ArticleScientific reports2021
A novel Bacillus ligniniphilus catechol 2,3-dioxygenase shows unique substrate preference and metal requirement.
Article in Scientific reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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9 citing papers in PubMed.
- Mimicking Extradiol Dioxygenase Reactivity on Iridium.Journal of the American Chemical Society · 2026Article
- Lignocellulose degradation characteristics and mechanisms of raw and NaOH-pretreated wheat straw by Irpex lacteus QJ: multi-omics analysis.Bioresources and bioprocessing · 2026Article
- Genome-based analysis of Bacillus velezensis Bm3 isolated from a vulnerable dioxin-contaminated site in central Syria reveals mechanisms of dioxin degradation.Scientific reports · 2026Article
- Overproduction of glycolipopeptide bio-amphiphile by Pseudomonas aeruginosa mutant generated through three-tier cocktail random mutagenesis.BMC microbiology · 2026Article
- Uncovering the lignin-degrading potential of Serratia quinivorans AORB19: insights from genomic analyses and alkaline lignin degradation.BMC microbiology · 2024Article
- Assay Development for Metal-Dependent Enzymes-Influence of Reaction Buffers on Activities and Kinetic Characteristics.ACS omega · 2023Article
- A high throughput screening process and quick isolation of novel lignin-degrading microbes from large number of natural biomasses.Biotechnology reports (Amsterdam, Netherlands) · 2023Article
- Reduction of phenolics in faba bean meal using recombinantly produced and purifiedBioresources and bioprocessing · 2023Article
- mibPOPdb: An online database for microbial biodegradation of persistent organic pollutants.iMeta · 2022Article
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7 authors.
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Abstract
Identification of novel enzymes from lignin degrading microorganisms will help to develop biotechnologies for biomass valorization and aromatic hydrocarbons degradation. Bacillus ligniniphilus L1 grows with alkaline lignin as the single carbon source and is a great candidate for ligninolytic enzyme identification. The first dioxygenase from strain L1 was heterologously expressed, purified, and characterized with an optimal temperature and pH of 32.5 °C and 7.4, respectively. It showed the highest activity with 3-ethylcatechol and significant activities with other substrates in the decreasing order of 3-ethylcatechol > 3-methylcatechol > 3-isopropyl catechol > 2, 3-dihydroxybiphenyl > 4-methylcatechol > catechol. It did not show activities against other tested substrates with similar structures. Most reported catechol 2,3-dioxygenases (C23Os) are Fe
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