ArticlePloS one2015
Overexpression of a novel thermostable and chloride-tolerant laccase from Thermus thermophilus SG0.5JP17-16 in Pichia pastoris and its application in synthetic dye decolorization.
Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
27 citing papers in PubMed, 72 citations in OpenAlex.
- ESM-Ezy: a deep learning strategy for the mining of novel multicopper oxidases with superior properties.Nature communications · 2025Article
- Structure-Function Relationship of the β-Hairpin ofInternational journal of molecular sciences · 2025Article
- Current Understanding on the Heterogenous Expression of Plastic Depolymerising Enzymes inBioengineering (Basel, Switzerland) · 2025Review
- Leveraging bacterial laccases to facilitate the decomposition of xenobiotic compounds: a review.3 Biotech · 2024Review
- Biochemical characterization of a recombinant laccase from Halalkalibacterium halodurans C-125 and its application in the biotransformation of organic compounds.Biotechnology letters · 2024Article
- A temperature dependent pilin promoter for production of thermostable enzymes in Thermus thermophilus.Microbial cell factories · 2023Article
- Crystal structures of a dodecameric multicopper oxidase from Marinithermus hydrothermalis.Acta crystallographica. Section D, Structural biology · 2021Article
- Novel Cold-Adapted Recombinant Laccase KbLcc1 fromInternational journal of molecular sciences · 2021Article
- Extremophiles, a Nifty Tool to Face Environmental Pollution: From Exploitation of Metabolism to Genome Engineering.International journal of environmental research and public health · 2021Review
- Structural analysis and biochemical properties of laccase enzymes from two Pediococcus species.Microbial biotechnology · 2021Article
- Genome-based engineering of ligninolytic enzymes in fungi.Microbial cell factories · 2021Review
- Fast decolorization of azo dyes in alkaline solutions by a thermostable metal-tolerant bacterial laccase and proposed degradation pathways.Extremophiles : life under extreme conditions · 2020Article
- Hyperstabilization of a thermophile bacterial laccase and its application for industrial dyes degradation.3 Biotech · 2020Article
- Article
- Laccases: structure, function, and potential application in water bioremediation.Microbial cell factories · 2019Review
- Article
- Aptitude of Oxidative Enzymes for Treatment of Wastewater Pollutants: A Laccase Perspective.Molecules (Basel, Switzerland) · 2019Review
- Axial bonds at the T1 Cu site of Thermus thermophilus SG0.5JP17-16 laccase influence enzymatic properties.FEBS open bio · 2019Article
- A thermostable laccase from Thermus sp. 2.9 and its potential for delignification of Eucalyptus biomass.AMB Express · 2019Article
- Microbial diversity of thermophiles with biomass deconstruction potential in a foliage-rich hot spring.MicrobiologyOpen · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Laccases have been used for the decolorization and detoxification of synthetic dyes due to their ability to oxidize a wide variety of dyes with water as the sole byproduct. A putative laccase gene (LacTT) from Thermus thermophilus SG0.5JP17-16 was screened using the genome mining approach, and it was highly expressed in Pichia pastoris, yielding a high laccase activity of 6130 U/L in a 10-L fermentor. The LacTT open reading frame encoded a protein of 466 amino acid residues with four putative Cu-binding regions. The optimal pH of the recombinant LacTT was 4.5, 6.0, 7.5 and 8.0 with 2,2'-azino-bis(3-ethylbenzothazoline-6-sulfonic acid) (ABTS), syringaldazine (SGZ), guaiacol, and 2,6-dimethoxyphenol (2,6-DMP) as the substrate, respectively. The optimal temperature of LacTT was 90°C with guaiacol as the substrate. LacTT was highly stable at pH 4.0-11.0 and thermostable at 40°C-90°C, confirming that it is a pH-stable and thermostable laccase. Furthermore, LacTT also exhibited high tolerance to halides such as NaCl, NaBr and NaF, and decolorized 100%, 94%, 94% and 73% of Congo Red, Reactive Black B and Reactive Black WNN, and Remazol Brilliant Blue R, respectively. Interestingly, addition of high concentration of NaCl increased the RBBR decolorization efficiency of LacTT. These results suggest that LacTT is a good candidate for industrial applications such as dyestuff processing and degradation of dyes in textile wastewaters.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.