ArticleBiotechnology for biofuels2014
Ligninolytic peroxidase genes in the oyster mushroom genome: heterologous expression, molecular structure, catalytic and stability properties, and lignin-degrading ability.
Article in Biotechnology for biofuels, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
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Who cites it
53 citing papers in PubMed, 137 citations in OpenAlex.
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- Semiautomated Monitoring of Longitudinal Microbial Metabolic Dynamics: A Study Case for Lignin Degradation.ACS omega · 2026Article
- Enzymatic and Non-Enzymatic decolorization of synthetic dyes using spent mushroom substrate.World journal of microbiology & biotechnology · 2025Article
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- Structure-function characterization of two enzymes from novel subfamilies of manganese peroxidases secreted by the lignocellulose-degrading Agaricales fungi Agrocybe pediades and Cyathus striatus.Biotechnology for biofuels and bioproducts · 2024Article
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- Development of reference genes for RT-qPCR analysis of gene expression in Pleurotus pulmonarius for biotechnological applications.Scientific reports · 2023Article
- A mutant R70V/E166A of short manganese peroxidase showing MnApplied microbiology and biotechnology · 2023Article
- Recent Theoretical Insights into the Oxidative Degradation of Biopolymers and Plastics by Metalloenzymes.International journal of molecular sciences · 2023Review
- Recent Advancements and Challenges in Lignin Valorization: Green Routes towards Sustainable Bioproducts.Molecules (Basel, Switzerland) · 2022Review
- Looking into the world's largest elephant population in search of ligninolytic microorganisms for biorefineries: a mini-review.Biotechnology for biofuels and bioproducts · 2022Review
- Fluoxetine Removal from Aqueous Solutions Using a Lignocellulosic Substrate Colonized by the White-Rot FungusInternational journal of environmental research and public health · 2022Article
- Recent Advances in Synthesis and Degradation of Lignin and Lignin Nanoparticles and Their Emerging Applications in Nanotechnology.Materials (Basel, Switzerland) · 2022Review
- The Manganese Peroxidase Gene Family ofMicroorganisms · 2021Article
- Wood-feeding termite gut symbionts as an obscure yet promising source of novel manganese peroxidase-producing oleaginous yeasts intended for azo dye decolorization and biodiesel production.Biotechnology for biofuels · 2021Article
- A plant host, Nicotiana benthamiana, enables the production and study of fungal lignin-degrading enzymes.Communications biology · 2021Article
- A Multiomic Approach to Understand HowJournal of fungi (Basel, Switzerland) · 2021Article
- Experimental and theoretical insights into the effects of pH on catalysis of bond-cleavage by the lignin peroxidase isozyme H8 from Phanerochaete chrysosporium.Biotechnology for biofuels · 2021Article
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundThe genome of Pleurotus ostreatus, an important edible mushroom and a model ligninolytic organism of interest in lignocellulose biorefineries due to its ability to delignify agricultural wastes, was sequenced with the purpose of identifying and characterizing the enzymes responsible for lignin degradation.
resultsHeterologous expression of the class II peroxidase genes, followed by kinetic studies, enabled their functional classification. The resulting inventory revealed the absence of lignin peroxidases (LiPs) and the presence of three versatile peroxidases (VPs) and six manganese peroxidases (MnPs), the crystal structures of two of them (VP1 and MnP4) were solved at 1.0 to 1.1 Å showing significant structural differences. Gene expansion supports the importance of both peroxidase types in the white-rot lifestyle of this fungus. Using a lignin model dimer and synthetic lignin, we showed that VP is able to degrade lignin. Moreover, the dual Mn-mediated and Mn-independent activity of P. ostreatus MnPs justifies their inclusion in a new peroxidase subfamily. The availability of the whole POD repertoire enabled investigation, at a biochemical level, of the existence of duplicated genes. Differences between isoenzymes are not limited to their kinetic constants. Surprising differences in their activity T50 and residual activity at both acidic and alkaline pH were observed. Directed mutagenesis and spectroscopic/structural information were combined to explain the catalytic and stability properties of the most interesting isoenzymes, and their evolutionary history was analyzed in the context of over 200 basidiomycete peroxidase sequences.
conclusionsThe analysis of the P. ostreatus genome shows a lignin-degrading system where the role generally played by LiP has been assumed by VP. Moreover, it enabled the first characterization of the complete set of peroxidase isoenzymes in a basidiomycete, revealing strong differences in stability properties and providing enzymes of biotechnological interest.
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