Evidence map›Paper›PMID 40551113›Full record

ArticleMicrobial cell factories2025

Production, purification, and characterization of a thermally stable, Acidophilic Cellulase from Aspergillus awamori AFE1 isolated from Longhorn beetle (Cerambycidae latreille).

Ayoola E Afe, Olusola T Lawal, Olufemi S Bamidele, Farhad Badshah, Bukola R Oyelere, Andrew N Efomah, Mostafa A Abdel-Maksoud, Sabiha Fatima, Abdulaziz Alamri, Mohamed A El-Tayeb and 1 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Microbial cell factories, 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. Review
  2. 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

11 authors.

Ayoola E AfeEnzyme and Microbial Technology Unit, Department of Biochemistry, School of Life Sciences, Federal University of Technology, Akure, 340252, Nigeria. afeae@futa.edu.ng.
Olusola T LawalEnzyme and Microbial Technology Unit, Department of Biochemistry, School of Life Sciences, Federal University of Technology, Akure, 340252, Nigeria.
Olufemi S BamideleEnzyme and Microbial Technology Unit, Department of Biochemistry, School of Life Sciences, Federal University of Technology, Akure, 340252, Nigeria.
Farhad BadshahShenzhen Branch, Guangdong Laboratory of Lingnan Modern Agriculture, Key Laboratory of Livestock and Poultry Multi-Omics of MARA, Agricultural Genomics Institute at Shenzhen, Chinese Academy of Agricultural Sciences, Shenzhen, 518000, China.
Bukola R OyelereDepartment of Microbiology, Federal University of Technology, Akure, 340252, Nigeria.
Andrew N EfomahSchool of Environmental Science and Engineering/Tianjin Key Lab of Biomass-Wastes Utilization/Key Laboratory of Ministry of Education, Tianjin University, Tianjin, 300072, China.
Mostafa A Abdel-MaksoudChair of Biomedical Applications of Nanomaterials, Biochemistry Department, College of Science, King Saud University, P.O. Box 2455, Riyadh 11451, Saudi Arabia.
Sabiha FatimaDepartment of Clinical Laboratory Science, College of Applied Medical Sciences, King Saud University, Riyadh, 11433, Saudi Arabia.
Abdulaziz AlamriBiochemistry Department, College of Science, King Saud University, Riyadh, 11451, Saudi Arabia.
Mohamed A El-TayebBotany and Microbiology Department, College of Science, King Saud University, Riyadh, Saudi Arabia.
David M SanniEnzyme and Microbial Technology Unit, Department of Biochemistry, School of Life Sciences, Federal University of Technology, Akure, 340252, Nigeria. dmsanni@futa.edu.ng.

Funding

Researchers Supporting Project RSPD2025R552
6 · The paper itself

Abstract

backgroundThe relentless pursuit of cost-effective cellulase, a key enzyme in the biocatalytic conversion of cellulose, has led to exploring insect guts as potential sources of biocatalysts. Herbivorous insects' intestinal tracts are recognized as rich reservoirs of cellulolytic microorganisms. This study investigates cellulase production, purification, and characterization from Aspergillus awamori AFE1, isolated from the gut of longhorn beetles (Cerambycidae latreille). Basic cellulase production parameters were optimized. The cellulase produced under optimum conditions was purified by ammonium sulphate precipitation and chromatographic methods, followed by characterization of the purified enzyme.

resultsOptimum cellulase production was observed at pH 5 and 30 °C, using cellulose and NaNO

conclusionThis study has shown Aspergillus awamori AFE1, isolated from the Longhorn beetle gut, as a unique source of acid-stable, thermostable, and organic solvent-resistant cellulase with industrial potential. Its unique enzymatic properties offer promising applications in biofuel production and lignocellulosic biomass conversion.

Indexed as

AspergillusCellulaseColeopteraAnimalsCelluloseEnzyme StabilityHydrogen-Ion ConcentrationTemperatureCellulaseCelluloseAspergillus AwamoriCellulaseEnzyme purificationLonghorned beetle

Identifiers

PMID40551113
PMCPMC12186396

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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.