Evidence map›Paper›PMID 26510006›Full record

ArticlePloS one2015

Displaying Lipase B from Candida antarctica in Pichia pastoris Using the Yeast Surface Display Approach: Prospection of a New Anchor and Characterization of the Whole Cell Biocatalyst.

Marcelo Victor Holanda Moura, Giulia Pontes da Silva, Antônio Carlos de Oliveira Machado, Fernando Araripe Gonçalves Torres, Denise Maria Guimarães Freire, Rodrigo Volcan Almeida

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

7 citing papers in PubMed, 43 citations in OpenAlex.

  1. Review
  2. Article
  3. Frontiers in microbiology · 2022
    Article
  4. Cell-surface engineering of yeasts for whole-cell biocatalysts.Bioprocess and biosystems engineering · 2021
    Review
  5. Review
  6. Review
  7. 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.

Marcelo Victor Holanda MouraInstituto de Química, Universidade Federal do Rio de Janeiro, Rio de Janeiro, RJ, Brasil.
Giulia Pontes da SilvaInstituto de Química, Universidade Federal do Rio de Janeiro, Rio de Janeiro, RJ, Brasil.
Antônio Carlos de Oliveira MachadoInstituto de Química, Universidade Federal do Rio de Janeiro, Rio de Janeiro, RJ, Brasil.
Fernando Araripe Gonçalves TorresDepartamento de Biologia Celular, Universidade de Brasília, Brasília, DF, Brasil.
Denise Maria Guimarães FreireInstituto de Química, Universidade Federal do Rio de Janeiro, Rio de Janeiro, RJ, Brasil.
Rodrigo Volcan AlmeidaInstituto de Química, Universidade Federal do Rio de Janeiro, Rio de Janeiro, RJ, Brasil.
Universidade Federal do Rio de Janeiro · BRUniversidade de Brasília · BR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Yeast Surface Display (YSD) is a strategy to anchor proteins on the yeast cell wall which has been employed to increase enzyme stability thus decreasing production costs. Lipase B from Candida antarctica (LipB) is one of the most studied enzymes in the context of industrial biotechnology. This study aimed to assess the biochemical features of this important biocatalyst when immobilized on the cell surface of the methylotrophic yeast Pichia pastoris using the YSD approach. For that purpose, two anchors were tested. The first (Flo9) was identified after a prospection of the P. pastoris genome being related to the family of flocculins similar to Flo1 but significantly smaller. The second is the Protein with Internal Repeats (Pir1) from P. pastoris. An immunolocalization assay showed that both anchor proteins were able to display the reporter protein EGFP in the yeast outer cell wall. LipB was expressed in P. pastoris fused either to Flo9 (FLOLIPB) or Pir1 (PIRLIPB). Both constructions showed hydrolytic activity towards tributyrin (>100 U/mgdcw and >80 U/mgdcw, respectively), optimal hydrolytic activity around 45°C and pH 7.0, higher thermostability at 45°C and stability in organic solvents when compared to a free lipase.

Indexed as

Cell Surface Display TechniquesTwo-Hybrid System TechniquesCandidaCatalysisComputational BiologyEnzyme StabilityGene ExpressionGenes, ReporterHydrogen-Ion ConcentrationLipasePichiaTemperatureLipase

Identifiers

PMID26510006
PMCPMC4624902
OpenAlexW1863062082

What OpenQuestion holds

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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.