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The Comparative Abilities of a Small Laccase and a Dye-Decoloring Peroxidase From the Same Bacterium to Transform Natural and Technical Lignins

https://doi.org/10.3389/fmicb.2021.723524
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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1002/bab.2015openalex-snapshot
Biochemical features of dye‐decolorizing peroxidases: Current impact on lignin degradation
inferredcites →https://doi.org/10.1002/jms.3541openalex-snapshot
A critique on the structural analysis of lignins and application of novel tandem mass spectrometric strategies to determine lignin sequencing
inferredcites →https://doi.org/10.1002/jobm.200900338openalex-snapshot
Lignin‐modifying enzymes in filamentous basidiomycetes – ecological, functional and phylogenetic review
inferredcites →https://doi.org/10.1007/s00018-014-1826-6openalex-snapshot
Electron transfer and reaction mechanism of laccases
inferredcites →https://doi.org/10.1007/s00253-016-7560-2openalex-snapshot
Comparative analysis of lignin peroxidase and manganese peroxidase activity on coniferous and deciduous wood using ToF-SIMS
inferredcites →https://doi.org/10.1007/s10295-013-1371-6openalex-snapshot
DyP-type Peroxidases: A Promising and Versatile Class of Enzymes
inferredcites →https://doi.org/10.1007/s12010-008-8279-zopenalex-snapshot
Structure and Action Mechanism of Ligninolytic Enzymes
inferredcites →https://doi.org/10.1016/j.biotechadv.2014.12.008openalex-snapshot
Can laccases catalyze bond cleavage in lignin?
inferredcites →https://doi.org/10.1016/j.biotechadv.2017.06.003openalex-snapshot
Oxidoreductases on their way to industrial biotransformations
inferredcites →https://doi.org/10.1016/j.copbio.2014.01.009openalex-snapshot
Advancing lignocellulose bioconversion through direct assessment of enzyme action on insoluble substrates
inferredcites →https://doi.org/10.1016/j.copbio.2019.02.018openalex-snapshot
Lignin biosynthesis and its integration into metabolism
inferredcites →https://doi.org/10.1016/j.copbio.2019.02.019openalex-snapshot
Lignin structure and its engineering
inferredcites →https://doi.org/10.1016/j.enzmictec.2020.109669openalex-snapshot
Microbial lignin peroxidases: Applications, production challenges and future perspectives
inferredcites →https://doi.org/10.1016/j.jbiotec.2020.11.007openalex-snapshot
Lignin-oxidizing activity of bacterial laccases characterized using soluble substrates and polymeric lignin
inferredcites →https://doi.org/10.1016/j.molcatb.2007.11.023openalex-snapshot
Phenolic compounds as likely natural mediators of laccase: A mechanistic assessment
inferredcites →https://doi.org/10.1016/j.tibtech.2020.03.010openalex-snapshot
Harnessing the Power of Enzymes for Tailoring and Valorizing Lignin
inferredcites →https://doi.org/10.1016/s0014-5793(97)00301-3openalex-snapshot
Laccase is essential for lignin degradation by the white‐rot fungus Pycnoporus cinnabarinus
inferredcites →https://doi.org/10.1016/s0165-2370(00)00116-9openalex-snapshot
Studies on wheat lignin degradation by Pleurotus species using analytical pyrolysis
inferredcites →https://doi.org/10.1021/ac1023028openalex-snapshot
Expanding the Library of Secondary Ions That Distinguish Lignin and Polysaccharides in Time-of-Flight Secondary Ion Mass Spectrometry Analysis of Wood
inferredcites →https://doi.org/10.1021/ac3005346openalex-snapshot
Application of Time-of-Flight-Secondary Ion Mass Spectrometry for the Detection of Enzyme Activity on Solid Wood Substrates
inferredcites →https://doi.org/10.1021/acs.iecr.0c03718openalex-snapshot
Bromide-Based Ionic Liquid Treatment of Hardwood Organosolv Lignin Yielded a More Reactive Biobased Polyol
inferredcites →https://doi.org/10.1021/acssuschemeng.7b03451openalex-snapshot
Laccase/Mediator Systems: Their Reactivity toward Phenolic Lignin Structures
inferredcites →https://doi.org/10.1021/acssuschemeng.9b04912openalex-snapshot
Laccase-Catalyzed Oxidation of Lignin Induces Production of H 2 O 2
inferredcites →https://doi.org/10.1021/bi500285topenalex-snapshot
Roles of Small Laccases fromStreptomycesin Lignin Degradation
inferredcites →https://doi.org/10.1021/bm049521vopenalex-snapshot
Identifying the Characteristic Secondary Ions of Lignin Polymer Using ToF−SIMS
inferredcites →https://doi.org/10.1021/cb300383yopenalex-snapshot
Identification and Characterization of a Multifunctional Dye Peroxidase from a Lignin-Reactive Bacterium
inferredcites →https://doi.org/10.1021/ja203972qopenalex-snapshot
Discovery and Characterization of Heme Enzymes from Unsequenced Bacteria: Application to Microbial Lignin Degradation
inferredcites →https://doi.org/10.1038/srep42121openalex-snapshot
Enhanced delignification of steam-pretreated poplar by a bacterial laccase
inferredcites →https://doi.org/10.1074/jbc.m111.332171openalex-snapshot
Distal Heme Pocket Residues of B-type Dye-decolorizing Peroxidase
inferredcites →https://doi.org/10.1080/12298093.2020.1816151openalex-snapshot
Comparative Genomics Platform and Phylogenetic Analysis of Fungal Laccases and Multi-Copper Oxidases
inferredcites →https://doi.org/10.1110/ps.04759104openalex-snapshot
Characterization of SLAC: A small laccase from Streptomyces coelicolor with unprecedented activity
inferredcites →https://doi.org/10.1111/1751-7915.12422openalex-snapshot
Laccase: a multi‐purpose biocatalyst at the forefront of biotechnology
inferredcites →https://doi.org/10.1111/febs.13224openalex-snapshot
Lignin‐degrading enzymes
inferredcites →https://doi.org/10.1111/j.1574-4976.2005.00010.xopenalex-snapshot
Fungal laccases – occurrence and properties
inferredcites →https://doi.org/10.1111/ppl.12688openalex-snapshot
Direct analysis by time‐of‐flight secondary ion mass spectrometry reveals action of bacterial laccase‐mediator systems on both hardwood and softwood samples
inferredcites →https://doi.org/10.1186/1754-6834-6-132openalex-snapshot
Towards practical time-of-flight secondary ion mass spectrometry lignocellulolytic enzyme assays
inferredcites →https://doi.org/10.1186/1754-6834-7-6openalex-snapshot
Pretreatment with laccase and a phenolic mediator degrades lignin and enhances saccharification of Eucalyptus feedstock
inferredcites →https://doi.org/10.1186/s13068-020-01713-zopenalex-snapshot
Evidence for ligninolytic activity of the ascomycete fungus Podospora anserina
inferredcites →https://doi.org/10.1515/boca-2015-0007openalex-snapshot
Fungal laccases as tools for biodegradation of industrial dyes
inferredcites →https://doi.org/10.1515/hf-2017-0096openalex-snapshot
Demethylation and other modifications of industrial softwood kraft lignin by laccase-mediators
inferredcites →https://doi.org/10.3389/fenrg.2014.00012openalex-snapshot
Lignin Biodegradation with Laccase-Mediator Systems
inferredcites →https://doi.org/10.3390/ijms21030966openalex-snapshot
Laccase Properties, Physiological Functions, and Evolution

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

inferred← citeshttps://doi.org/10.2139/ssrn.4569069openalex-extracted
A Functional Screening Pipeline to Uncover Fungal Laccase-Like Multicopper Oxidases that Transform Industrial Lignins
inferred← citeshttps://doi.org/10.1007/s00253-022-11916-zopenalex-snapshot
Enzymatic synthesis of kraft lignin-acrylate copolymers using an alkaline tolerant laccase
inferred← citeshttps://doi.org/10.1007/s12010-026-05784-wopenalex-snapshot
Dye-Decolorizing Peroxidase for Lignin Depolymerization: a Comprehensive Review on Enzyme Structural Characteristics, Reaction-Influencing Factors and Efficiency-Enhancing Strategies
inferred← citeshttps://doi.org/10.1016/bs.mie.2025.01.045openalex-snapshot
Recombinant expression of bacterial lignin-active laccases and peroxidase in Streptomyces lividans
inferred← citeshttps://doi.org/10.1016/bs.mie.2025.01.058openalex-snapshot
Analytical strategies for the investigation of enzymatic and microbial ligninolytic activities
inferred← citeshttps://doi.org/10.1016/j.biortech.2023.130084openalex-snapshot
Functional screening pipeline to uncover laccase-like multicopper oxidase enzymes that transform industrial lignins
inferred← citeshttps://doi.org/10.1016/j.biotechadv.2023.108153openalex-snapshot
Biocatalysis for biorefineries: The case of dye-decolorizing peroxidases
inferred← citeshttps://doi.org/10.1016/j.biotechadv.2025.108647openalex-snapshot
Enzymatic depolymerization of lignin and electrocatalytic hydrodeoxygenation for the production of reduced aromatic compounds: A review and perspective
inferred← citeshttps://doi.org/10.1016/j.tibtech.2022.09.014openalex-snapshot
Creative biological lignin conversion routes toward lignin valorization
inferred← citeshttps://doi.org/10.1021/acsomega.4c05043openalex-snapshot
Dye-Decolorizing Peroxidases Maintain High Stability and Turnover on Kraft Lignin and Lignocellulose Substrates
inferred← citeshttps://doi.org/10.1039/d3se01435eopenalex-snapshot
Perspectives and advances in consolidated bioprocessing strategies for lignin valorization
inferred← citeshttps://doi.org/10.1128/aem.00205-24openalex-snapshot
Characterization of Amycolatopsis 75iv2 dye-decolorizing peroxidase on O -glycosides
inferred← citeshttps://doi.org/10.1186/s12934-023-02075-5openalex-snapshot
Secretory expression of recombinant small laccase genes in Gram-positive bacteria
inferred← citeshttps://doi.org/10.1186/s40643-023-00640-9openalex-snapshot
Laccase-catalyzed lignin depolymerization in deep eutectic solvents: challenges and prospects
inferred← citeshttps://doi.org/10.2174/1389203723666220704090416openalex-snapshot
Comparison of Laccases and Hemeproteins Systems in Bioremediation of Organic Pollutants
inferred← citeshttps://doi.org/10.6084/m9.figshare.22641049openalex-snapshot
Additional file 1 of Secretory expression of recombinant small laccase genes in Gram-positive bacteria
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