Evidence map›Paper›PMID 39080612›Full record

ArticleMicrobial cell factories2024

Production, purification, characterization, and safety evaluation of constructed recombinant D-psicose 3-epimerase.

Nisit Watthanasakphuban, Pimsiriya Srila, Phitsanu Pinmanee, Charatda Punvittayagul, Nopphon Petchyam, Boontiwa Ninchan

Abstract read
In one paragraph

Article in Microbial cell factories, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Review
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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

6 authors.

Nisit WatthanasakphubanDepartment of Biotechnology, Faculty of Agro-Industry, Kasetsart University, Chatuchak, Bangkok, 10900, Thailand.
Pimsiriya SrilaDepartment of Biotechnology, Faculty of Agro-Industry, Kasetsart University, Chatuchak, Bangkok, 10900, Thailand.
Phitsanu PinmaneeEnzyme Technology Research Team, National Center of Genetic Engineering and Biotechnology (BIOTEC), Pathum Thani, 12120, Thailand.
Charatda PunvittayagulCenter of Veterinary Medical Diagnostic and Animal Health Innovation, Faculty of Veterinary Medicine, Chiang Mai University, Chiang Mai, 50100, Thailand.
Nopphon PetchyamCenter for Advanced Therapeutics, Institute of Molecular Biosciences, Mahidol University, Nakhon Pathom, 73170, Thailand.
Boontiwa NinchanDepartment of Biotechnology, Faculty of Agro-Industry, Kasetsart University, Chatuchak, Bangkok, 10900, Thailand. boontiwa.ni@ku.th.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundD-psicose 3-epimerase (DPEase) is a potential catalytic enzyme for D-psicose production. D-psicose, also known as D-allulose, is a low-calorie sweetener that has gained considerable attention as a healthy alternative sweetener due to its notable physicochemical properties. This research focused on an in-depth investigation of the expression of the constructed DPEase gene from Agrobacterium tumefaciens in Escherichia coli for D-psicose synthesis. Experimentally, this research created the recombinant enzyme, explored the optimization of gene expression systems and protein purification strategies, investigated the enzymatic characterization, and then optimized the D-psicose production. Finally, the produced D-psicose syrup underwent acute toxicity evaluation to provide scientific evidence supporting its safety.

resultsThe optimization of DPEase expression involved the utilization of Mn

conclusionsThese findings have direct and practical implications for the industrial-scale production of D-psicose, a valuable rare sugar with a broad range of applications in the food and pharmaceutical industries. This research should advance the understanding of DPEase biocatalysis and offers a roadmap for the successful scale-up production of rare sugars, opening new avenues for their utilization in various industrial processes.

Indexed as

Escherichia coliFructoseRecombinant ProteinsAgrobacterium tumefaciensAnimalsBacterial ProteinsCarbohydrate EpimerasesRacemases and EpimerasesRatsBacterial ProteinsCarbohydrate EpimerasesFructosepsicoseRacemases and EpimerasesRecombinant ProteinsAcute toxicityAlluloseD-psicoseD-psicose 3-epimeraseEpimerizationRare sugars

Identifiers

PMID39080612
PMCPMC11290309

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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.