Evidence map›Paper›PMID 39115691›Full record

ArticleBioprocess and biosystems engineering2024

Recombinant expression and characterization of the endochitinase Chit36-TA from Trichoderma asperellum in Komagataella phaffii for chitin degradation of black soldier fly exuviae.

Luisa Gebele, Andreas Wilke, Axel Salliou, Laura Schneider, Daniel Heid, Tobias Stadelmann, Corinna Henninger, Uzair Ahmed, Melanie Broszat, Pascale Müller and 4 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Bioprocess and biosystems engineering, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed, 1 pooled it
–field-weighted citation impact
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

2 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Review
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

14 authors.

Luisa GebeleFaculty of Mechanical and Process Engineering, Hochschule Offenburg, 77652, Offenburg, Germany.
Andreas WilkeFaculty of Mechanical and Process Engineering, Hochschule Offenburg, 77652, Offenburg, Germany.
Axel SalliouÉcole Supérieure de Biotechnologie de Strasbourg, 67412, Illkirch Cedex, France.
Laura SchneiderDepartment Life Sciences and Engineering, Technische Hochschule Bingen, 55411, Bingen am Rhein, Germany.
Daniel HeidFaculty of Mechanical and Process Engineering, Hochschule Offenburg, 77652, Offenburg, Germany.
Tobias StadelmannFaculty of Mechanical and Process Engineering, Hochschule Offenburg, 77652, Offenburg, Germany.
Corinna HenningerFaculty of Mechanical and Process Engineering, Hochschule Offenburg, 77652, Offenburg, Germany.
Uzair AhmedFaculty of Mechanical and Process Engineering, Hochschule Offenburg, 77652, Offenburg, Germany.
Melanie BroszatFaculty of Mechanical and Process Engineering, Hochschule Offenburg, 77652, Offenburg, Germany.
Pascale MüllerFaculty of Mechanical and Process Engineering, Hochschule Offenburg, 77652, Offenburg, Germany.
Georg DuselDepartment Life Sciences and Engineering, Technische Hochschule Bingen, 55411, Bingen am Rhein, Germany.
Michał KrzyżaniakDepartment of Genetics, Plant Breeding and Bioresource Engineering, University of Warmia and Mazury in Olsztyn, Plac Łódzki 3, 10-724, Olsztyn, Poland.
Katrin OchsenreitherDepartment of Chemical and Process Engineering, Karlsruhe Institute of Technology (KIT), 76131, Karlsruhe, Germany.
Thomas EiseleFaculty of Mechanical and Process Engineering, Hochschule Offenburg, 77652, Offenburg, Germany. thomas.eisele@hs-offenburg.de.

Funding

Deutsche Forschungsgemeinschaft 466169172National Science Centre, Poland UMO-2020/39/I/NZ9/00907
6 · The paper itself

Abstract

The natural polymer chitin is an abundant source for valuable N-acetylchitooligosaccharides and N-acetylglucosamine applicable in several industries. The endochitinase Chit36-TA from Trichoderma asperellum was recombinantly expressed in Komagataella phaffii for the enzymatic degradation of chitin from unused insect exuviae into N-acetylchitooligosaccharides. Chit36-TA was purified by Ni-NTA affinity chromatography and subsequently biochemically characterized. After deglycosylation, the endochitinase had a molecular weight of 36 kDa. The optimum pH for Chit36-TA was 4.5. The temperature maximum of Chit36-TA was determined to be 50 °C, while it maintained > 93% activity up to 60 °C. The chitinase was thermostable up to 45 °C and exhibited ~ 50% activity after a 15 min incubation at 57 °C. Chit36-TA had a maximum specific enzyme activity of 50 nkat/mg with a K

Indexed as

ChitinChitinasesHypocrealesRecombinant ProteinsAnimalsFungal ProteinsHydrogen-Ion ConcentrationSaccharomycetalesSimuliidaeChitinChitinasesFungal ProteinsRecombinant ProteinsBiopolymerBlack soldier fly larvaeChitinChitinasesKomagataella phaffiiTrichoderma asperellum

Identifiers

PMID39115691
PMCPMC11399303

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.