ArticleMolecules (Basel, Switzerland)2016
Biochemical Characteristics of Three Laccase Isoforms from the Basidiomycete Pleurotus nebrodensis.
Article in Molecules (Basel, Switzerland), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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13 citing papers in PubMed, 36 citations in OpenAlex.
- A novel laccase from Trametes polyzona with high performance in the decolorization of textile dyes.AMB Express · 2024Article
- Biochemical Characterization of Laccase from Spirulina CPCC-695 and Their Role in Estrone Degradation.The protein journal · 2024Article
- Expression and Characterization of Laccase Lac1 from Coriolopsis trogii Strain Mafic-2001 in Pichia pastoris and Its Degradation of Lignin.Applied biochemistry and biotechnology · 2023Article
- From pomiculture waste to biotechnological raw material: efficient transformation using ligninosomes and cellulosomes from Pleurotus spp.Bioresources and bioprocessing · 2022Article
- Characterization of a Novel Laccase LAC-Yang1 from White-Rot FungusMolecules (Basel, Switzerland) · 2021Article
- Assessing the Biodegradation of Vulcanised Rubber Particles by Fungi Using Genetic, Molecular and Surface Analysis.Frontiers in bioengineering and biotechnology · 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
- Multicopper oxidase (MCO) laccase from3 Biotech · 2020Article
- Estrone degrading enzymes ofBiotechnology reports (Amsterdam, Netherlands) · 2020Article
- Laccase Properties, Physiological Functions, and Evolution.International journal of molecular sciences · 2020Review
- β-Carotene from Yeasts Enhances Laccase Production ofFrontiers in microbiology · 2017Article
- Diversity of Ligninolytic Enzymes and Their Genes in Strains of the GenusFrontiers in microbiology · 2017Article
- Degradation of dyes using crude extract and a thermostable and pH-stable laccase isolated from Pleurotus nebrodensis.Bioscience reports · 2016Article
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6 authors at 4 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
The characterization of three laccase isoforms from Pleurotus nebrodensis is described. Isoenzymes Lac1, Lac2 and Lac3 were purified to homogeneity using ion exchange chromatography on DEAE-cellulose, CM-cellulose and Q-Sepharose and a gel filtration step on Superdex 75. The molecular weights of the purified laccases were estimated to be 68, 64 and 51 kDa, respectively. The isoenzymes demonstrated the same optimum pH at 3.0 but slightly different temperature optima: 50-60 °C for Lac1 and Lac3 and 60 °C for Lac2. Lac2 was always more stable than the other two isoforms and exposure to 50 °C for 120 min caused 30% loss in activity. Lac2 was relatively less stable than the other two isoforms when exposed to the pH range of 3.0-8.0 for 24 h, but inactivation only occurred initially, with around 70% residual activity being maintained during the whole process. Oxidative ability towards aromatic compounds varied substantially among the isoforms and each of them displayed preference toward some substrates. Kinetic constants (Km, Kcat) were determined by using a 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) diammonium salt (ABTS) assay, with Lac3 showing the best affinity and Lac2 displaying the highest catalytic efficiency. Amino acid sequences from peptides derived from digestion of isoenzymes showed great consistency with laccases in the databases.
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