ArticleFolia microbiologica2024
Production of laccase enzyme from Curvularia lunata MY3: purification and characterization.
Article in Folia microbiologica, 2024. 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, 14 citations in OpenAlex.
- Characterization and application potential of a robust recombinant laccase rTpLcc3 from Trametes polyzona for textile dye decolorization.Scientific reports · 2026Article
- Purification and characterization of the laccase produced by the Lysinibacillus boronitolerans and its role in the decolourization of synthetic dyes.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2026Article
- A review of the current anti-New microbes and new infections · 2026Review
- Article
- Purification and biochemical characterization of laccase from3 Biotech · 2025Article
- Article
- Microbiological Aspects and Enzymatic Characterization ofJournal of fungi (Basel, Switzerland) · 2024Article
- Optimization, purification and characterization of laccase from a new endophytic Trichoderma harzianum AUMC14897 isolated from Opuntia ficus-indica and its applications in dye decolorization and wastewater treatment.Microbial cell factories · 2024Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Laccase-producing fungus (MY3) was successfully isolated from soil samples collected from Mansoura Governorate, Egypt. This fungal isolate has shown a high laccase production level over other isolated fungi. The identity of this isolate was determined by the molecular technique 18SrRNA as Curvularia lunata MY3. The enzyme purification was performed using ammonium sulfate precipitation followed by Sephacryl S-200 and DEAE-Sepharose column chromatography. The denatured enzyme using SDS-PAGE had a molar mass of 65 kDa. The purified laccase had an optimum temperature at 40 °C for enzyme activity with 57.3 kJ/mol activation energy for 2,2'-azino-bis-3-ethylbenzothiazoline-6-sulfonic acid (ABTS) oxidation. The enzyme had an optimum pH of 5.0, and it has shown a high stability at the acidic range (4.5 to 5.5). Mn
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