Evidence map›Paper›PMID 26867601›Full record

ArticleWorld journal of microbiology & biotechnology2016

Heterologous expression and characterisation of a laccase from Colletotrichum lagenarium and decolourisation of different synthetic dyes.

Bo Wang, Ying Yan, Yongsheng Tian, Wei Zhao, Zhengjun Li, Jianjie Gao, Rihe Peng, Quanhong Yao

Abstract read
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In one paragraph

Article in World journal of microbiology & biotechnology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
11.0field-weighted citation impact, top 2% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

11 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
  2. Review
  3. ARTP Mutagenesis ofJournal of microbiology and biotechnology · 2025
    Article
  4. Article
  5. Article
  6. Novel Cold-Adapted Recombinant Laccase KbLcc1 fromInternational journal of molecular sciences · 2021
    Article
  7. Review
  8. Article
  9. Article
  10. Review
  11. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 1 institution in 1 country.

Bo WangBiotechnological Research Institute, Shanghai Academy of Agricultural Sciences, Shanghai, 201106, China. wangbosaas@163.com.
Ying YanCrop Breeding and Cultivation Research Institute, Shanghai Academy of Agricultural Sciences, Shanghai, 201403, China.
Yongsheng TianBiotechnological Research Institute, Shanghai Academy of Agricultural Sciences, Shanghai, 201106, China.
Wei ZhaoBiotechnological Research Institute, Shanghai Academy of Agricultural Sciences, Shanghai, 201106, China.
Zhengjun LiBiotechnological Research Institute, Shanghai Academy of Agricultural Sciences, Shanghai, 201106, China.
Jianjie GaoBiotechnological Research Institute, Shanghai Academy of Agricultural Sciences, Shanghai, 201106, China.
Rihe PengBiotechnological Research Institute, Shanghai Academy of Agricultural Sciences, Shanghai, 201106, China.
Quanhong YaoBiotechnological Research Institute, Shanghai Academy of Agricultural Sciences, Shanghai, 201106, China. yao.quanhong65@yahoo.com.
Shanghai Academy of Agricultural Sciences · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Laccases have received considerable attention in recent decades because of their ability to oxidise a large spectrum of phenolic and non-phenolic organic substrates and highly recalcitrant environmental pollutants. In this research, a laccase gene from Colletotrichum lagenarium was chemically synthesised using yeast bias codons and expressed in Pichia pastoris. The molecular mass of the recombinant laccase was estimated to be 64.6 kDa by SDS-PAGE, and the enzyme exhibited maximum activity at pH 3.6-4.0 but more stability in buffer with higher pH (>pH 3.6). The optimal reaction temperature of the enzyme was 40 °C, beyond which stability significantly decreased. By using 2,2'-azino-bis-(3-ethylbenzothiazoline)-6-sulphonate (ABTS) as a substrate, K m and V max values of 0.34 mM and 7.11 mM min(-1) mg(-1), respectively, were obtained. Using ABTS as a mediator, the laccase could oxidise hydroquinone to p-benzoquinone and decolourise the synthetic dyes malachite green, crystal violet and orange G. These results indicated that the laccase could be used to treat industrial effluents containing artificial dyes.

Indexed as

Gene ExpressionBenzothiazolesBiotransformationColletotrichumColoring AgentsElectrophoresis, Polyacrylamide GelEnzyme StabilityHydrogen-Ion ConcentrationKineticsLaccaseMolecular WeightPichiaRecombinant ProteinsSaccharomycetalesSubstrate SpecificitySulfonic Acids2,2'-azino-di-(3-ethylbenzothiazoline)-6-sulfonic acidBenzothiazolesColoring AgentsLaccaseRecombinant ProteinsSulfonic AcidsCharacterisationColletotrichum lagenariumLaccasePichia pastorisSynthetic dyes

Identifiers

PMID26867601
OpenAlexW2464646983

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.