Evidence map›Paper›PMID 39335925›Full record

ArticleFoods (Basel, Switzerland)2024

Boosting Fructosyl Transferase's Thermostability and Catalytic Performance for Highly Efficient Fructooligosaccharides (FOS) Production.

Dandan Niu, Nan Zhao, Jun Wang, Nokuthula Peace Mchunu, Kugen Permaul, Suren Singh, Zhengxiang Wang

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Foods (Basel, Switzerland), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Review
  2. Review
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

7 authors.

Dandan NiuDepartment of Biological Chemical Engineering, College of Chemical Engineering and Material Sciences, Tianjin University of Science and Technology, Tianjin 300457, China.
Nan ZhaoDepartment of Biological Chemical Engineering, College of Chemical Engineering and Material Sciences, Tianjin University of Science and Technology, Tianjin 300457, China.
Jun WangTianjin Key Laboratory of Industrial Microbiology, College of Biotechnology, Tianjin University of Science and Technology, Tianjin 300457, China.
Nokuthula Peace MchunuNational Research Foundation, P.O. Box 2600, Pretoria 0001, South Africa.
Kugen PermaulDepartment of Biotechnology and Food Technology, Faculty of Applied Sciences, Durban University of Technology, P.O. Box 1334, Durban 4001, South Africa.
Suren SinghDepartment of Biotechnology and Food Technology, Faculty of Applied Sciences, Durban University of Technology, P.O. Box 1334, Durban 4001, South Africa.
Zhengxiang WangDepartment of Biological Chemical Engineering, College of Chemical Engineering and Material Sciences, Tianjin University of Science and Technology, Tianjin 300457, China.

Funding

the Intergovernmental International Scientific and Technological Innovation Cooperation Program, MOST, China 2018YFE0100400the Intergovernmental International Scientific and Technological Innovation Cooperation Program, MOST, China 2021YFE0106200the Tianjin Outstanding Talent Program, China JC20200309
6 · The paper itself

Abstract

Achieving enzymatic food processing at high substrate concentrations can significantly enhance production efficiency; however, related studies are notably insufficient. This study focused on the enzymatic synthesis of fructooligosaccharides (FOS) at high temperature and high substrate concentration. Results revealed that increased viscosity and limited substrate solubility in high-concentration systems could be alleviated by raising the reaction temperature, provided it aligned with the enzyme's thermostability. Further analysis of enzyme thermostability in real sucrose solutions demonstrates that the enzyme's thermostability was remarkedly improved at higher sucrose concentrations, evidenced by a 10.3 °C increase in melting temperature (

Indexed as

engineering process optimizationenzymatic catalysis efficiencyenzyme-catalyzed FOS synthesishigh substrate concentrationthermostability of enzymes

Identifiers

PMID39335925
PMCPMC11431173

What OpenQuestion holds

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Registered trials

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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.