Evidence map›Paper›PMID 38245740›Full record

ReviewMicrobial cell factories2024

Chitinous material bioconversion by three new chitinases from the yeast Mestchnikowia pulcherrima.

Marina Minguet-Lobato, Fadia V Cervantes, Noa Míguez, Francisco J Plou, María Fernández-Lobato

Open access · goldAbstract readReview
In one paragraph

Review in Microbial cell factories, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
2.8field-weighted citation impact, top 10% 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

9 citing papers in PubMed, 12 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Biochemical analyses of a new GH18 chitinase fromApplied and environmental microbiology · 2025
    Article
  6. Article
  7. Article
  8. Potential ofFrontiers in microbiology · 2025
    Review
  9. 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

5 authors at 3 institutions in 1 country.

Marina Minguet-LobatoDepartment of Molecular Biology, Centre for Molecular Biology Severo Ochoa (CBMSO, CSIC-UAM), University Autonomous from Madrid, C/ Nicolás Cabrera, 1. Cantoblanco, Madrid, 28049, Spain.
Fadia V CervantesInstitute of Catalysis and Petrochemistry, CSIC. C/ Marie Curie, 2. Cantoblanco, Madrid, 28049, Spain.
Noa MíguezInstitute of Catalysis and Petrochemistry, CSIC. C/ Marie Curie, 2. Cantoblanco, Madrid, 28049, Spain.
Francisco J PlouInstitute of Catalysis and Petrochemistry, CSIC. C/ Marie Curie, 2. Cantoblanco, Madrid, 28049, Spain. fplou@icp.csic.es.
María Fernández-LobatoDepartment of Molecular Biology, Centre for Molecular Biology Severo Ochoa (CBMSO, CSIC-UAM), University Autonomous from Madrid, C/ Nicolás Cabrera, 1. Cantoblanco, Madrid, 28049, Spain. mfernandez@cbm.csic.es.
Instituto de Catálisis y Petroleoquímica · ESCentro de Biología Molecular Severo Ochoa · ESUniversidad Autónoma de Madrid · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundChitinases are widely distributed enzymes that perform the biotransformation of chitin, one of the most abundant polysaccharides on the biosphere, into useful value-added chitooligosaccharides (COS) with a wide variety of biotechnological applications in food, health, and agricultural fields. One of the most important group of enzymes involved in the degradation of chitin comprises the glycoside hydrolase family 18 (GH18), which harbours endo- and exo-enzymes that act synergistically to depolymerize chitin. The secretion of a chitinase activity from the ubiquitous yeast Mestchnikowia pulcherrima and their involvement in the post-harvest biological control of fungal pathogens was previously reported.

resultsThree new chitinases from M. pulcherrima, MpChit35, MpChit38 and MpChit41, were molecularly characterized and extracellularly expressed in Pichia pastoris to about 91, 90 and 71 mU ml

conclusionsThree new chitinases from the yeast M. pulcherrima were molecularly characterized and their enzymatic and structural characteristics analysed. These enzymes transformed chitinous materials to fully and partially acetylated COS through different modes of splitting, which make them interesting biocatalysts for deeper structural-function studies on the challenging enzymatic conversion of chitin.

Indexed as

ChitinasesChitosanChitinProteinsSaccharomyces cerevisiaeChitinChitinasesChitosanProteinsBiotransformationChitinChitinaseChitin wastesChitooligosaccharidesChitosanGH18Mestchnikowia

Identifiers

PMID38245740
PMCPMC10799394
OpenAlexW4391051814

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.