ArticleExtremophiles : life under extreme conditions2017
Identification of a novel copper-activated and halide-tolerant laccase in Geobacillus thermopakistaniensis.
Article in Extremophiles : life under extreme conditions, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 26 citations in OpenAlex.
- Biochemical characterization of a recombinant laccase from Halalkalibacterium halodurans C-125 and its application in the biotransformation of organic compounds.Biotechnology letters · 2024Article
- Review
- Thermostable Bacterial Laccase: Catalytic Properties and Its Application in Biotransformation of Emerging Pollutants.ACS omega · 2023Article
- Recombinant expression and characterization of a new laccase, bioinformatically identified, from the Antarctic thermophilic bacterium Geobacillus sp. ID17.Extremophiles : life under extreme conditions · 2023Article
- Structural analysis and biochemical properties of laccase enzymes from two Pediococcus species.Microbial biotechnology · 2021Article
- Hydrophobic and Anti-Fouling Performance of Surface on Parabolic Morphology.International journal of environmental research and public health · 2020Article
- A thermostable laccase from Thermus sp. 2.9 and its potential for delignification of Eucalyptus biomass.AMB Express · 2019Article
- Bacterial laccases: promising biological green tools for industrial applications.Cellular and molecular life sciences : CMLS · 2018Review
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Authors and funding
7 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Genome search of Geobacillus thermopakistaniensis, formerly Geobacillus sp. SBS-4S, revealed the presence of an open reading frame (ESU71923) annotated as laccase. However, the gene product did not display any laccase-like activity against the substrates examined. The laccase activity was, therefore, purified from G. thermopakistaniensis cells and N-terminal amino acid residues of the enzyme were determined. These residues matched the N-terminal sequence of an open reading frame annotated as a copper oxidase (ESU72270). In order to characterize the enzyme, recombinant ESU72270 was prepared in Escherichia coli. The recombinant protein was found to exhibit a negligible amount of laccase activity when produced in the absence of copper in the growth medium. However, the recombinant protein exhibited significantly high laccase activity when produced in the presence of copper. The recombinant enzyme showed highest activity at 60 °C and a pH of 7-7.5. The purified enzyme was highly tolerant to various halides and organic solvents, thus having a potential for various industrial applications. To the best of our knowledge, this is the first characterization of a laccase from genus Geobacillus which identifies a gene responsible for functional laccase in this genus.
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