Evidence map›Paper›PMID 26846788›Full record

ArticleMicrobial cell factories2016

New approaches to achieve high level enzyme production in Streptomyces lividans.

Laura Sevillano, Erik Vijgenboom, Gilles P van Wezel, Margarita Díaz, Ramón I Santamaría

Open access · goldAbstract read
In one paragraph

Article in Microbial cell factories, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
6.1field-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

21 citing papers in PubMed, 56 citations in OpenAlex.

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  14. Frontiers in bioengineering and biotechnology · 2021
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  18. Germination and Growth Analysis ofFrontiers in microbiology · 2018
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  19. Characterization of Sigma Factor Genes inFrontiers in microbiology · 2018
    Article
  20. Article
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 3 institutions in 2 countries.

Laura SevillanoInstituto de Biología Funcional y Genómica/Departamento de Microbiología y Genética, Consejo Superior de Investigaciones Científicas (CSIC)/Universidad de Salamanca, C/Zacarías González nº 2, 37007, Salamanca, Spain. laura.sevillano@usal.es.
Erik VijgenboomMolecular Biotechnology, IBL, Sylvius Laboratory, Leiden University, Leiden, The Netherlands. vijgenbo@biology.leidenuniv.nl.
Gilles P van WezelMolecular Biotechnology, IBL, Sylvius Laboratory, Leiden University, Leiden, The Netherlands. g.wezel@biology.leidenuniv.nl.
Margarita DíazInstituto de Biología Funcional y Genómica/Departamento de Microbiología y Genética, Consejo Superior de Investigaciones Científicas (CSIC)/Universidad de Salamanca, C/Zacarías González nº 2, 37007, Salamanca, Spain. mardi@usal.es.
Ramón I SantamaríaInstituto de Biología Funcional y Genómica/Departamento de Microbiología y Genética, Consejo Superior de Investigaciones Científicas (CSIC)/Universidad de Salamanca, C/Zacarías González nº 2, 37007, Salamanca, Spain. santa@usal.es.
Instituto de Biología Funcional y Genómica · ESLeiden University · NLConsejo Superior de Investigaciones Científicas · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundActinomycetes are saprophytic soil bacteria, and a rich source of industrial enzymes. While some of these enzymes can be produced using well-characterized production platforms such as Escherichia coli or Bacillus subtilis, Streptomyces lividans may be the preferred host for proper folding and efficient secretion of active enzymes. A combination of promoters, signal peptides and hosts were tested in order to obtain the best protein expression in this actinomycete. The xylanase, Xys1, from S. halstedii, the α-amylase, Amy, from S. griseus and the small laccase, SLAC, from S. coelicolor were used as reporters.

resultsThe promoters xysAp from S. halstedii JM8 and pstSp from S. lividans were the most efficient among those tested. An improvement of 17 % was obtained in xylanase activity when the signal peptide of the α-amylase protein (Amy) of S. griseus IMRU3570 was used to direct its secretion. Enhanced expression of SsgA, a protein that plays a role in processes that require cell-wall remodelling, resulted in a improvement of 40 and 70 % of xylanase and amylase production, respectively. Deletion of genes SLI7232 and SLI4452 encoding putative repressors of xysAp provided improvement of production up to 70 % in the SLI7232 deletion strain. However, full derepression of this promoter activity was not obtained under the conditions assayed.

conclusionsStreptomyces lividans is a frequently used platform for industrial enzyme production and a rational strain-development approach delivered significant improvement of protein production by this host.

Indexed as

AmylasesBacterial ProteinsGene DeletionGenetic EngineeringPlasmidsPromoter Regions, GeneticProtein Sorting SignalsProtein TransportRepressor ProteinsStreptomyces lividansXylosidasesAmylasesBacterial ProteinsProtein Sorting SignalsRepressor ProteinsXylosidases

Identifiers

PMID26846788
PMCPMC4743123
OpenAlexW2266839951

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.