ArticlePloS one2014
Characterization of an alkali- and halide-resistant laccase expressed in E. coli: CotA from Bacillus clausii.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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35 citing papers in PubMed, 116 citations in OpenAlex.
- Mitigating alkaline instability induced by tyrosine-tyrosine repulsion in an FcγRIIIa-binding protein through phenylalanine substitution.Journal of biochemistry · 2026Article
- Catalytically active inclusion bodies of Bacillus clausii laccase protein recombinantly produced in E. coli for dye decolorization.Microbial cell factories · 2026Article
- Recent Advances in Laccase Production: Challenges and Future Perspectives.Journal of microbiology and biotechnology · 2025Review
- Engineering the Bacterial Laccase CotA for Functional Expression and Dye Decolorization Through Site-Directed Mutagenesis.Biology · 2025Article
- Enhanced discovery of bacterial laccase-like multicopper oxidase through computer simulation and metagenomic analysis of industrial wastewater.FEBS open bio · 2025Article
- Biochemical characterization of a recombinant laccase from Halalkalibacterium halodurans C-125 and its application in the biotransformation of organic compounds.Biotechnology letters · 2024Article
- Review
- Research of Multicopper Oxidase and Its Degradation of Histamine inMicroorganisms · 2023Article
- Heterologous expression, purification, and characterization of thermo- and alkali-tolerant laccase-like multicopper oxidase from Bacillus mojavensis TH309 and determination of its antibiotic removal potential.Archives of microbiology · 2023Article
- Isolation and Characterization of a Novel Laccase-Producing Bacteria Bhargavaea beijingensis from Paper and Pulp Effluent-Treated Soil Using In Silico Approaches.Current microbiology · 2023Article
- Improvement of thermoalkaliphilic laccase (CtLac) by a directed evolution and application to lignin degradation.Applied microbiology and biotechnology · 2023Article
- A fast, sensitive and fluorescent LPMO activity assay.Frontiers in microbiology · 2023Article
- Current Progress and Future Perspectives on the Use of Bacillus clausiiMicroorganisms · 2022Review
- Biochemical and Structural Properties of a High-Temperature-Active Laccase fromFoods (Basel, Switzerland) · 2022Article
- Broad thermal spectrum metagenomic laccase with action for dye decolorization and fentin hydroxide treatment.AMB Express · 2022Article
- MPEPE, a predictive approach to improve protein expression inComputational and structural biotechnology journal · 2022Article
- Use of Copper as a Trigger for the in Vivo Activity of E. coli Laccase CueO: A Simple Tool for Biosynthetic Purposes.Chembiochem : a European journal of chemical biology · 2021Article
- Colorimetric LPMO assay with direct implication for cellulolytic activity.Biotechnology for biofuels · 2021Article
- Laccase isoform diversity on basal medium in Cyathus bulleri and role in decolorization/detoxification of textile dyes and effluent.World journal of microbiology & biotechnology · 2020Article
- Article
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3 authors at 1 institution in 1 country.
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Abstract
The limitations of fungal laccases at higher pH and salt concentrations have intensified the search for new extremophilic bacterial laccases. We report the cloning, expression, and characterization of the bacterial cotA from Bacillus clausii, a supposed alkalophilic ortholog of cotA from B. subtilis. Both laccases were expressed in E. coli strain BL21(DE3) and characterized fully in parallel for strict benchmarking. We report activity on ABTS, SGZ, DMP, caffeic acid, promazine, phenyl hydrazine, tannic acid, and bilirubin at variable pH. Whereas ABTS, promazine, and phenyl hydrazine activities vs. pH were similar, the activity of B. clausii cotA was shifted upwards by ~0.5-2 pH units for the simple phenolic substrates DMP, SGZ, and caffeic acid. This shift is not due to substrate affinity (K(M)) but to pH dependence of catalytic turnover: The k(cat) of B. clausii cotA was 1 s⁻¹ at pH 6 and 5 s⁻¹ at pH 8 in contrast to 6 s⁻¹ at pH 6 and 2 s⁻¹ at pH 8 for of B. subtilis cotA. Overall, k(cat)/K(M) was 10-fold higher for B. subtilis cotA at pH(opt). While both proteins were heat activated, activation increased with pH and was larger in cotA from B. clausii. NaCl inhibited activity at acidic pH, but not up to 500-700 mM NaCl in alkaline pH, a further advantage of the alkali regime in laccase applications. The B. clausii cotA had ~20 minutes half-life at 80°C, less than the ~50 minutes at 80°C for cotA from B. subtilis. While cotA from B. subtilis had optimal stability at pH~8, the cotA from B. clausii displayed higher combined salt- and alkali-resistance. This resistance is possibly caused by two substitutions (S427Q and V110E) that could repel anions to reduce anion-copper interactions at the expense of catalytic proficiency, a trade-off of potential relevance to laccase optimization.
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