ArticleApplied and environmental microbiology2010
LccA, an archaeal laccase secreted as a highly stable glycoprotein into the extracellular medium by Haloferax volcanii.
Article in Applied and environmental microbiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
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Who cites it
48 citing papers in PubMed, 127 citations in OpenAlex.
- Mechanistic insights into redox activity and catalytic determinants of the haloarchaeal flavin-dependent oxidoreductasebioRxiv : the preprint server for biology · 2026Article
- Recent Advances in Laccase Production: Challenges and Future Perspectives.Journal of microbiology and biotechnology · 2025Review
- Biochemical properties of glycerol kinase from the hypersaline-adapted archaeonApplied and environmental microbiology · 2025Article
- A colorful new reporter system to evaluate gene expression in the archaeon Haloferax volcanii.Extremophiles : life under extreme conditions · 2025Article
- Leveraging bacterial laccases to facilitate the decomposition of xenobiotic compounds: a review.3 Biotech · 2024Review
- Extremozyme-Based Biosensors for Environmental Pollution Monitoring: Recent Developments.Biosensors · 2024Review
- Optimization of laccase from Stenotrophomonas maltophilia E1 by submerge fermentation using coconut husk with its detoxification and biodecolorization ability of synthetic dyes.Bioresources and bioprocessing · 2023Article
- Secretory expression of recombinant small laccase genes in Gram-positive bacteria.Microbial cell factories · 2023Article
- Bioactive molecules from haloarchaea: Scope and prospects for industrial and therapeutic applications.Frontiers in microbiology · 2023Review
- Elimination and detoxification of phenanthrene assisted by a laccase from halophileJournal of environmental health science & engineering · 2022Article
- Eminent Industrial and Biotechnological Applications of Laccases from Bacterial Source: a Current Overview.Applied biochemistry and biotechnology · 2022Review
- Modifying Surface Charges of a Thermophilic Laccase Toward Improving Activity and Stability in Ionic Liquid.Frontiers in bioengineering and biotechnology · 2022Article
- Extremophiles, a Nifty Tool to Face Environmental Pollution: From Exploitation of Metabolism to Genome Engineering.International journal of environmental research and public health · 2021Review
- Halophilic archaea and their potential to generate renewable fuels and chemicals.Biotechnology and bioengineering · 2021Review
- Genome-based engineering of ligninolytic enzymes in fungi.Microbial cell factories · 2021Review
- High-level synthesis and secretion of laccase, a metalloenzyme biocatalyst, by the halophilic archaeon Haloferax volcanii.Methods in enzymology · 2021Article
- Extremophilic Oxidoreductases for the Industry: Five Successful Examples With Promising Projections.Frontiers in bioengineering and biotechnology · 2021Review
- Phenoloxidases in Plants-How Structural Diversity Enables Functional Specificity.Frontiers in plant science · 2021Review
- Haloferax volcanii for biotechnology applications: challenges, current state and perspectives.Applied microbiology and biotechnology · 2020Review
- Laccase Properties, Physiological Functions, and Evolution.International journal of molecular sciences · 2020Review
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4 authors at 1 institution in 1 country.
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Abstract
Laccases couple the oxidation of phenolic compounds to the reduction of molecular oxygen and thus span a wide variety of applications. While laccases of eukaryotes and bacteria are well characterized, these enzymes have not been described in archaea. Here, we report the purification and characterization of a laccase (LccA) from the halophilic archaeon Haloferax volcanii. LccA was secreted at high levels into the culture supernatant of a recombinant H. volcanii strain, with peak activity (170 +/- 10 mU.ml(-)(1)) at stationary phase (72 to 80 h). LccA was purified 13-fold to an overall yield of 72% and a specific activity of 29.4 U.mg(-)(1) with an absorbance spectrum typical of blue multicopper oxidases. The mature LccA was processed to expose an N-terminal Ala after the removal of 31 amino acid residues and was glycosylated to 6.9% carbohydrate content. Purified LccA oxidized a variety of organic substrates, including bilirubin, syringaldazine (SGZ), 2,2,-azino-bis-(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS), and dimethoxyphenol (DMP), with DMP oxidation requiring the addition of CuSO(4). Optimal oxidation of ABTS and SGZ was at 45 degrees C and pH 6 and pH 8.4, respectively. The apparent K(m) values for SGZ, bilirubin, and ABTS were 35, 236, and 670 muM, with corresponding k(cat) values of 22, 29, and 10 s(-)(1), respectively. The purified LccA was tolerant of high salt, mixed organosolvents, and high temperatures, with a half-life of inactivation at 50 degrees C of 31.5 h.
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