Evidence map›Paper›PMID 18035441›Full record

ArticleJournal of biotechnology2008

Exploitation of the S-layer self-assembly system for site directed immobilization of enzymes demonstrated for an extremophilic laminarinase from Pyrococcus furiosus.

Helga Tschiggerl, Andreas Breitwieser, Guy de Roo, Theo Verwoerd, Christina Schäffer, Uwe B Sleytr

Open access · greenAbstract read
In one paragraph

Article in Journal of biotechnology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.8field-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

12 citing papers in PubMed, 56 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. S-layers: principles and applications.FEMS microbiology reviews · 2014
    Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. 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 1 institution in 1 country.

Helga TschiggerlCenter for NanoBiotechnology, University of Natural Resources and Applied Life Sciences, Gregor-Mendel-Strasse 33, A-1180 Vienna, Austria.
Andreas Breitwieser
Guy de Roo
Theo Verwoerd
Christina Schäffer
Uwe B Sleytr
BOKU University · AT

Funding

Austrian Science Fund FWF P 19047
6 · The paper itself

Abstract

A fusion protein based on the S-layer protein SbpA from Bacillus sphaericus CCM 2177 and the enzyme laminarinase (LamA) from Pyrococcus furiosus was designed and overexpressed in Escherichia coli. Due to the construction principle, the S-layer fusion protein fully retained the self-assembly capability of the S-layer moiety, while the catalytic domain of LamA remained exposed at the outer surface of the formed protein lattice. The enzyme activity of the S-layer fusion protein monolayer obtained upon recrystallization on silicon wafers, glass slides and different types of polymer membranes was determined colorimetrically and related to the activity of sole LamA that has been immobilized with conventional techniques. LamA aligned within the S-layer fusion protein lattice in a periodic and orientated fashion catalyzed twice the glucose release from the laminarin polysaccharide substrate in comparison to the randomly immobilized enzyme. In combination with the good shelf-life and the high resistance towards temperature and diverse chemicals, these novel composites are regarded a promising approach for site-directed enzyme immobilization.

Indexed as

Archaeal ProteinsBiotechnologyCatalysisCellulaseCross-Linking ReagentsCrystallizationEnzymes, ImmobilizedEnzyme StabilityMembrane GlycoproteinsMembranes, ArtificialPyrococcus furiosusRecombinant Fusion ProteinsTemperatureArchaeal ProteinsCellulaseCross-Linking ReagentsEnzymes, ImmobilizedMembrane GlycoproteinsMembranes, ArtificialRecombinant Fusion ProteinsS-layer proteins

Identifiers

PMID18035441
PMCPMC4396859
OpenAlexW2053117925

What OpenQuestion holds

Textmetadata
LicenceTDM
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.