ArticleMicrobial cell factories2023
Purification and biochemical characterization of two laccase isoenzymes isolated from Trichoderma harzianum S7113 and its application for bisphenol A degradation.
Article in Microbial cell factories, 2023. 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, 58 citations in OpenAlex.
- Laccase immobilization on a natural lignocellulosic biomass support: optimization, characterization, and bisphenol A degradation.3 Biotech · 2026Article
- Eco-friendly azo dye removal via a robust laccase from Acinetobacter baumannii KMSP005: a thermo-alkaliphilic biocatalytic approach.Biotechnology letters · 2026Article
- Boosting laccase production by Penicillium commune s6 via solid-state fermentation on phenolic agri-wastes: statistical enhancement and bioremediation application in dye decolorization.BMC biotechnology · 2026Article
- Development of SpyTag/SpyCatcher-driven thermostable cyclic laccase and its application in lignin and dye degradation and polymerization of phenolic compounds.Science China. Life sciences · 2026Article
- Simultaneous degradation of aflatoxin BFrontiers in nutrition · 2026Article
- Purification and biochemical characterization of laccase from3 Biotech · 2025Article
- Article
- Kinetic studies on optimized extracellular laccase from Trichoderma harzianum PP389612 and its capabilities for azo dye removal.Microbial cell factories · 2024Article
- Improvement of Laccase Production byJournal of fungi (Basel, Switzerland) · 2023Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
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Abstract
Two laccase isoenzymes (LacA and LacB) were isolated from a novel Trichoderma harzianum S7113 isolate employing ammonium sulfate precipitation, Sephadex G100, and DEAE Sepharose ion exchange chromatography. The molecular weights of the purified LacA and LacB laccases were estimated to be 63 and 48 kDa, respectively. The two isoenzymes had their optimum activities at the same temperature (50 °C), but at slightly different pH values (pH 3.0 for LacA and pH 2.5 for LacB). LacA and LacB had the same thermal stability at 40 °C and pH stability at pH 9.0. The two isoenzymes also showed a high level of specific activity toward ABTS, where the K
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