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Article

Comparing Ligninolytic Capabilities of Bacterial and Fungal Dye-Decolorizing Peroxidases and Class-II Peroxidase-Catalases

1
Centro de Investigaciones Biológicas “Margarita Salas” (CIB), CSIC, Ramiro de Maeztu 9, E-28040 Madrid, Spain
2
Instituto de Catálisis y Petroleoquímica (ICP), CSIC, Marie Curie 2, E-28049 Madrid, Spain
*
Author to whom correspondence should be addressed.
These two authors contributed equally to this work.
Current address: Norwegian University of Life Sciences (NMBU), 1430 Ås, Norway.
Academic Editor: Yasushi Sugano
Int. J. Mol. Sci. 2021, 22(5), 2629; https://doi.org/10.3390/ijms22052629
Received: 3 February 2021 / Revised: 27 February 2021 / Accepted: 28 February 2021 / Published: 5 March 2021
(This article belongs to the Special Issue Universe of DyP-type Peroxidase)
We aim to clarify the ligninolytic capabilities of dye-decolorizing peroxidases (DyPs) from bacteria and fungi, compared to fungal lignin peroxidase (LiP) and versatile peroxidase (VP). With this purpose, DyPs from Amycolatopsis sp., Thermomonospora curvata, and Auricularia auricula-judae, VP from Pleurotus eryngii, and LiP from Phanerochaete chrysosporium were produced, and their kinetic constants and reduction potentials determined. Sharp differences were found in the oxidation of nonphenolic simple (veratryl alcohol, VA) and dimeric (veratrylglycerol-β- guaiacyl ether, VGE) lignin model compounds, with LiP showing the highest catalytic efficiencies (around 15 and 200 s−1·mM−1 for VGE and VA, respectively), while the efficiency of the A. auricula-judae DyP was 1–3 orders of magnitude lower, and no activity was detected with the bacterial DyPs. VP and LiP also showed the highest reduction potential (1.28–1.33 V) in the rate-limiting step of the catalytic cycle (i.e., compound-II reduction to resting enzyme), estimated by stopped-flow measurements at the equilibrium, while the T. curvata DyP showed the lowest value (1.23 V). We conclude that, when using realistic enzyme doses, only fungal LiP and VP, and in much lower extent fungal DyP, oxidize nonphenolic aromatics and, therefore, have the capability to act on the main moiety of the native lignin macromolecule. View Full-Text
Keywords: lignin transformation; dye-decolorizing peroxidases; lignin peroxidases; versatile peroxidases; lignin model dimers; reduction potential; kinetic constants; long-range electron transfer lignin transformation; dye-decolorizing peroxidases; lignin peroxidases; versatile peroxidases; lignin model dimers; reduction potential; kinetic constants; long-range electron transfer
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MDPI and ACS Style

Linde, D.; Ayuso-Fernández, I.; Laloux, M.; Aguiar-Cervera, J.E.; de Lacey, A.L.; Ruiz-Dueñas, F.J.; Martínez, A.T. Comparing Ligninolytic Capabilities of Bacterial and Fungal Dye-Decolorizing Peroxidases and Class-II Peroxidase-Catalases. Int. J. Mol. Sci. 2021, 22, 2629. https://doi.org/10.3390/ijms22052629

AMA Style

Linde D, Ayuso-Fernández I, Laloux M, Aguiar-Cervera JE, de Lacey AL, Ruiz-Dueñas FJ, Martínez AT. Comparing Ligninolytic Capabilities of Bacterial and Fungal Dye-Decolorizing Peroxidases and Class-II Peroxidase-Catalases. International Journal of Molecular Sciences. 2021; 22(5):2629. https://doi.org/10.3390/ijms22052629

Chicago/Turabian Style

Linde, Dolores, Iván Ayuso-Fernández, Marcos Laloux, José E. Aguiar-Cervera, Antonio L. de Lacey, Francisco J. Ruiz-Dueñas, and Angel T. Martínez. 2021. "Comparing Ligninolytic Capabilities of Bacterial and Fungal Dye-Decolorizing Peroxidases and Class-II Peroxidase-Catalases" International Journal of Molecular Sciences 22, no. 5: 2629. https://doi.org/10.3390/ijms22052629

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