Evidence map›Paper›PMID 37533727›Full record

ArticleEngineering in life sciences2023

Identification and characterization of inulinases by bioinformatics analysis of bacterial glycoside hydrolases family 32 (GH32).

Fatemeh Khosravi, Ehsan Mohseni Fard, Marzieh Hosseininezhad, Hadi Shoorideh

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Engineering in life sciences, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
1.3field-weighted citation impact, top 22% 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

4 citing papers in PubMed, 8 citations in OpenAlex.

  1. Review
  2. Article
  3. Genome Characteristics of the Endophytic FungusJournal of fungi (Basel, Switzerland) · 2024
    Article
  4. Article
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

4 authors at 3 institutions in 2 countries.

Fatemeh KhosraviPh. D. student of Agriculture Biotechnology University of Zanjan Zanjan Iran.
Ehsan Mohseni FardDepartment of Plant Production and Genetics Faculty of Agriculture University of Zanjan Zanjan Iran.
Marzieh HosseininezhadDepartment of Food Biotechnology Research Institute of Food Science and Technology Mashhad Iran.
Hadi ShooridehDryland Pulses Research Department North Khorassan Agricultural Research, Education and Extension Organization (AREEO) Shirvan Iran.
University of Zanjan · IRAgricultural Research & Education Organization · IRInstitute of Food Science and Technology · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The glycoside hydrolase family contains enzymes that break the glycosidic bonds of carbohydrates by hydrolysis. Inulinase is one of the most important industrial enzymes in the family of Glycoside Hydrolases 32 (GH32). In this study, to identify and classify bacterial inulinases initially, 16,002 protein sequences belonging to the GH32 family were obtained using various databases. The inulin-effective enzymes (endoinulinase and exoinulinase) were identified. Eight endoinulinases (EC 3.2.1.7) and 4318 exoinulinases (EC 3.2.1.80) were found. Then, the localization of endoinulinase and exoinulinase enzymes in the cell was predicted. Among them, two extracellular endoinulinases and 1232 extracellular exoinulinases were found. The biochemical properties of 363 enzymes of the genus

Indexed as

bacteriaEC numberGlycoside Hydrolase 32inulininulinase

Identifiers

PMID37533727
PMCPMC10390659
OpenAlexW4383723461

What Socratic holds

Textmetadata
LicenceCC BY-NC-ND
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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 Socratic graph.