Evidence map›Paper›PMID 41045416›Full record

ArticleApplied biochemistry and biotechnology2025

The Lipase Enzyme Attached Micromotors for Degradation of Oils As Water Contaminant.

Elif Sever, Ulviye Kilimci, Deniz Aktaş Uygun

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Article in Applied biochemistry and biotechnology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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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

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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

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

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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

3 authors.

Elif SeverGraduate School of Health Science, Aydın Adnan Menderes University, Aydın, Türkiye.
Ulviye KilimciFaculty of Science, Department of Chemistry, Aydın Adnan Menderes University, Aydın, Türkiye.
Deniz Aktaş UygunGraduate School of Health Science, Aydın Adnan Menderes University, Aydın, Türkiye. daktasuygun@gmail.com.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In this study, a research design was implemented to investigate the potential of PPy-COOH/Ni micromotors for the degradation of oils as water pollutants. The study's objective was to determine the micromotors' capacity for oil removal. For this purpose, PPy-COOH/Ni micromotors were prepared by template-directed electrodeposition method, and lipase enzyme (from Porcine Pancreas) was covalently bound to these micromotors. The micromotors were characterized by SEM, EDX, and FTIR techniques. From the SEM photographs, it was found that the synthesized micromotors were cylindrical, about 5 μm in diameter and 15 μm in size. In addition, from the FTIR spectra, the binding of lipase enzyme to the micromotors was shown by amide I, II, and III bonds at 1640 cm

Indexed as

Enzymes, ImmobilizedLipaseOilsWater Pollutants, ChemicalAnimalsHydrogen-Ion ConcentrationSwineTemperatureEnzymes, ImmobilizedLipaseOilsWater Pollutants, ChemicalImmobilizationLipaseMicromotorOil degradationTriacylglycerol

Identifiers

What OpenQuestion holds

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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 OpenQuestion graph.