Evidence map›Paper›PMID 35296345›Full record

ArticleBiotechnology for biofuels and bioproducts2022

PACER: a novel 3D plant cell wall model for the analysis of non-catalytic and enzymatic responses.

Mareike Monschein, Edita Jurak, Tanja Paasela, Taru Koitto, Vera Lambauer, Mirko Pavicic, Thomas Enjalbert, Claire Dumon, Emma R Master

Open access · goldAbstract read
In one paragraph

Article in Biotechnology for biofuels and bioproducts, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.6field-weighted citation impact, top 41% 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

1 citing paper in PubMed, 7 citations in OpenAlex.

  1. Loosenin-Like Proteins fromApplied and environmental microbiology · 2023
    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 5 institutions in 4 countries.

Mareike MonscheinDepartment of Bioproducts and Biosystems, Aalto University, Kemistintie 1, 02150, Espoo, Finland.
Edita JurakDepartment of Bioproducts and Biosystems, Aalto University, Kemistintie 1, 02150, Espoo, Finland.
Tanja PaaselaDepartment of Agricultural Sciences, Viikki Plant Science Centre, University of Helsinki, P.O. Box 27, 00014, Helsinki, Finland.
Taru KoittoDepartment of Bioproducts and Biosystems, Aalto University, Kemistintie 1, 02150, Espoo, Finland.
Vera LambauerDepartment of Bioproducts and Biosystems, Aalto University, Kemistintie 1, 02150, Espoo, Finland.
Mirko PavicicDepartment of Agricultural Sciences, Viikki Plant Science Centre, University of Helsinki, P.O. Box 27, 00014, Helsinki, Finland.
Thomas EnjalbertToulouse Biotechnology Institute (TBI), Université de Toulouse, CNRS, INRAE, INSA, 31077, Toulouse, France.
Claire DumonToulouse Biotechnology Institute (TBI), Université de Toulouse, CNRS, INRAE, INSA, 31077, Toulouse, France.
Emma R MasterDepartment of Bioproducts and Biosystems, Aalto University, Kemistintie 1, 02150, Espoo, Finland. emma.master@aalto.fi.ORCID http://orcid.org/0000-0002-6837-9817
Aalto University · FICentre National de la Recherche Scientifique · FRUniversity of Helsinki · FIUniversity of Groningen · NLUniversity of Toronto · CA

Funding

Agence Nationale de la Recherche ANR-18-CES43-DECOH2020 European Research Council 648925
6 · The paper itself

Abstract

backgroundSubstrate accessibility remains a key limitation to the efficient enzymatic deconstruction of lignocellulosic biomass. Limited substrate accessibility is often addressed by increasing enzyme loading, which increases process and product costs. Alternatively, considerable efforts are underway world-wide to identify amorphogenesis-inducing proteins and protein domains that increase the accessibility of carbohydrate-active enzymes to targeted lignocellulose components.

resultsWe established a three-dimensional assay, PACER (plant cell wall model for the analysis of non-catalytic and enzymatic responses), that enables analysis of enzyme migration through defined lignocellulose composites. A cellulose/azo-xylan composite was made to demonstrate the PACER concept and then used to test the migration and activity of multiple xylanolytic enzymes. In addition to non-catalytic domains of xylanases, the potential of loosenin-like proteins to boost xylanase migration through cellulose/azo-xylan composites was observed.

conclusionsThe PACER assay is inexpensive and parallelizable, suitable for screening proteins for ability to increase enzyme accessibility to lignocellulose substrates. Using the PACER assay, we visualized the impact of xylan-binding modules and loosenin-like proteins on xylanase mobility and access to targeted substrates. Given the flexibility to use different composite materials, the PACER assay presents a versatile platform to study impacts of lignocellulose components on enzyme access to targeted substrates.

Indexed as

AmorphogenesisAssay developmentEnzyme accessibilityLignocelluloseLooseninXylanXylanase

Identifiers

PMID35296345
PMCPMC8928621
OpenAlexW4220982841

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.