Evidence map›Paper›PMID 30909913›Full record

ArticleMicrobial cell factories2019

Redesign of a novel D-allulose 3-epimerase from Staphylococcus aureus for thermostability and efficient biocatalytic production of D-allulose.

Zhangliang Zhu, Dengke Gao, Chao Li, Ying Chen, Menglu Zhu, Xin Liu, Masaru Tanokura, Hui-Min Qin, Fuping Lu

Open access · goldAbstract read
In one paragraph

Article in Microbial cell factories, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
5.1field-weighted citation impact, top 4% 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

13 citing papers in PubMed, 61 citations in OpenAlex.

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  12. Expression, Purification, Refolding, and Characterization of aFrontiers in bioengineering and biotechnology · 2020
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  13. Review onFrontiers in bioengineering and biotechnology · 2020
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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

9 authors at 1 institution in 1 country.

Zhangliang ZhuKey Laboratory of Industrial Fermentation Microbiology of the Ministry of Education, Tianjin Key Laboratory of Industrial Microbiology, College of Biotechnology, National Engineering Laboratory for Industrial Enzymes, Tianjin University of Science and Technology, Tianjin, 300457, People's Republic of China.
Dengke GaoKey Laboratory of Industrial Fermentation Microbiology of the Ministry of Education, Tianjin Key Laboratory of Industrial Microbiology, College of Biotechnology, National Engineering Laboratory for Industrial Enzymes, Tianjin University of Science and Technology, Tianjin, 300457, People's Republic of China.
Chao LiKey Laboratory of Industrial Fermentation Microbiology of the Ministry of Education, Tianjin Key Laboratory of Industrial Microbiology, College of Biotechnology, National Engineering Laboratory for Industrial Enzymes, Tianjin University of Science and Technology, Tianjin, 300457, People's Republic of China.
Ying ChenKey Laboratory of Industrial Fermentation Microbiology of the Ministry of Education, Tianjin Key Laboratory of Industrial Microbiology, College of Biotechnology, National Engineering Laboratory for Industrial Enzymes, Tianjin University of Science and Technology, Tianjin, 300457, People's Republic of China.
Menglu ZhuKey Laboratory of Industrial Fermentation Microbiology of the Ministry of Education, Tianjin Key Laboratory of Industrial Microbiology, College of Biotechnology, National Engineering Laboratory for Industrial Enzymes, Tianjin University of Science and Technology, Tianjin, 300457, People's Republic of China.
Xin LiuKey Laboratory of Industrial Fermentation Microbiology of the Ministry of Education, Tianjin Key Laboratory of Industrial Microbiology, College of Biotechnology, National Engineering Laboratory for Industrial Enzymes, Tianjin University of Science and Technology, Tianjin, 300457, People's Republic of China.
Masaru TanokuraKey Laboratory of Industrial Fermentation Microbiology of the Ministry of Education, Tianjin Key Laboratory of Industrial Microbiology, College of Biotechnology, National Engineering Laboratory for Industrial Enzymes, Tianjin University of Science and Technology, Tianjin, 300457, People's Republic of China. amtanok@mail.ecc.u-tokyo.ac.jp.
Hui-Min QinKey Laboratory of Industrial Fermentation Microbiology of the Ministry of Education, Tianjin Key Laboratory of Industrial Microbiology, College of Biotechnology, National Engineering Laboratory for Industrial Enzymes, Tianjin University of Science and Technology, Tianjin, 300457, People's Republic of China. huiminqin@tust.edu.cn.
Fuping LuKey Laboratory of Industrial Fermentation Microbiology of the Ministry of Education, Tianjin Key Laboratory of Industrial Microbiology, College of Biotechnology, National Engineering Laboratory for Industrial Enzymes, Tianjin University of Science and Technology, Tianjin, 300457, People's Republic of China. lfp@tust.edu.cn.
Tianjin University of Science and Technology · CN

Funding

National Natural Science Foundation of China 31771911
6 · The paper itself

Abstract

backgroundA novel D-allulose 3-epimerase from Staphylococcus aureus (SaDAE) has been screened as a D-allulose 3-epimerase family enzyme based on its high specificity for D-allulose. It usually converts both D-fructose and D-tagatose to respectively D-allulose and D-sorbose. We targeted potential biocatalysts for the large-scale industrial production of rare sugars.

resultsSaDAE showed a high activity on D-allulose with an affinity of 41.5 mM and catalytic efficiency of 1.1 s

conclusionsWe redesigned SaDAE for thermostability and biocatalytic production of D-allulose. The research will aid the development of industrial biocatalysts for D-allulose.

Indexed as

Carbohydrate EpimerasesMetabolic EngineeringStaphylococcus aureusBacterial ProteinsFructoseHydrogen-Ion ConcentrationKineticsSubstrate SpecificityBacterial ProteinsCarbohydrate EpimerasesFructosepsicoseD-Allulose 3-epimeraseSite-directed saturation mutagenesisStructural analysisThermostabilityTIM-barrel fold

Identifiers

PMID30909913
PMCPMC6432756
OpenAlexW2936313965

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.