Evidence map›Paper›PMID 40632773›Full record

ArticlePloS one2025

Production of recombinant D-allulose 3-epimerase utilizing an auto-induction approach in fermentor cultures suitable for industrial application.

Kenny Lischer, Fina Amreta Laksmi, Yudhi Nugraha, Helbert, Fauziah Az-Zahra, David Herawan, Ario Betha Juanssilfero, Des Saputro Wibowo, Kharisma Panji Ramadhan, Isa Nuryana and 1 more

Abstract read
In one paragraph

Article in PloS one, 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
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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

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.

Kenny LischerDepartment of Chemical Engineering, University of Indonesia, Jakarta, Indonesia.ORCID https://orcid.org/0000-0003-1424-1609
Fina Amreta LaksmiResearch Center for Applied Microbiology, National Research and Innovation Agency, Bogor, West Java, Indonesia.ORCID https://orcid.org/0000-0001-6887-2276
Yudhi NugrahaResearch Center for Molecular Biology Eijkman, National Research and Innovation Agency, Bogor, West Java, Indonesia.ORCID https://orcid.org/0000-0003-1186-4093
Helbert
Fauziah Az-ZahraResearch Center for Applied Microbiology, National Research and Innovation Agency, Bogor, West Java, Indonesia.
David HerawanDepartment of Chemical Engineering, University of Indonesia, Jakarta, Indonesia.ORCID https://orcid.org/0009-0009-7440-6357
Ario Betha JuanssilferoResearch Center for Environmental and Clean Technology, National Research and Innovation Agency, Bogor, West Java, Indonesia.ORCID https://orcid.org/0000-0002-6837-9681
Des Saputro WibowoResearch Center for Applied Microbiology, National Research and Innovation Agency, Bogor, West Java, Indonesia.
Kharisma Panji RamadhanResearch Center for Applied Microbiology, National Research and Innovation Agency, Bogor, West Java, Indonesia.
Isa NuryanaResearch Center for Applied Microbiology, National Research and Innovation Agency, Bogor, West Java, Indonesia.
Mohd Shukuri Mohamad AliEnzyme and Microbial Technology Research Centre, Universiti Putra Malaysia, Selangor, Malaysia.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

D-Allulose 3-epimerase (DAEase) is the key enzyme catalyzing D-fructose to catalyze into D-allulose, a rare sugar in foods, which has lately drawn increasing worldwide attention owing to its possible health advantages and application as a substitute sucrose. This work focused on the development of an economical, scalable production method of DAEase by using the Escherichia coli BL21 star™ (DE3) as host expression. The research work aims to optimize the production of the enzyme through an auto-induction strategy in chemically defined media by using lactose as a natural inducer, thereby overcoming various limitations of conventional IPTG induction methods. The optimal concentration of lactose, glucose, and glycerol for maximum expression of DAEase was determined to be 1.5%, 0.125%, and 1.5%, respectively. Fermentor-scale optimization yielded a maximum amount of this enzyme with 5% inoculant, 300 rpm agitation, and 2 vvm aeration. Purification by affinity and anion exchange chromatography resulted in a sevenfold increase in specific activity with an overall yield of 12% and 43 mg of pure recombinant DAEase per liter of culture. Enzyme assays confirmed that DAEase had catalytic activity in the conversion of D-fructose to D-allulose, which was further confirmed by HPLC analysis. This optimized auto-induction-based strategy demonstrated its potential for large-scale production of DAEase in a cost-effective manner with enhanced reproducibility to meet industrial demands for synthesizing D-allulose.

Indexed as

BioreactorsCarbohydrate EpimerasesFermentationRacemases and EpimerasesRecombinant ProteinsEscherichia coliFructoseGlucoseGlycerolLactoseCarbohydrate EpimerasesFructoseGlucoseGlycerolLactosepsicoseRacemases and EpimerasesRecombinant Proteins

Identifiers

PMID40632773
PMCPMC12240355

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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.