ArticleFolia microbiologica2020
A first report on competitive inhibition of laccase enzyme by lignin degradation intermediates.
Article in Folia microbiologica, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
5 citing papers in PubMed, 10 citations in OpenAlex.
- Production ofMolecules (Basel, Switzerland) · 2025Article
- Fungus-mediated bacterial survival and migration enhance wood lignin degradation.Applied and environmental microbiology · 2025Article
- Biodegradation of screenings from sewage treatment by white rot fungi.Fungal biology and biotechnology · 2025Article
- Isothermal titration calorimetric assessment of lignin conversion by laccases.Biotechnology and bioengineering · 2022Article
- New liquid supports in the development of integrated platforms for the reuse of oxidative enzymes and polydopamine production.Frontiers in bioengineering and biotechnology · 2022Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Laccases have been widely explored for their ligninolytic capability in bioethanol production and bioremediation of industrial effluents. However, low reaction rates have posed a major challenge to commercialization of such processes. This study reports the first evidence of laccase inhibition by two types of lignin degradation intermediates - fungal-solubilized lignin and alkali-treated lignin - thus offering a highly plausible explanation for low reaction rates due to buildup of inhibitors during the actual process. Reversed-phase high-performance liquid chromatography revealed the presence of similar polar compounds in both lignin samples. A detailed kinetic study on laccase, using 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulphonic acid) (ABTS) as the substrate, was used to calculate the Michaelis constant (K
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Registered trials
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