Description of the first fungal dye-decolorizing peroxidase oxidizing manganese(II)

Fernandez-Fueyo, Elena; Linde, Dolores; Almendral, David; Lopez-Lucendo, María F.; Ruiz-Duenas, Francisco J.; Martinez, Angel T.

doi:10.1007/s00253-015-6665-3

Description of the first fungal dye-decolorizing peroxidase oxidizing manganese(II)

Journal Article · Wed May 13 00:00:00 EDT 2015 · Applied Microbiology and Biotechnology

DOI:https://doi.org/10.1007/s00253-015-6665-3· OSTI ID:1343259

Fernandez-Fueyo, Elena ^[1]; Linde, Dolores ^[2]; Almendral, David ^[2]; Lopez-Lucendo, María F. ^[2]; Ruiz-Duenas, Francisco J. ^[2]; Martinez, Angel T. ^[2]

Centro de Investigaciones Biologicas, Madrid (Spain); Office of Scientific and Technical Information (OSTI)
Centro de Investigaciones Biologicas, Madrid (Spain)

Two phylogenetically divergent genes of the new family of dye-decolorizing peroxidases (DyPs) were found during comparison of the four DyP genes identified in the Pleurotus ostreatus genome with over 200 DyP genes from other basidiomycete genomes. The heterologously expressed enzymes (Pleos-DyP1 and Pleos-DyP4, following the genome nomenclature) efficiently oxidize anthraquinoid dyes (such as Reactive Blue 19), which are characteristic DyP substrates, as well as low redox-potential dyes (such as 2,2-azinobis-(3-ethylbenzothiazoline-6-sulfonic acid)) and substituted phenols. However, only Pleos-DyP4 oxidizes the high redox-potential dye Reactive Black 5, at the same time that it displays high thermal and pH stability. Unexpectedly, both enzymes also oxidize Mn²⁺ to Mn³⁺, albeit with very different catalytic efficiencies. Pleos-DyP4 presents a Mn²⁺ turnover (56 s^–1) nearly in the same order of the two other Mn²⁺-oxidizing peroxidase families identified in the P. ostreatus genome: manganese peroxidases (100 ^s–1 average turnover) and versatile peroxidases (145 s^–1 average turnover), whose genes were also heterologously expressed. Oxidation of Mn²⁺ has been reported for an Amycolatopsis DyP (24 s^–1) and claimed for other bacterial DyPs, albeit with lower activities, but this is the first time that Mn²⁺ oxidation is reported for a fungal DyP. Interestingly, Pleos-DyP4 (together with ligninolytic peroxidases) is detected in the secretome of P. ostreatus grown on different lignocellulosic substrates. In conclusion, it is suggested that generation of Mn³⁺ oxidizers plays a role in the P. ostreatus white-rot lifestyle since three different families of Mn²⁺-oxidizing peroxidase genes are present in its genome being expressed during lignocellulose degradation.

View Accepted Manuscript (DOE)

Research Organization:: Center for Biological Research (CIB), Madrid (Spain)

Sponsoring Organization:: Spanish Ministry of Economy and Competitiveness (MINECO) (Spain); USDOE Office of Science (SC)

Grant/Contract Number:: AC02-05CH11231

OSTI ID:: 1343259

Journal Information:: Applied Microbiology and Biotechnology, Journal Name: Applied Microbiology and Biotechnology Journal Issue: 21 Vol. 99; ISSN 0175-7598

Publisher:: SpringerCopyright Statement

Country of Publication:: United States

Language:: English

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Enzymatic Degradation of Lignin in Soil: A Review Datta, Rahul; Kelkar, Aditi; Baraniya, Divyashri Sustainability, Vol. 9, Issue 7 https://doi.org/10.3390/su9071163	journal	July 2017

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59 BASIC BIOLOGICAL SCIENCES
60 APPLIED LIFE SCIENCES
Dye-decolorizing peroxidases
Evolutionary history
Genome mining
Lignocellulose secretome
Manganese(II) oxidation
Pleurotus ostreatus

Description of the first fungal dye-decolorizing peroxidase oxidizing manganese(II)

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