Evidence map›Paper›PMID 38265740›Full record

ArticleMolecular biotechnology2024

Improved Expression of a Thermostable GH18 Bacterial Chitinase in Two Different Escherichia coli Strains and Its Potential Use in Plant Protection and Biocontrol of Phytopathogenic Fungi.

Aymen Ezzine, Safa Ben Hadj Mohamed, Sofiane Bezzine, Yosra Aoudi, Mohamed Rabeh Hajlaoui, Laura Baciou, Issam Smaali

Abstract read
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Article in Molecular biotechnology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
–field-weighted citation impact
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

5 citing papers in PubMed.

  1. Article
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  5. Recovery of terbium byFrontiers in microbiology · 2024
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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

7 authors.

Aymen EzzineLaboratory of Protein Engineering and Bioactive Molecules (LIP-MB), LR11ES24, National Institute of Applied Sciences and Technology, University of Carthage, 1080, Tunis Cedex, Tunisia. e.aymen@yahoo.fr.ORCID http://orcid.org/0000-0003-2074-6988
Safa Ben Hadj MohamedLaboratory of Protein Engineering and Bioactive Molecules (LIP-MB), LR11ES24, National Institute of Applied Sciences and Technology, University of Carthage, 1080, Tunis Cedex, Tunisia.
Sofiane BezzineLaboratory of Protein Engineering and Bioactive Molecules (LIP-MB), LR11ES24, National Institute of Applied Sciences and Technology, University of Carthage, 1080, Tunis Cedex, Tunisia.
Yosra AoudiLaboratory of Protein Engineering and Bioactive Molecules (LIP-MB), LR11ES24, National Institute of Applied Sciences and Technology, University of Carthage, 1080, Tunis Cedex, Tunisia.
Mohamed Rabeh HajlaouiNational Institute of Agronomic Research (INRAT), Laboratory of Biotechnology Applied to Agriculture, 1004, El Menzah, Tunis, Tunisia.
Laura BaciouInstitut de Chimie Physique UMR 8000, CNRS, Université Paris-Saclay, 91405, Orsay, France.
Issam SmaaliLaboratory of Protein Engineering and Bioactive Molecules (LIP-MB), LR11ES24, National Institute of Applied Sciences and Technology, University of Carthage, 1080, Tunis Cedex, Tunisia.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Chitinases are enzymes that can break down chitin, a major component of the exoskeleton of insects and fungi. This feature makes them potential biopesticides in agriculture since they are considered a safe and environmentally friendly alternative to synthetic pesticides. In this work, we performed a comparative study between two different bacterial expression strains to produce a recombinant chitinase with improved stability. Escherichia coli strains Origami B and BL21 (DE3) were selected for their distinct cytosolic environment to express BhChitA chitinase of Bacillus halodurans C-125 and to investigate the role of disulfide bond formation and proper folding on its stability and activity. Expression of the recombinant BhChitA in bacterial strain containing oxidative cytosol (Origami B) improved its activity and stability. Although both expression systems have comparable biochemical properties (temperature range 20-80 °C and pH spectrum 3-10), BhChitA expressed in Origami strain seems more stable than expressed in BL21. Furthermore, the optimal expression conditions of the recombinant BhChitA has been carried out at 30 °C during 6 h for the Origami strain, against 20 °C during 2 h for BL21. On the other hand, no significant differences were detected between the two enzymes when the effect of metal ions was tested. These findings correlate with the analysis of the overall structure of BhChitA. The model structure permitted to localize disulfide bond, which form a stable connection between the substrate-binding residues and the hydrophobic core. This link is required for efficient binding of the chitin insertion domain to the substrate. BhChitA exhibited in vitro antifungal effect against phytopathogenic fungi and suppressed necrosis of Botrytis cinerea on detached tomato leaves. In vitro assays showed the influence of BhChitA on growth suppression of Botrytis cinerea (53%) Aspergillus niger (65%), Fusarium graminearum (25%), and Fusarium oxysporum (34%). Our results highlight the importance of the bacterial expression system with oxidative cytosol in producing promising biopesticides that can be applied for post-harvest processing and crop protection.

Indexed as

ChitinasesEnzyme StabilityEscherichia coliFusariumRecombinant ProteinsBacillusBacterial ProteinsBotrytisHydrogen-Ion ConcentrationPlant DiseasesTemperatureBacterial ProteinsChitinasesRecombinant ProteinsBiopesticideDisulfide bondsGH18 chitinasesMolecular modelingPlant protection

Identifiers

PMID38265740

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Registered trials

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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.