Evidence map›Paper›PMID 33076889›Full record

ArticleBMC biotechnology2020

A novel high performance in-silico screened metagenome-derived alkali-thermostable endo-β-1,4-glucanase for lignocellulosic biomass hydrolysis in the harsh conditions.

Shohreh Ariaeenejad, Atefeh Sheykh Abdollahzadeh Mamaghani, Morteza Maleki, Kaveh Kavousi, Mehdi Foroozandeh Shahraki, Ghasem Hosseini Salekdeh

Open access · goldAbstract read
In one paragraph

Article in BMC biotechnology, 2020. 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
3.4field-weighted citation impact, top 7% 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, 54 citations in OpenAlex.

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  5. Microbial β-glucanases: production, properties, and engineering.World journal of microbiology & biotechnology · 2023
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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

6 authors at 3 institutions in 2 countries.

Shohreh AriaeenejadDepartment of Systems and Synthetic Biology, Agricultural Biotechnology Research Institute of Iran (ABRII), Agricultural Research Education and Extension Organization (AREEO), P. O. Box: 31535-1897, Karaj, Iran. shariaee@gmail.com.ORCID 0000-0001-6385-5098
Atefeh Sheykh Abdollahzadeh MamaghaniDepartment of Systems and Synthetic Biology, Agricultural Biotechnology Research Institute of Iran (ABRII), Agricultural Research Education and Extension Organization (AREEO), P. O. Box: 31535-1897, Karaj, Iran.
Morteza MalekiDepartment of Systems and Synthetic Biology, Agricultural Biotechnology Research Institute of Iran (ABRII), Agricultural Research Education and Extension Organization (AREEO), P. O. Box: 31535-1897, Karaj, Iran.
Kaveh KavousiLaboratory of Complex Biological Systems and Bioinformatics (CBB), Institute of Biochemistry and Biophysics (IBB), University of Tehran, Tehran, Iran.
Mehdi Foroozandeh ShahrakiLaboratory of Complex Biological Systems and Bioinformatics (CBB), Institute of Biochemistry and Biophysics (IBB), University of Tehran, Tehran, Iran.
Ghasem Hosseini SalekdehDepartment of Systems and Synthetic Biology, Agricultural Biotechnology Research Institute of Iran (ABRII), Agricultural Research Education and Extension Organization (AREEO), P. O. Box: 31535-1897, Karaj, Iran. h_salekdeh@abrii.ac.ir.
Agricultural Research & Education Organization · IRUniversity of Tehran · IRAgricultural Biotechnology Research Institute of Iran · IR

Funding

Agricultural Biotechnology Research Institute of Iran -
6 · The paper itself

Abstract

backgroundLignocellulosic biomass, is a great resource for the production of bio-energy and bio-based material since it is largely abundant, inexpensive and renewable. The requirement of new energy sources has led to a wide search for novel effective enzymes to improve the exploitation of lignocellulose, among which the importance of thermostable and halotolerant cellulase enzymes with high pH performance is significant.

resultsThe primary aim of this study was to discover a novel alkali-thermostable endo-β-1,4-glucanase from the sheep rumen metagenome. At first, the multi-step in-silico screening approach was utilized to find primary candidate enzymes with superior properties. Among the computationally selected candidates, PersiCel4 was found and subjected to cloning, expression, and purification followed by functional and structural characterization. The enzymes' kinetic parameters, including V

conclusionConsidering the urgent demand for stable cellulases that are operational on extreme temperature and pH conditions and due to several proposed distinctive characteristics of PersiCel4, it can be used in the harsh condition for bioconversion of lignocellulosic biomass.

Indexed as

BiomassMetagenomeAlkaliesAnimalsCellulaseCloning, MolecularComputer SimulationEndo-1,4-beta XylanasesEnzyme StabilityEscherichia coliGene Expression Regulation, BacterialHydrogen-Ion ConcentrationHydrolysisKineticsLigninOryzaAlkaliesCellulaseEndo-1,4-beta XylanasesLigninlignocelluloseRecombinant ProteinsEnzymatic hydrolysisIn-silico screeningMetagenomeNovel endo-β-1,4-glucanaseRice straw

Identifiers

PMID33076889
PMCPMC7574624
OpenAlexW3093141145

What OpenQuestion holds

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LicenceCC BY
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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.