Evidence map›Paper›PMID 30971250›Full record

ArticleMicrobial cell factories2019

Enhanced extracellular expression of Bacillus stearothermophilus α-amylase in Bacillus subtilis through signal peptide optimization, chaperone overexpression and α-amylase mutant selection.

Dongbang Yao, Lingqia Su, Na Li, Jing Wu

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 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
8.3field-weighted citation impact, top 2% 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

39 citing papers in PubMed, 105 citations in OpenAlex.

  1. Review
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  8. Efficient expression of a novelFrontiers in microbiology · 2025
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  11. Display of Lignin Peroxidase on the Surface of Bacillus subtilis.Applied biochemistry and biotechnology · 2024
    Article
  12. Article
  13. The Construction of an Environmentally Friendly Super-Secreting Strain ofInternational journal of molecular sciences · 2024
    Article
  14. Article
  15. Microorganisms · 2024
    Review
  16. 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

4 authors at 1 institution in 1 country.

Dongbang YaoState Key Laboratory of Food Science and Technology, Jiangnan University, 1800 Lihu Avenue, Wuxi, 214122, Jiangsu, China.
Lingqia SuState Key Laboratory of Food Science and Technology, Jiangnan University, 1800 Lihu Avenue, Wuxi, 214122, Jiangsu, China.
Na LiState Key Laboratory of Food Science and Technology, Jiangnan University, 1800 Lihu Avenue, Wuxi, 214122, Jiangsu, China.
Jing WuState Key Laboratory of Food Science and Technology, Jiangnan University, 1800 Lihu Avenue, Wuxi, 214122, Jiangsu, China. jingwu@jiangnan.edu.cn.ORCID http://orcid.org/0000-0002-6591-0529
Jiangnan University · CN

Funding

111 Project No. 111-2-06China National Funds for Distinguished Young Scientists 31425020national first-class discipline program of Light Industry Technology and Engineering LITE2018-03National Natural Science Foundation of China 31730067Natural Science Foundation of Jiangsu Province BK20180082
6 · The paper itself

Abstract

backgroundOur laboratory has constructed a Bacillus stearothermophilus α-amylase (AmyS) derivative with excellent enzymatic properties. Bacillus subtilis is generally regarded as safe and has excellent protein secretory capability, but heterologous extracellular production level of B. stearothermophilus α-amylase in B. subtilis is very low.

resultsIn this study, the extracellular production level of B. stearothermophilus α-amylase in B. subtilis was enhanced by signal peptide optimization, chaperone overexpression and α-amylase mutant selection. The α-amylase optimal signal peptide (SP

conclusionsThis is the first report that describes an improvement of B. stearothermophilus α-amylase extracellular production levels in B. subtilis using these strategies, and this represents the highest extracellular production level ever reported for α-amylase from B. stearothermophilus in B. subtilis. This high-level production provides a basis for enhanced industrial production of α-amylase. These extracellular production level improvement approaches are also expected to be valuable in the expression of other enzymes in B. subtilis.

Indexed as

Protein Sorting Signalsalpha-AmylasesBacillus subtilisBacterial ProteinsFermentationGene ExpressionGeobacillus stearothermophilusIndustrial MicrobiologyMolecular ChaperonesMutationPromoter Regions, Geneticalpha-AmylasesBacterial ProteinsMolecular ChaperonesProtein Sorting SignalsAlpha-amylaseChaperoneHigh-cell-density fermentationMutantSignal peptide

Identifiers

PMID30971250
PMCPMC6458788
OpenAlexW2946196249

What OpenQuestion holds

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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.