Evidence map›Paper›PMID 41108388›Full record

ArticleApplied microbiology and biotechnology2025

Immobilized inclusion bodies of recombinant cold-adaptive lipase from Antarctic Pseudomonas sp. as catalysts.

Muhammad Nura Bello, Suriana Sabri, Normi Mohd Yahaya, Fairolniza Mohd Shariff, Mohd Shukuri Mohamad Ali

Abstract read
In one paragraph

Article in Applied microbiology 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.

0numbers the graph read from it
0cells of the map it votes in
0citing 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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

5 authors.

Muhammad Nura BelloEnzyme and Microbial Technology Research Centre, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia, 43400, Serdang, Malaysia.
Suriana SabriEnzyme and Microbial Technology Research Centre, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia, 43400, Serdang, Malaysia.
Normi Mohd YahayaEnzyme and Microbial Technology Research Centre, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia, 43400, Serdang, Malaysia.
Fairolniza Mohd ShariffEnzyme and Microbial Technology Research Centre, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia, 43400, Serdang, Malaysia.
Mohd Shukuri Mohamad AliEnzyme and Microbial Technology Research Centre, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia, 43400, Serdang, Malaysia. mshukuri@upm.edu.my.ORCID https://orcid.org/0000-0003-2751-9649

Funding

Universiti Putra Malaysia GPB/2021/9708100
6 · The paper itself

Abstract

Immobilization of lipase has been receiving attention for a long time; this is because of the need for robust catalysts by industries. Numerous literature has reported improvements in the properties of immobilized lipase in terms of stability when exposed to extreme conditions of temperature, pH, and organic solvents commonly encountered in most industrial settings. However, some microbial lipases that have the potential to catalyze significant reactions do occur in the form of inclusion bodies when expressed in Escherichia coli. This research aimed to immobilize catalytically active inclusion bodies (CatIBs) of LipAMS8 lipase onto Seplite LX120 as the adsorption material. Scanning electron microscopy and Fourier infrared spectroscopy were used to ascertain the immobilization. Immobilized CatIBs have an optimum temperature of 20 °C and pH of 9.0. They exhibit high stability to broad temperatures, pH levels, and organic solvents, with excellent storage stability and reusability, retaining 50% of their residual activity after ten cycles. They demonstrated excellent activity in the transesterification of waste cooking oil with methanol, in which 2% of the immobilized CatIBs produced up to 98% biodiesel in a ratio of 1:9 at 25 °C for 7 h at 200 rpm. LipAMS8 CatIBs immobilization improved their stability and capability to produce biodiesel at lower temperatures. KEY POINTS: •Catalytically active inclusion bodies from recombinant AMS8 lipase occurring naturally were successfully immobilized onto seplite LX120. Morphological and structural analyses using SEM and FITR confirmed the immobilization. •Characterization revealed the immobilized LipAMS8 CatIBs to maintain the residual activity of up to 50% at a broad temperature (10-80 °C) and pH (4-12). •Interactions with metal ions and various organic solvents manifest their stability. Transesterification reaction with methanol using palm cooking oil to produce biodiesel at 25 °C which revealed their synthetic capacity.

Indexed as

Enzymes, ImmobilizedInclusion BodiesLipasePseudomonasAntarctic RegionsBiofuelsCold TemperatureEnzyme StabilityEscherichia coliEsterificationHydrogen-Ion ConcentrationMethanolRecombinant ProteinsSolventsTemperatureBiofuelsEnzymes, ImmobilizedLipaseMethanolRecombinant ProteinsSolventsAntarcticCold-adaptedImmobilizationInclusion bodyLipasePseudomonas

Identifiers

PMID41108388
PMCPMC12535532

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
Read underepoch 390

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.