Evidence map›Paper›PMID 34720466›Full record

ArticleCellulose (London, England)2021

Non-productive binding of cellobiohydrolase i investigated by surface plasmon resonance spectroscopy.

Florian Csarman, Claudia Gusenbauer, Lena Wohlschlager, Gijs van Erven, Mirjam A Kabel, Johannes Konnerth, Antje Potthast, Roland Ludwig

Open access · hybridAbstract read
In one paragraph

Article in Cellulose (London, England), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.6field-weighted citation impact, top 37% 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

3 citing papers in PubMed, 8 citations in OpenAlex.

  1. Article
  2. Article
  3. 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

8 authors at 2 institutions in 2 countries.

Florian CsarmanDepartment of Food Science and Technology, Biocatalysis and Biosensing Laboratory, BOKU University of Natural Resources and Life Sciences, Muthgasse 18, 1190 Vienna, Austria.
Claudia GusenbauerDepartment of Materials Sciences and Process Engineering, Institute of Wood Technology and Renewable Materials, BOKU - University of Natural Resources and Life Sciences, Konrad-Lorenz-Straße 24, 3430 Tulln, Austria.
Lena WohlschlagerDepartment of Food Science and Technology, Biocatalysis and Biosensing Laboratory, BOKU University of Natural Resources and Life Sciences, Muthgasse 18, 1190 Vienna, Austria.
Gijs van ErvenLaboratory of Food Chemistry, Wageningen University and Research, Bornse Weilanden 9, 6708 WG Wageningen, The Netherlands.
Mirjam A KabelLaboratory of Food Chemistry, Wageningen University and Research, Bornse Weilanden 9, 6708 WG Wageningen, The Netherlands.
Johannes KonnerthDepartment of Materials Sciences and Process Engineering, Institute of Wood Technology and Renewable Materials, BOKU - University of Natural Resources and Life Sciences, Konrad-Lorenz-Straße 24, 3430 Tulln, Austria.
Antje PotthastDepartment of Chemistry, Division of Chemistry of Renewable Resources, BOKU - University of Natural Resources and Life Sciences, Konrad-Lorenz-Straße 24, 3430 Tulln, Austria.
Roland LudwigDepartment of Food Science and Technology, Biocatalysis and Biosensing Laboratory, BOKU University of Natural Resources and Life Sciences, Muthgasse 18, 1190 Vienna, Austria.ORCID 0000-0002-5058-5874
BOKU University · ATWageningen University & Research · NL

Funding

European Research Council 726396
6 · The paper itself

Abstract

Future biorefineries are facing the challenge to separate and depolymerize biopolymers into their building blocks for the production of biofuels and basic molecules as chemical stock. Fungi have evolved lignocellulolytic enzymes to perform this task specifically and efficiently, but a detailed understanding of their heterogeneous reactions is a prerequisite for the optimization of large-scale enzymatic biomass degradation. Here, we investigate the binding of cellulolytic enzymes onto biopolymers by surface plasmon resonance (SPR) spectroscopy for the fast and precise characterization of enzyme adsorption processes. Using different sensor architectures, SPR probes modified with regenerated cellulose as well as with lignin films were prepared by spin-coating techniques. The modified SPR probes were analyzed by atomic force microscopy and static contact angle measurements to determine physical and surface molecular properties. SPR spectroscopy was used to study the activity and affinity of SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1007/s10570-021-04002-6.

Indexed as

Biomass hydrolysisCellobiohydrolaseGlycosylationLigninNon-productive bindingSurface plasmon resonance

Identifiers

PMID34720466
PMCPMC8550311
OpenAlexW3193796982

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.