Evidence map›Paper›PMID 23587421›Full record

ArticleMicrobial cell factories2013

Thermal adaptability of Kluyveromyces marxianus in recombinant protein production.

Stefano Raimondi, Elena Zanni, Alberto Amaretti, Claudio Palleschi, Daniela Uccelletti, Maddalena Rossi

Open access · goldAbstract read
In one paragraph

Article in Microbial cell factories, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

14 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
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  3. High-level expression of leghemoglobin inFrontiers in bioengineering and biotechnology · 2023
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  6. Establishment ofJournal of fungi (Basel, Switzerland) · 2021
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  9. The Model SystemLife (Basel, Switzerland) · 2020
    Review
  10. Article
  11. Enzymatic hydrolysis ofBiotechnology reports (Amsterdam, Netherlands) · 2019
    Article
  12. Article
  13. Article
  14. 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

6 authors at 2 institutions in 1 country.

Stefano RaimondiDepartment of Life Sciences, University of Modena and Reggio Emilia, Modena, Italy.
Elena Zanni
Alberto Amaretti
Claudio Palleschi
Daniela Uccelletti
Maddalena Rossi
Sapienza University of Rome · ITUniversity of Modena and Reggio Emilia · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundKluyveromyces marxianus combines the ease of genetic manipulation and fermentation with the ability to efficiently secrete high molecular weight proteins, performing eukaryotic post-translational modifications. It is able to grow efficiently in a wide range of temperatures. The secretion performances were analyzed in the host K. marxianus L3 in the range between 5°C and 40°C by means of 3 different reporter proteins, since temperature appears a key parameter for production and secretion of recombinant proteins.

resultsThe recombinant strains were able to grow up to 40°C and, along the tested temperature interval (5-40°C), the specific growth rates (μ) were generally lower as compared to those of the untransformed strain. Biomass yields were slightly affected by temperature, with the highest values reached at 15°C and 30°C. The secretion of the endogenous β-fructofuranosidase, used as an internal control, was efficient in the range of the tested temperature, as evaluated by assaying the enzyme activity in the culture supernatants. The endogenous β-fructofuranosidase production was temperature dependent, with the highest yield at 30°C. The heterologous proteins HSA, GAA and Sod1p were all successfully produced and secreted between 5°C and 40°C, albeit each one presented a different optimal production temperature (15, 40, 5-30°C for HSA, GAA and Sod1p, respectively).

conclusionsK. marxianus L3 has been identified as a promising and flexible cell factory. In a sole host, the optimization of growth temperatures for the efficient secretion of each individual protein can be carried out over a wide range of temperatures.

Indexed as

beta-FructofuranosidaseBiomassGlucan 1,4-alpha-GlucosidaseHumansKluyveromycesRecombinant ProteinsSerum AlbuminSuperoxide DismutaseSuperoxide Dismutase-1Temperaturebeta-FructofuranosidaseGlucan 1,4-alpha-GlucosidaseRecombinant ProteinsSerum AlbuminSOD1 protein, humanSuperoxide DismutaseSuperoxide Dismutase-1

Identifiers

PMID23587421
PMCPMC3655038
OpenAlexW2095903673

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.