Evidence map›Paper›PMID 41034391›Full record

ArticleScientific reports2025

Preparation and enzymatic activity analysis of rChiA-DP derived from the Bacillus proteolyticus IMH/B-1 Strain isolated from Dermacentor nuttalli.

Fang Liu, Jile Huge, Muhammad Adeel Hassan, Syed Qaswar Ali Shah, Yuxin Liu, Gele Teri, Geqi Yila, Rina Sua, Letu Geri

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Scientific reports, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
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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

9 authors.

Fang Liu *Department of Veterinary Microbiology and Immunology, College of Veterinary Medicine, Inner Mongolia Agricultural University, No. 306 Zhaowuda Road, Hohhot, 010018, Inner Mongolia, China.
Jile Huge *Department of Veterinary Microbiology and Immunology, College of Veterinary Medicine, Inner Mongolia Agricultural University, No. 306 Zhaowuda Road, Hohhot, 010018, Inner Mongolia, China.
Muhammad Adeel HassanDepartment of Parasitology, Cholistan University of Veterinary and Animal Sciences , Bahawalpur, 63100, Pakistan.
Syed Qaswar Ali ShahDepartment of Zoology, Cholistan University of Veterinary and Animal Sciences , Bahawalpur, 63100, Pakistan.
Yuxin LiuDepartment of Veterinary Microbiology and Immunology, College of Veterinary Medicine, Inner Mongolia Agricultural University, No. 306 Zhaowuda Road, Hohhot, 010018, Inner Mongolia, China.
Gele TeriDepartment of Veterinary Microbiology and Immunology, College of Veterinary Medicine, Inner Mongolia Agricultural University, No. 306 Zhaowuda Road, Hohhot, 010018, Inner Mongolia, China.
Geqi YilaDepartment of Veterinary Microbiology and Immunology, College of Veterinary Medicine, Inner Mongolia Agricultural University, No. 306 Zhaowuda Road, Hohhot, 010018, Inner Mongolia, China.
Rina SuaDepartment of Veterinary Microbiology and Immunology, College of Veterinary Medicine, Inner Mongolia Agricultural University, No. 306 Zhaowuda Road, Hohhot, 010018, Inner Mongolia, China.
Letu GeriDepartment of Veterinary Microbiology and Immunology, College of Veterinary Medicine, Inner Mongolia Agricultural University, No. 306 Zhaowuda Road, Hohhot, 010018, Inner Mongolia, China. geriletusy@imau.edu.cn.

Funding

the Inner Mongolia Agricultural University First-Class Professional Course Construction Project SYKJYB202303the National Natural Science Foundation of China 3236190021
6 · The paper itself

Abstract

This study aimed to clone and express chitinase genes from Bacillus proteolyticus strains and characterize the enzymatic properties of recombinant enzymes. Bacillus proteolyticus was isolated from the body of Dermacentor nuttalli and renamed IMH/B-1. Chitin-degrading enzymes were screened via clear zone assay and PCR. The chitinase A gene (ChiA) was successfully cloned, and the recombinant plasmid pET28a-rChiA-DP (Dermatestor-derived Protein) was constructed. Recombinant chitinase protein (rChiA-DP) was expressed in Escherichia coli BL21 using IPTG induction and purified by nickel-nitrilotriacetic acid (Ni-NTA) affinity chromatography. Bioinformatic tools were used to predict the rChiA-DP protein sequences, analyse its enzyme family classification, and identify key amino acid residues in its catalytic domain. The enzymatic activity of rChiA-DP, along with its nematode resistance and antifungal effects on Caenorhabditis elegans (C. elegans) and fungi (Aspergillus sp.), was assessed under varied temperatures, pH, metal ions, salt concentrations and substrates. The amino acid sequence of the rChiA-DP contains a chitin-binding domain (CBD) (substrate binding), a fibronectin type III domain (FN3)(structural stability), and a catalytic domain with a typical TIM-barrel molecular structure (catalytic scaffold). SDS-PAGE analysis revealed that the molecular weight of the rChiA-DP was approximately 74.6 kDa, which is consistent with the theoretical predictions. The optimal conditions for rChiA-DP enzyme activity were 40 °C and pH 7.0. Enzyme activity was significantly enhanced by 10 mM Ba

Indexed as

BacillusBacterial ProteinsChitinasesDermacentorAmino Acid SequenceAnimalsAntifungal AgentsCaenorhabditis elegansChitinCloning, MolecularEscherichia coliHydrogen-Ion ConcentrationRecombinant ProteinsAntifungal AgentsBacterial ProteinsChitinChitinasesRecombinant ProteinsBacillusCaenorhabditis elegansEnzymatic activityFungiRecombinant chitinase

Identifiers

PMID41034391
PMCPMC12489124

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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.