Evidence map›Paper›PMID 30963480›Full record

ArticleMolecular biotechnology2019

High Conversion of D-Fructose into D-Allulose by Enzymes Coupling with an ATP Regeneration System.

Qin Xiao, Junrong Niu, Hou Liu, Youcai Liu, Xingding Zhou

Abstract read
PubMed Publisher
In one paragraph

Article in Molecular biotechnology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.8field-weighted citation impact, top 15% of its field
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

10 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
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  3. Article
  4. Article
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  7. Metabolically EngineeredFrontiers in bioengineering and biotechnology · 2022
    Article
  8. 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

5 authors at 2 institutions in 2 countries.

Qin XiaoCollege of Chemistry and Chemical Engineering, Central South University, Changsha, 410083, Hunan, China.
Junrong NiuCollege of Chemistry and Chemical Engineering, Central South University, Changsha, 410083, Hunan, China.
Hou LiuCollege of Chemistry and Chemical Engineering, Central South University, Changsha, 410083, Hunan, China.
Youcai LiuCollege of Chemistry and Chemical Engineering, Central South University, Changsha, 410083, Hunan, China. lycllf@126.com.
Xingding ZhouSchool of Life Sciences and Chemical Technology, Ngee Ann Polytechnic, Singapore, 599489, Singapore. ZHOU_Xingding@np.edu.sg.
Central South University · CNNgee Ann Polytechnic · SG

Funding

Ministry of Education of Singapore 17GAP002
6 · The paper itself

Abstract

D-Allulose is a rare monosaccharide that exists in extremely small quantities in nature, and it is also hard to prepare at a large scale via chemical or enzyme synthetic route due to low conversion and downstream separation complexity. Using D-psicose epimerase and L-rhamnulose kinase, a method enabling high conversion of D-allulose from D-fructose without the need for a tedious isomer separation step was established recently. However, this method requires expensive ATP to facilitate the reaction. In the present study, an ATP regenerate system was developed coupling with polyphosphate kinase. In our optimized reaction with purified enzymes, the conversion rate of 99% D-fructose was achieved at the concentrations of 2 mM ATP, 5 mM polyphosphate, 20 mM D-fructose, and 20 mM Mg

Indexed as

Adenosine TriphosphateBiotransformationCarbohydrate EpimerasesCations, DivalentCloning, MolecularEnzyme AssaysEscherichia coliFructoseGene ExpressionGenetic VectorsMagnesiumPhosphotransferases (Alcohol Group Acceptor)PolyphosphatesRecombinant Fusion ProteinsSubcellular FractionsThermotoga maritimaAdenosine TriphosphateCarbohydrate EpimerasesCations, DivalentFructoseMagnesiumPhosphotransferases (Alcohol Group Acceptor)PolyphosphatespsicoseRecombinant Fusion ProteinsrhamnulokinaseATP regeneration systemD-AlluloseD-FructoseL-Rhamnulose kinasePolyphosphatePolyphosphate kinase

Identifiers

PMID30963480
OpenAlexW2937930432

What OpenQuestion holds

Textmetadata
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.