Evidence map›Paper›PMID 33789740›Full record

ArticleBiotechnology for biofuels2021

Disulfide bond engineering of AppA phytase for increased thermostability requires co-expression of protein disulfide isomerase in Pichia pastoris.

Laura Navone, Thomas Vogl, Pawarisa Luangthongkam, Jo-Anne Blinco, Carlos H Luna-Flores, Xiaojing Chen, Juhani von Hellens, Stephen Mahler, Robert Speight

Open access · goldAbstract read
In one paragraph

Article in Biotechnology for biofuels, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
4.7field-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

20 citing papers in PubMed, 50 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Improved Thermal Stability of a Novel Acidophilic Phytase.Journal of microbiology and biotechnology · 2024
    Article
  7. Review
  8. Microorganisms · 2024
    Review
  9. COMicrobial cell factories · 2024
    Article
  10. Effect ofMolecules (Basel, Switzerland) · 2023
    Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Enhanced Thermostability of D-Psicose 3-Epimerase fromInternational journal of molecular sciences · 2021
    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

9 authors at 3 institutions in 2 countries.

Laura NavoneFaculty of Science, Queensland University of Technology, Brisbane, QLD, Australia. laura.navone@qut.edu.au.ORCID http://orcid.org/0000-0003-3672-3799
Thomas VoglDepartment of Computer Science and Applied Mathematics, Weizmann Institute of Science, Rehovot, Israel.
Pawarisa LuangthongkamFaculty of Science, Queensland University of Technology, Brisbane, QLD, Australia.
Jo-Anne BlincoFaculty of Science, Queensland University of Technology, Brisbane, QLD, Australia.
Carlos H Luna-FloresFaculty of Science, Queensland University of Technology, Brisbane, QLD, Australia.
Xiaojing ChenBioproton Pty Ltd, Brisbane, QLD, Australia.
Juhani von HellensBioproton Pty Ltd, Brisbane, QLD, Australia.
Stephen MahlerARC Training Centre for Biopharmaceutical Innovation, The University of Queensland, Brisbane, QLD, Australia.
Robert SpeightFaculty of Science, Queensland University of Technology, Brisbane, QLD, Australia.
Queensland University of Technology · AUThe University of Queensland · AUWeizmann Institute of Science · IL

Funding

Austrian Science Fund FWF J 4256
6 · The paper itself

Abstract

backgroundPhytases are widely used commercially as dietary supplements for swine and poultry to increase the digestibility of phytic acid. Enzyme development has focused on increasing thermostability to withstand the high temperatures during industrial steam pelleting. Increasing thermostability often reduces activity at gut temperatures and there remains a demand for improved phyases for a growing market.

resultsIn this work, we present a thermostable variant of the E. coli AppA phytase, ApV1, that contains an extra non-consecutive disulfide bond. Detailed biochemical characterisation of ApV1 showed similar activity to the wild type, with no statistical differences in k

conclusionsOverall, the results show that protein engineering for enhanced enzymatic properties like thermostability may result in folding complexity and decreased production in microbial systems. Hence parallel development of improved production strains is imperative to achieve the desirable levels of recombinant protein for industrial processes.

Indexed as

ChaperoneDisulfide bondFoldingPhytaseThermostability

Identifiers

PMID33789740
PMCPMC8010977
OpenAlexW3151560699

What Socratic 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 Socratic graph.