Characterization of Two Hydrogen Peroxide Resistant Peroxidases from Rhodococcus opacus 1CP

• Published in: Applied sciences Vol. 11; no. 17; p. 7941
• Main Authors: Ngo, Anna Christina R., Conrad, Catleen, Gómez Baraibar, Álvaro, Matura, Anke, van Pée, Karl-Heinz, Tischler, Dirk
• Format: Journal Article
• Language: English
• Published: Basel MDPI AG 01.09.2021
• Subjects: Actionbacteria; Anthraquinone dyes; Antibiotics; Azo dyes; Bioremediation; biotransformation; Chemicals; Cloning; Contaminants; Decoloring; dye degradation; Dyp-type peroxidase; E coli; Enzymes; Gene expression; H2O2 tolerance; Heme; heme-dependent enzyme; Hydrogen peroxide; Lignin; Microorganisms; Mutation; Pigments; Plasmids; Proteins; Rhodococcus; Rhodococcus opacus; Sulfonic acid; Germany
• ISSN: 2076-3417; 2076-3417
• DOI: 10.3390/app11177941

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 Rhodococcus opacus 1CP (DypA and DypB) were cloned and expressed in Escherichia coli. 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 H2O2, retaining its activities at about 10 mM H2O2 for DypA and about 4.9 mM H2O2 for DypB.