Evidence map›Paper›PMID 25036001›Full record

ArticlePloS one2014

Structure-based rational design to enhance the solubility and thermostability of a bacterial laccase Lac15.

Zemin Fang, Peng Zhou, Fei Chang, Qiang Yin, Wei Fang, Jing Yuan, Xuecheng Zhang, Yazhong Xiao

Open access · goldAbstract readComparative Study
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
5.1field-weighted citation impact, top 6% 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

7 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
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  5. Review
  6. Review
  7. How to enjoy laccases.Cellular and molecular life sciences : CMLS · 2015
    Review
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.

Zemin FangSchool of Life Sciences, Anhui University, Hefei, Anhui, China; Anhui Provincial Engineering Technology Research Center of Microorganisms and Biocatalysis, Hefei, Anhui, China.
Peng ZhouSchool of Life Sciences, Anhui University, Hefei, Anhui, China; Anhui Provincial Engineering Technology Research Center of Microorganisms and Biocatalysis, Hefei, Anhui, China.
Fei ChangSchool of Life Sciences, Anhui University, Hefei, Anhui, China; Anhui Provincial Engineering Technology Research Center of Microorganisms and Biocatalysis, Hefei, Anhui, China.
Qiang YinSchool of Life Sciences, Anhui University, Hefei, Anhui, China; Anhui Provincial Engineering Technology Research Center of Microorganisms and Biocatalysis, Hefei, Anhui, China.
Wei FangSchool of Life Sciences, Anhui University, Hefei, Anhui, China; Anhui Provincial Engineering Technology Research Center of Microorganisms and Biocatalysis, Hefei, Anhui, China.
Jing YuanSchool of Life Sciences, Anhui University, Hefei, Anhui, China; Anhui Provincial Engineering Technology Research Center of Microorganisms and Biocatalysis, Hefei, Anhui, China.
Xuecheng ZhangSchool of Life Sciences, Anhui University, Hefei, Anhui, China; Anhui Provincial Engineering Technology Research Center of Microorganisms and Biocatalysis, Hefei, Anhui, China.
Yazhong XiaoSchool of Life Sciences, Anhui University, Hefei, Anhui, China; Anhui Provincial Engineering Technology Research Center of Microorganisms and Biocatalysis, Hefei, Anhui, China.
Anhui University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Bacterial laccases are ideal alternatives of fungal laccases for specific industrial applications due to specific characteristics such as alkalescence dependence and high chloride tolerance. However, some bacterial laccases presented as inclusion bodies when expressing in Escherichia coli and showed thermal instability. In this study, rational design was employed to enhance the solubility and the thermostablity of the bacterial laccase Lac15-His6 based on the crystal structure obtained previously. After deletion of His-tag and residues323-332, the obtained Lac15D was completely expressed in soluble form even at a higher temperature of 28°C, compared to only 50% of Lac15-His6 expressed solubly at 16°C. It showed a two-time higher activity at temperatures lower than 35°C and a half-life increasing from 72 min to 150 min at 45°C. When used in chromogenic reactions, Lac15D showed constant activity toward dye precursors and their combinations under alkaline conditions, demonstrating its application potential in hair coloring biotechnology.

Indexed as

Bacterial ProteinsCatalysisChromogenic CompoundsCrystallography, X-RayEscherichia coliHair DyesHot TemperatureHydrogen-Ion ConcentrationLaccaseModels, MolecularProtein ConformationProtein EngineeringProtein StabilityRecombinant Fusion ProteinsSolubilityStructure-Activity RelationshipBacterial ProteinsChromogenic CompoundsHair DyesLaccaseRecombinant Fusion Proteins

Identifiers

PMID25036001
PMCPMC4103834
OpenAlexW1985410247

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.