Facile Immobilization of Enzyme via Co-Electrospinning: A Simple Method for Enhancing Enzyme Reusability and Monitoring an Activity-Based Organic Semiconductor.

Musab M Aldhahri, Yaaser Q Almulaiky, Reda M El-Shishtawy, Waleed Al-Shawafi, Ahmed Alngadh, Rayan Maghrabi

Abstract read

In one paragraph

Article in ACS omega, 2018. 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.

Synthesis of Cellulose Hexanoate, Benzoate, and Mixed Esters: Exploring Their Potential as Enzyme Immobilization Platforms.Macromolecular bioscience · 2025
Article
Efficient Conversion of 5-Hydroxymethylfurfural to 2,5-Furandicarboxylic Acid by the Magnetic Laccase Nanoflowers-2,2,6,6-Tetramethylpiperidin-1-Oxyl System.Materials (Basel, Switzerland) · 2025
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

6 authors.

Musab M AldhahriCenter of Nanotechnology, King Abdulaziz University, P.O. Box 80216, Jeddah 21589, Saudi Arabia.

Yaaser Q AlmulaikyDepartment of Biochemistry, Faculty of Science, University of Jeddah, P.O.Box 80203, Jeddah 21589, Saudi Arabia.

Reda M El-ShishtawyDepartment of Biochemistry, Department of Chemistry, and Department of Biochemistry, King Abdulaziz University, P. O. Box 80200, Jeddah 21589, Saudi Arabia.

Waleed Al-ShawafiDepartment of Biochemistry, Department of Chemistry, and Department of Biochemistry, King Abdulaziz University, P. O. Box 80200, Jeddah 21589, Saudi Arabia.

Ahmed AlngadhKing Abdulaziz City for Science and Technology, P.O. Box 6086, Riyadh 11442, Saudi Arabia.

Rayan MaghrabiDepartment of Biochemistry, Department of Chemistry, and Department of Biochemistry, King Abdulaziz University, P. O. Box 80200, Jeddah 21589, Saudi Arabia.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The stability, reusability, and monitoring of enzyme activity have been investigated to improve their efficiency for successful utilization in a broad range of industrial and medical applications. Herein, we present a simple method for fabricating an electrospun fiber/enzyme scaffold via co-electrospinning. The characterization of soluble and immobilized α-amylases with regard to pH, thermal stability, and reusability were studied. An organic light emitting material tris(8-hydroxyquinoline)aluminum was incorporated to monitor the enzyme activity for several reuses.

Identifiers

PMID31458817

DOI10.1021/acsomega.8b00366

PMCPMC6644564

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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.