Evidence map›Paper›PMID 38523202›Full record

ArticleBiotechnology letters2024

Computer-aided rational design strategy based on protein surface charge to improve the thermal stability of a novel esterase from Geobacillus jurassicus.

Runfei Song, Jin Zhang, Mengyu Zhu, Lin Lin, Wei Wei, Dongzhi Wei

Abstract read
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In one paragraph

Article in Biotechnology letters, 2024. 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
0.5field-weighted citation impact, top 38% 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

0 citing papers in PubMed, 2 citations in OpenAlex.

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

6 authors at 2 institutions in 1 country.

Runfei SongState Key Laboratory of Bioreactor Engineering, Newworld Institute of Biotechnology, East China University of Science and Technology, 130 Meilong Road, 200237, Shanghai, People's Republic of China.
Jin ZhangState Key Laboratory of Bioreactor Engineering, Newworld Institute of Biotechnology, East China University of Science and Technology, 130 Meilong Road, 200237, Shanghai, People's Republic of China.
Mengyu ZhuState Key Laboratory of Bioreactor Engineering, Newworld Institute of Biotechnology, East China University of Science and Technology, 130 Meilong Road, 200237, Shanghai, People's Republic of China.
Lin LinSchool of Chemical and Environmental Engineering, Shanghai Institute of Technology, Shanghai, 201418, People's Republic of China.
Wei WeiState Key Laboratory of Bioreactor Engineering, Newworld Institute of Biotechnology, East China University of Science and Technology, 130 Meilong Road, 200237, Shanghai, People's Republic of China. weiwei@ecust.edu.cn.ORCID http://orcid.org/0000-0002-7613-2021
Dongzhi WeiState Key Laboratory of Bioreactor Engineering, Newworld Institute of Biotechnology, East China University of Science and Technology, 130 Meilong Road, 200237, Shanghai, People's Republic of China.
East China University of Science and Technology · CNNational Engineering Research Center for Nanotechnology · CN

Funding

Key Technologies Research and Development Program 2021YFC2100300Shanghai Institute of Technology's collaborative innovation fundation 10120K228051Shanghai Institute of Technology's scientific research start funds 10120K226107Shanghai Natural Science Foundation No. 20ZR1415400
6 · The paper itself

Abstract

objectivesAlthough Geobacillus are significant thermophilic bacteria source, there are no reports of thermostable esterase gene in Geobacillus jurassicus or rational design strategies to increase the thermal stability of esterases.

resultsGene gju768 showed a highest similarity of 15.20% to esterases from Geobacillus sp. with detail enzymatic properties. Using a combination of Gibbs Unfolding Free Energy (∆∆G) calculator and the distance from the mutation site to the catalytic site (Ds

conclusionCloning of gene gju768 and rational design based on surface charge engineering contributed to the identification of thermostable esterase from Geobacillus sp. and the exploration of evolutionary strategies for thermal stability.

Indexed as

Enzyme StabilityEsterasesGeobacillusBacterial ProteinsCloning, MolecularComputer-Aided DesignBacterial ProteinsEsterasesRational designSite-directed mutagenesisSurface charge protein engineeringThermostable esterase

Identifiers

PMID38523202
OpenAlexW4393157180

What OpenQuestion holds

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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.