Evidence map›Paper›PMID 24031719›Full record

ArticleBrazilian journal of microbiology : [publication of the Brazilian Society for Microbiology]2011

Characterization of a chitinase with antifungal activity from a native Serratia marcescens B4A.

Mandana Zarei, Saeed Aminzadeh, Hossein Zolgharnein, Alireza Safahieh, Morteza Daliri, Kambiz Akbari Noghabi, Ahmad Ghoroghi, Abbasali Motallebi

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In one paragraph

Article in Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology], 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
0.8field-weighted citation impact, top 29% 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

39 citing papers in PubMed, 78 citations in OpenAlex.

  1. Article
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  4. Functional and Genomic Characterization ofPlants (Basel, Switzerland) · 2026
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  15. An overview of viral chitinases: General properties and biotechnological potential.Experimental biology and medicine (Maywood, N.J.) · 2023
    Review
  16. Review
  17. Article
  18. Review
  19. 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

8 authors at 2 institutions in 1 country.

Mandana ZareiDepartment of Animal and Marine Biotechnology, National Institute of Genetic Engineering and Biotechnology (NIGEB) , Shahrak-e Pajoohesh Km 15, Tehran-Karaj Highway, Tehran , Iran ; Faculty of Marine Sciences, Khorramshahr Marine Sciences and Technology University , Khorramshahr , Iran.
Saeed Aminzadeh
Hossein Zolgharnein
Alireza Safahieh
Morteza Daliri
Kambiz Akbari Noghabi
Ahmad Ghoroghi
Abbasali Motallebi
National Institute of Genetic Engineering and Biotechnology · IRKhorramshahr University of Marine Science and Technology · IR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Chitinases have the ability of chitin digestion that constitutes a main compound of the cell wall in many of the phytopathogens such as fungi. In the following investigation, a novel chitinase with antifungal activity was characterized from a native Serratia marcescens B4A. Partially purified enzyme had an apparent molecular mass of 54 kDa. It indicated an optimum activity in pH 5 at 45°C. Enzyme was stable in 55°C for 20 min and at a pH range of 3-9 for 90 min at 25°C. When the temperature was raised to 60°C, it might affect the structure of enzymes lead to reduction of chitinase activity. Moreover, the Km and Vmax values for chitin were 8.3 mg/ml and 2.4 mmol/min, respectively. Additionally, the effect of some cations and chemical compounds were found to stimulate the chitinase activity. In addition, Iodoacetamide and Idoacetic acid did not inhibit enzyme activity, indicating that cysteine residues are not part of the catalytic site of chitinase. Finally, chitinase activity was further monitored by scanning electronic microscopy data in which progressive changes in chitin porosity appeared upon treatment with chitinase. This enzyme exhibited antifungal activity against Rhizoctonia solani, Bipolaris sp, Alternaria raphani, Alternaria brassicicola, revealing a potential application for the industry with potentially exploitable significance. Fungal chitin shows some special features, in particular with respect to chemical structure. Difference in chitinolytic ability must result from the subsite structure in the enzyme binding cleft. This implies that why the enzyme didn't have significant antifungal activity against other Fungi.

Indexed as

AntifungalCharacterizationChitinaseSerratia marcescens B4A

Identifiers

PMID24031719
PMCPMC3768790
OpenAlexW2046086559

What OpenQuestion holds

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LicenceCC BY-NC
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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.