ArticleAMB Express2019
A thermostable laccase from Thermus sp. 2.9 and its potential for delignification of Eucalyptus biomass.
Article in AMB Express, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 35 citations in OpenAlex.
- Bacterial laccases for green remediation of contaminants of emerging concern: from molecular cloning to metagenomic and computational insights.Biodegradation · 2026Review
- Laccase-catalyzed conversion of residual agricultural biomass to lignin-derived aromatic compounds.World journal of microbiology & biotechnology · 2025Article
- Structure-Function Relationship of the β-Hairpin ofInternational journal of molecular sciences · 2025Article
- Characterization of a Novel One-Domain Halotolerant Laccase from Parageobacillus thermoglucosidasius and Its Application in Dye Decolorization.Applied biochemistry and biotechnology · 2023Article
- Laccases as green and versatile biocatalysts: from lab to enzyme market-an overview.Bioresources and bioprocessing · 2021Review
- Laccase-mediated delignification and detoxification of lignocellulosic biomass: removing obstacles in energy generation.Environmental science and pollution research international · 2021Review
- Extremophiles, a Nifty Tool to Face Environmental Pollution: From Exploitation of Metabolism to Genome Engineering.International journal of environmental research and public health · 2021Review
- Extremophilic Oxidoreductases for the Industry: Five Successful Examples With Promising Projections.Frontiers in bioengineering and biotechnology · 2021Review
- Fast decolorization of azo dyes in alkaline solutions by a thermostable metal-tolerant bacterial laccase and proposed degradation pathways.Extremophiles : life under extreme conditions · 2020Article
- Degradation of Aflatoxin BToxins · 2019Article
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Authors and funding
10 authors at 5 institutions in 2 countries.
Funding
Abstract
Laccases are multicopper oxidases that are being studied for their potential application in pretreatment strategies of lignocellulosic feedstocks for bioethanol production. Here, we report the expression and characterization of a predicted laccase (LAC_2.9) from the thermophilic bacterial strain Thermus sp. 2.9 and investigate its capacity to delignify lignocellulosic biomass. The purified enzyme displayed a blue color typical of laccases, showed strict copper dependence and retained 80% of its activity after 16 h at 70 °C. At 60 °C, the enzyme oxidized 2,2'-azino-di-(3-ethylbenzthiazoline sulfonate) (ABTS) and 2,6-dimethoxyphenol (DMP) at optimal pH of 5 and 6, respectively. LAC_2.9 had higher substrate specificity (k
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.