Evidence map›Paper›PMID 24962396›Full record

ReviewMolecules (Basel, Switzerland)2014

Polyhydroyxalkanoate synthase fusions as a strategy for oriented enzyme immobilisation.

David O Hooks, Mark Venning-Slater, Jinping Du, Bernd H A Rehm

Open access · goldAbstract readReview
In one paragraph

Review in Molecules (Basel, Switzerland), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
2.7field-weighted citation impact, top 11% 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

11 citing papers in PubMed, 35 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. Special Issue: Enzyme Immobilization 2016.Molecules (Basel, Switzerland) · 2017
    Article
  8. Article
  9. Enzyme Engineering for In Situ Immobilization.Molecules (Basel, Switzerland) · 2016
    Review
  10. Article
  11. Editorial: Special issue--Enzyme immobilization.Molecules (Basel, Switzerland) · 2014
    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

4 authors at 2 institutions in 1 country.

David O HooksInstitute of Fundamental Sciences, Massey University, Private Bag 11222, Palmerston North 4442, New Zealand. d.o.hooks@massey.ac.nz.
Mark Venning-SlaterInstitute of Fundamental Sciences, Massey University, Private Bag 11222, Palmerston North 4442, New Zealand. m.venningslater@massey.ac.nz.
Jinping DuInstitute of Fundamental Sciences, Massey University, Private Bag 11222, Palmerston North 4442, New Zealand. j.du@massey.ac.nz.
Bernd H A RehmInstitute of Fundamental Sciences, Massey University, Private Bag 11222, Palmerston North 4442, New Zealand. b.rehm@massey.ac.nz.
Massey University · NZMacDiarmid Institute for Advanced Materials and Nanotechnology · NZ

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Polyhydroxyalkanoate (PHA) is a carbon storage polymer produced by certain bacteria in unbalanced nutrient conditions. The PHA forms spherical inclusions surrounded by granule associate proteins including the PHA synthase (PhaC). Recently, the intracellular formation of PHA granules with covalently attached synthase from Ralstonia eutropha has been exploited as a novel strategy for oriented enzyme immobilisation. Fusing the enzyme of interest to PHA synthase results in a bifunctional protein able to produce PHA granules and immobilise the active enzyme of choice to the granule surface. Functionalised PHA granules can be isolated from the bacterial hosts, such as Escherichia coli, and maintain enzymatic activity in a wide variety of assay conditions. This approach to oriented enzyme immobilisation has produced higher enzyme activities and product levels than non-oriented immobilisation techniques such as protein inclusion based particles. Here, enzyme immobilisation via PHA synthase fusion is reviewed in terms of the genetic designs, the choices of enzymes, the control of enzyme orientations, as well as their current and potential applications.

Indexed as

AcyltransferasesCorynebacterium glutamicumCupriavidus necatorEnzymes, ImmobilizedEscherichia coliLactococcus lactisMultienzyme ComplexesPolyhydroxyalkanoatesPolystyrenesProtein Structure, QuaternaryRecombinant Fusion ProteinsSubstrate SpecificityAcyltransferasesAmberlite XAD-2 resinEnzymes, ImmobilizedMultienzyme Complexespoly(3-hydroxyalkanoic acid) synthasePolyhydroxyalkanoatesPolystyrenesRecombinant Fusion Proteins

Identifiers

PMID24962396
PMCPMC6271518
OpenAlexW2058289390

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.