Evidence map›Paper›PMID 39755623›Full record

ArticleBMC biotechnology2025

Statistical optimization of pectinases from thermophilic Aspergillus fumigatus BT-4 employing response surface methodology through submerged fermentation using agricultural wastes.

Imran Ali, Roheena Abdullah, Sana Saqib, Kinza Nisar, Afshan Kaleem, Mehwish Iqtedar, Irfana Iqbal, Xiaoming Chen

Abstract read
In one paragraph

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

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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

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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

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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. AI-nanotech synergies: recent advances in sustainable bio-manufacturing.World journal of microbiology & biotechnology · 2026
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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.

Imran AliSchool of Life Science and Engineering, Southwest University of Science and Technology, Mianyang, China. imranalisheik@gmail.com.
Roheena AbdullahDepartment of Biotechnology, Lahore College for Women University, Lahore, Pakistan. roheena_abdullah@yahoo.com.
Sana SaqibDepartment of Biotechnology, Lahore College for Women University, Lahore, Pakistan.
Kinza NisarDepartment of Biotechnology, Lahore College for Women University, Lahore, Pakistan.
Afshan KaleemDepartment of Biotechnology, Lahore College for Women University, Lahore, Pakistan.
Mehwish IqtedarDepartment of Biotechnology, Lahore College for Women University, Lahore, Pakistan.
Irfana IqbalDepartment of Biotechnology, Lahore College for Women University, Lahore, Pakistan.
Xiaoming ChenSchool of Life Science and Engineering, Southwest University of Science and Technology, Mianyang, China. cxmxkd@163.com.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundIn this study, thermophilic pectinase-producing strains were isolated. Among all the isolates, strain No. 4 was identified as Aspergillus fumigatus BT-4 based on its morphology and 18 S rDNA analysis. This strain was employed to screen various fermentation media to enhance pectinase production. Pectinases are crucial enzymes with significant industrial applications, particularly in the food and textile industries. Identifying efficient pectinase producers and optimizing their production processes are essential for improving industrial applications.

resultsMaximum pectinase production was observed using 1% grapefruit peel in M5 media. Shake flask kinetics demonstrated the highest values of specific rate constant (qp), specific growth rate (µ), product yield coefficient (Y

conclusionsThe study successfully isolated and identified Aspergillus fumigatus BT-4 as a potent thermophilic pectinase producer. Optimization of the fermentation process using 1% grapefruit peel in M5 media significantly enhanced pectinase production. Using grapefruit peel as an agricultural waste in pectinase production reduces costs by eliminating the need for expensive raw materials and utilizing a low-cost, sustainable, and locally available substrate. This approach also minimizes waste disposal expenses, making the process more economical. The enzyme was effectively purified, and its kinetic and thermodynamic properties were thoroughly characterized, revealing its potential for industrial applications. The comprehensive analysis of production kinetics and optimization strategies provides a robust foundation for scaling up pectinase production, contributing to more efficient and cost-effective industrial processes.

Indexed as

Aspergillus fumigatusFermentationPolygalacturonaseAgricultureBiomassFungal ProteinsKineticsFungal ProteinsPolygalacturonaseA. fumigatusCoefficientKineticsPectinasesVolumetric rate

Identifiers

PMID39755623
PMCPMC11699716

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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.