Evidence map›Paper›PMID 23700177›Full record

ArticleJournal of industrial microbiology & biotechnology2013

Construction of a starch-inducible homologous expression system to produce cellulolytic enzymes from Acremonium cellulolyticus.

Hiroyuki Inoue, Tatsuya Fujii, Miho Yoshimi, Larry E Taylor, Stephen R Decker, Seiichiro Kishishita, Makoto Nakabayashi, Kazuhiko Ishikawa

Open access · bronzeAbstract read
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In one paragraph

Article in Journal of industrial microbiology & biotechnology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
3.1field-weighted citation impact, top 9% 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

15 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
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  4. Crystal structure of GH30-7 endoxylanase C from the filamentous fungus Talaromyces cellulolyticus.Acta crystallographica. Section F, Structural biology communications · 2020
    Article
  5. GH30-7 Endoxylanase C from the Filamentous FungusApplied and environmental microbiology · 2019
    Article
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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

8 authors at 2 institutions in 2 countries.

Hiroyuki InoueBiomass Refinery Research Center, National Institute of Advanced Industrial Science and Technology (AIST), 3-11-32 Kagamiyama, Higashi-Hiroshima, Hiroshima, 739-0046, Japan. inoue-h@aist.go.jp
Tatsuya Fujii
Miho Yoshimi
Larry E Taylor
Stephen R Decker
Seiichiro Kishishita
Makoto Nakabayashi
Kazuhiko Ishikawa
National Institute of Advanced Industrial Science and Technology · JPNational Renewable Energy Laboratory · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A starch-inducible homologous expression system in Acremonium cellulolyticus was constructed to successfully produce recombinant cellulolytic enzymes. A. cellulolyticus Y-94 produced amylolytic enzymes and cellulolytic enzymes as major proteins in the culture supernatant when grown with soluble starch (SS) and Solka-Flock cellulose (SF), respectively. To isolate a strong starch-inducible promoter, glucoamylase (GlaA), which belongs to glycoside hydrolase family 15, was purified from the SS culture of Y-94, and its gene was identified in the genome sequence. The 1.4-kb promoter and 0.4-kb terminator regions of glaA were amplified by polymerase chain reaction (PCR) and used in the construction of a plasmid that drives the expression of the cellobiohydrolase I (Cel7A) gene from A. cellulolyticus. The resultant expression plasmid, containing pyrF as a selection marker, was randomly integrated into the genome of the A. cellulolyticus Y-94 uracil auxotroph. The prototrophic transformant, Y203, produced recombinant Cel7A as an extracellular protein under control of the glaA promoter in the SS culture. Recombinant and wild-type Cel7A were purified from the SS culture of Y203 and the SF culture of A. cellulolyticus CF-2612, respectively. Both enzymes were found to have the same apparent molecular weight (60 kDa), thermostability (T m 67.0 °C), and optimum pH (pH 4.5), and showed similar catalytic properties for soluble and insoluble substrates. These results suggest that the A. cellulolyticus starch-inducible expression system will be helpful for characterization and improvement of fungal cellulolytic enzymes.

Indexed as

AcremoniumCelluloseCellulose 1,4-beta-CellobiosidaseGlucan 1,4-alpha-GlucosidasePromoter Regions, GeneticRecombinant ProteinsStarchCelluloseCellulose 1,4-beta-CellobiosidaseGlucan 1,4-alpha-GlucosidaseRecombinant ProteinsStarch

Identifiers

PMID23700177
OpenAlexW2000163261

What OpenQuestion holds

Textmetadata
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.