ArticlePloS one2016
Characterization of a Highly Thermostable and Organic Solvent-Tolerant Copper-Containing Polyphenol Oxidase with Dye-Decolorizing Ability from Kurthia huakuii LAM0618T.
Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Age-stratified gut microbial changes in diarrheal calves: insights from 16S rRNA sequencing across early development.Frontiers in microbiology · 2025Article
- Purification, characterization and three-dimensional structure prediction of multicopper oxidase Laccases from Trichoderma lixii FLU1 and Talaromyces pinophilus FLU12.Scientific reports · 2024Article
- Effects of Sodium Nitrate and Coated Methionine on Lactation Performance, Rumen Fermentation Characteristics, Amino Acid Metabolism, and Microbial Communities in Lactating Buffaloes.Microorganisms · 2023Article
- Characterization of a Recombinant Laccase B fromMolecules (Basel, Switzerland) · 2022Article
- Functional assignment to hypothetical proteins inBioinformation · 2022Article
- Formation of recombinant bifunctional fusion protein: A newer approach to combine the activities of two enzymes in a single protein.PloS one · 2022Article
- An Engineered Thermostable Laccase with Great Ability to Decolorize and Detoxify Malachite Green.International journal of molecular sciences · 2021Article
- Screening of Novel Laccase Producers-Isolation and Characterization of Cold-Adapted Laccase fromBiomolecules · 2021Article
- Optimisation of the Production and Bleaching Process for a New Laccase from Madurella mycetomatis, Expressed in Pichia pastoris: from Secretion to Yielding Prominent.Molecular biotechnology · 2021Article
- Heterologous Expression of Laccase FromFrontiers in microbiology · 2020Article
- Genome Sequencing Revealed the Biotechnological Potential of an Obligate ThermophileIndian journal of microbiology · 2019Article
- Biodetoxification of Phenolic Inhibitors from Lignocellulose Pretreatment usingMolecules (Basel, Switzerland) · 2018Article
- Characterization of AiiK, an AHL lactonase, from Kurthia huakui LAM0618Scientific reports · 2018Article
- Preparation of Biocolorant and Eco-Dyeing Derived from Polyphenols Based on Laccase-Catalyzed Oxidative Polymerization.Polymers · 2018Article
- Identification of a novel copper-activated and halide-tolerant laccase in Geobacillus thermopakistaniensis.Extremophiles : life under extreme conditions · 2017Article
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Authors and funding
11 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Laccases are green biocatalysts that possess attractive advantages for the treatment of resistant environmental pollutants and dye effluents. A putative laccase-like gene, laclK, encoding a protein of 29.3 kDa and belonging to the Cu-oxidase_4 superfamily, was cloned and overexpressed in Escherichia coli. The purified recombinant protein LaclK (LaclK) was able to oxidize typical laccase substrates such as 2,6-dimethoxyphenol and l-dopamine. The characteristic adsorption maximums of typical laccases at 330 nm and 610 nm were not detected for LaclK. Cu2+ was essential for substrate oxidation, but the ratio of copper atoms/molecule of LaclK was determined to only be 1:1. Notably, the optimal temperature of LaclK was 85°C with 2,6-dimethoxyphenol as substrates, and the half-life approximately 3 days at 80°C. Furthermore, 10% (v/v) organic solvents (methanol, ethanol, isopropyl alcohol, butyl alcohol, Triton x-100 or dimethyl sulfoxide) could promote enzymatic activity. LaclK exhibited wide-spectrum decolorization ability towards triphenylmethane dyes, azo dyes and aromatic dyes, decolorizing 92% and 94% of Victoria Blue B (25 μM) and Ethyl Violet (25 μM), respectively, at a concentration of 60 U/L after 1 h of incubation at 60°C. Overall, we characterized a novel thermostable and organic solvent-tolerant copper-containing polyphenol oxidase possessing dye-decolorizing ability. These unusual properties make LaclK an alternative for industrial applications, particularly processes that require high-temperature conditions.
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