Evidence map›Paper›PMID 34353307›Full record

ArticleBMC biotechnology2021

The study of laccase immobilization optimization and stability improvement on CTAB-KOH modified biochar.

Zhaobo Wang, Dajun Ren, Shan Jiang, Hongyan Yu, Yaohui Cheng, Shuqin Zhang, Xiaoqing Zhang, Wangsheng Chen

Open access · goldAbstract read
In one paragraph

Article in BMC biotechnology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
6.9field-weighted citation impact, top 4% 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

14 citing papers in PubMed, 60 citations in OpenAlex.

  1. Article
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  4. Chemical Modification ofInternational journal of molecular sciences · 2025
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  8. Construction and utilization of FeComputational and structural biotechnology journal · 2025
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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.

Zhaobo WangCollege of Resource and Environmental Engineering, Wuhan University of Science and Technology, Wuhan, 430081, China.
Dajun RenCollege of Resource and Environmental Engineering, Wuhan University of Science and Technology, Wuhan, 430081, China. dj_ren@163.com.
Shan JiangCollege of Resource and Environmental Engineering, Wuhan University of Science and Technology, Wuhan, 430081, China.
Hongyan YuCollege of Resource and Environmental Engineering, Wuhan University of Science and Technology, Wuhan, 430081, China.
Yaohui ChengCollege of Resource and Environmental Engineering, Wuhan University of Science and Technology, Wuhan, 430081, China.
Shuqin ZhangCollege of Resource and Environmental Engineering, Wuhan University of Science and Technology, Wuhan, 430081, China.
Xiaoqing ZhangCollege of Resource and Environmental Engineering, Wuhan University of Science and Technology, Wuhan, 430081, China.
Wangsheng ChenCollege of Resource and Environmental Engineering, Wuhan University of Science and Technology, Wuhan, 430081, China.
Wuhan University of Science and Technology · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundAlthough laccase has a good catalytic oxidation ability, free laccase shows a poor stability. Enzyme immobilization is a common method to improve enzyme stability and endow the enzyme with reusability. Adsorption is the simplest and common method. Modified biochar has attracted great attention due to its excellent performance.

resultsIn this paper, cetyltrimethylammonium bromide (CTAB)-KOH modified biochar (CKMB) was used to immobilize laccase by adsorption method (laccase@CKMB). Based on the results of the single-factor experiments, the optimal loading conditions of laccase@CKMB were studied with the assistance of Design-Expert 12 and response surface methods. The predicted optimal experimental conditions were laccase dosage 1.78 mg/mL, pH 3.1 and 312 K. Under these conditions, the activity recovery of laccase@CKMB was the highest, reaching 61.78%. Then, the CKMB and laccase@CKMB were characterized by TGA, FT-IR, XRD, BET and SEM, and the results showed that laccase could be well immobilized on CKMB, the maximum enzyme loading could reach 57.5 mg/g. Compared to free laccase, the storage and pH stability of laccase@CKMB was improved greatly. The laccase@CKMB retained about 40% of relative activity (4 °C, 30 days) and more than 50% of relative activity at pH 2.0-6.0. In addition, the laccase@CKMB indicated the reusability up to 6 reaction cycles while retaining 45.1% of relative activity. Moreover, the thermal deactivation kinetic studies of laccase@CKMB showed a lower k value (0.00275 min

conclusionsWe explored scientific and reasonable immobilization conditions of laccase@CKMB, and the laccase@CKMB possessed relatively better stabilities, which gave the immobilization of laccase on this cheap and easily available carrier material the possibility of industrial applications.

Indexed as

AdsorptionCetrimoniumCharcoalEnzymes, ImmobilizedEnzyme StabilityFungal ProteinsHydrogen-Ion ConcentrationHydroxidesKineticsLaccasePolyporaceaePotassium CompoundsTemperaturebiocharCetrimoniumCharcoalEnzymes, ImmobilizedFungal ProteinsHydroxidesLaccasePotassium Compoundspotassium hydroxideImmobilization optimizationLaccaseModified biocharStability improvement

Identifiers

PMID34353307
PMCPMC8343897
OpenAlexW3121325131

What OpenQuestion holds

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LicenceCC BY
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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.