ArticleMicrobial cell factories2012
Biocatalytic potential of laccase-like multicopper oxidases from Aspergillus niger.
Article in Microbial cell factories, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 34 citations in OpenAlex.
- Degradation of tetracycline, oxytetracycline & ampicillin by purified multiple copper oxidase like laccase from Stentrophomonas sp. YBX1.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2024Article
- Unusual Oligomeric Laccase-like Oxidases from AscomyceteMicroorganisms · 2023Article
- Article
- Discovery of two novel laccase-like multicopper oxidases from Pleurotus citrinopileatus and their application in phenolic oligomer synthesis.Biotechnology for biofuels · 2021Article
- Molecular cloning, expression and characterization of poxa1b gene from Pleurotus ostreatus.Molecular biology reports · 2019Article
- Exploring the genomic diversity of black yeasts and relatives (Studies in mycology · 2017Article
- A Thermostable Bilirubin-Oxidizing Enzyme from Activated Sludge Isolated by a Metagenomic Approach.Microbes and environments · 2016Article
- Article
- Laccase-catalyzed decolorization of malachite green: performance optimization and degradation mechanism.PloS one · 2015Article
- Functional characterization of a yellow laccase from Leucoagaricus gongylophorus.SpringerPlus · 2015Article
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3 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
backgroundLaccase-like multicopper oxidases have been reported in several Aspergillus species but they remain uncharacterized. The biocatalytic potential of the Aspergillus niger fungal pigment multicopper oxidases McoA and McoB and ascomycete laccase McoG was investigated.
resultsThe laccase-like multicopper oxidases McoA, McoB and McoG from the commonly used cell factory Aspergillus niger were homologously expressed, purified and analyzed for their biocatalytic potential. All three recombinant enzymes were monomers with apparent molecular masses ranging from 80 to 110 kDa. McoA and McoG resulted to be blue, whereas McoB was yellow. The newly obtained oxidases displayed strongly different activities towards aromatic compounds and synthetic dyes. McoB exhibited high catalytic efficiency with N,N-dimethyl-p-phenylenediamine (DMPPDA) and 2,2-azino-di(3-ethylbenzthiazoline) sulfonic acid (ABTS), and appeared to be a promising biocatalyst. Besides oxidizing a variety of phenolic compounds, McoB catalyzed successfully the decolorization and detoxification of the widely used textile dye malachite green.
conclusionsThe A. niger McoA, McoB, and McoG enzymes showed clearly different catalytic properties. Yellow McoB showed broad substrate specificity, catalyzing the oxidation of several phenolic compounds commonly present in different industrial effluents. It also harbored high decolorization and detoxification activity with the synthetic dye malachite green, showing to have an interesting potential as a new industrial biocatalyst.
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