is not fully understood, their capacity to degrade highly contaminant pigments such as azo dyes or anthraquinones make them excelle...
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MDPI AG
2021-08-01
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| author | Anna Christina R. Ngo Catleen Conrad Álvaro Gómez Baraibar Anke Matura Karl-Heinz van Pée Dirk Tischler |
| author_facet | Anna Christina R. Ngo Catleen Conrad Álvaro Gómez Baraibar Anke Matura Karl-Heinz van Pée Dirk Tischler |
| author_sort | Anna Christina R. Ngo |
| collection | DOAJ |
| description | The dye-decolorizing peroxidases (DyP) are a family of heme-dependent enzymes present on a broad spectrum of microorganisms. While the natural function of these enzymes is not fully understood, their capacity to degrade highly contaminant pigments such as azo dyes or anthraquinones make them excellent candidates for applications in bioremediation and organic synthesis. In this work, two novel DyP peroxidases from the organism <i>Rhodococcus opacus</i> 1CP (DypA and DypB) were cloned and expressed in <i>Escherichia coli</i>. The enzymes were purified and biochemically characterized. The activities of the two DyPs via 2,2′-azino-bis [3-ethylbenzthiazoline-6-sulphonic acid] (ABTS) assay and against Reactive Blue 5 were assessed and optimized. Results showed varying trends for DypA and DypB. Remarkably, these enzymes presented a particularly high tolerance towards H<sub>2</sub>O<sub>2</sub>, retaining its activities at about 10 mM H<sub>2</sub>O<sub>2</sub> for DypA and about 4.9 mM H<sub>2</sub>O<sub>2</sub> for DypB. |
| first_indexed | 2024-03-10T08:16:31Z |
| format | Article |
| id | doaj.art-8a032add4c4f44c199eb8671f1699484 |
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| issn | 2076-3417 |
| language | English |
| last_indexed | 2024-03-10T08:16:31Z |
| publishDate | 2021-08-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Applied Sciences |
| spelling | doaj.art-8a032add4c4f44c199eb8671f16994842023-11-22T10:18:54ZengMDPI AGApplied Sciences2076-34172021-08-011117794110.3390/app11177941Characterization of Two Hydrogen Peroxide Resistant Peroxidases from <i>Rhodococcus opacus</i> 1CPAnna Christina R. Ngo0Catleen Conrad1Álvaro Gómez Baraibar2Anke Matura3Karl-Heinz van Pée4Dirk Tischler5Microbial Biotechnology, Ruhr University Bochum, Universitätsstraße 150, 44780 Bochum, GermanyInstitute of Biosciences, Environmental Microbiology, TU Bergakademie Freiberg, Leipziger Str. 29, 09599 Freiberg, GermanyMicrobial Biotechnology, Ruhr University Bochum, Universitätsstraße 150, 44780 Bochum, GermanyAllgemeine Biochemie, Technische Universität Dresden, 01062 Dresden, GermanyAllgemeine Biochemie, Technische Universität Dresden, 01062 Dresden, GermanyMicrobial Biotechnology, Ruhr University Bochum, Universitätsstraße 150, 44780 Bochum, GermanyThe dye-decolorizing peroxidases (DyP) are a family of heme-dependent enzymes present on a broad spectrum of microorganisms. While the natural function of these enzymes is not fully understood, their capacity to degrade highly contaminant pigments such as azo dyes or anthraquinones make them excellent candidates for applications in bioremediation and organic synthesis. In this work, two novel DyP peroxidases from the organism <i>Rhodococcus opacus</i> 1CP (DypA and DypB) were cloned and expressed in <i>Escherichia coli</i>. The enzymes were purified and biochemically characterized. The activities of the two DyPs via 2,2′-azino-bis [3-ethylbenzthiazoline-6-sulphonic acid] (ABTS) assay and against Reactive Blue 5 were assessed and optimized. Results showed varying trends for DypA and DypB. Remarkably, these enzymes presented a particularly high tolerance towards H<sub>2</sub>O<sub>2</sub>, retaining its activities at about 10 mM H<sub>2</sub>O<sub>2</sub> for DypA and about 4.9 mM H<sub>2</sub>O<sub>2</sub> for DypB.https://www.mdpi.com/2076-3417/11/17/7941Dyp-type peroxidaseheme-dependent enzymedye degradationbiotransformationActionbacteriaH<sub>2</sub>O<sub>2</sub> tolerance |
| spellingShingle | Anna Christina R. Ngo Catleen Conrad Álvaro Gómez Baraibar Anke Matura Karl-Heinz van Pée Dirk Tischler Characterization of Two Hydrogen Peroxide Resistant Peroxidases from <i>Rhodococcus opacus</i> 1CP Applied Sciences Dyp-type peroxidase heme-dependent enzyme dye degradation biotransformation Actionbacteria H<sub>2</sub>O<sub>2</sub> tolerance |
| title | Characterization of Two Hydrogen Peroxide Resistant Peroxidases from <i>Rhodococcus opacus</i> 1CP |
| title_full | Characterization of Two Hydrogen Peroxide Resistant Peroxidases from <i>Rhodococcus opacus</i> 1CP |
| title_fullStr | Characterization of Two Hydrogen Peroxide Resistant Peroxidases from <i>Rhodococcus opacus</i> 1CP |
| title_full_unstemmed | Characterization of Two Hydrogen Peroxide Resistant Peroxidases from <i>Rhodococcus opacus</i> 1CP |
| title_short | Characterization of Two Hydrogen Peroxide Resistant Peroxidases from <i>Rhodococcus opacus</i> 1CP |
| title_sort | characterization of two hydrogen peroxide resistant peroxidases from i rhodococcus opacus i 1cp |
| topic | Dyp-type peroxidase heme-dependent enzyme dye degradation biotransformation Actionbacteria H<sub>2</sub>O<sub>2</sub> tolerance |
| url | https://www.mdpi.com/2076-3417/11/17/7941 |
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