Evidence map›Paper›PMID 33910612›Full record

ArticleBiotechnology for biofuels2021

Effect of solid loading on the behaviour of pectin-degrading enzymes.

Fan Li, Loïc Foucat, Estelle Bonnin

Open access · goldAbstract read
In one paragraph

Article in Biotechnology for biofuels, 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
2.7field-weighted citation impact, top 11% 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, 18 citations in OpenAlex.

  1. Review
  2. Article
  3. 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

3 authors at 2 institutions in 4 countries.

Fan LiINRAE, UR 1268, Biopolymers Interactions Assemblies BIA, F-44316, Nantes, France.
Loïc FoucatINRAE, UR 1268, Biopolymers Interactions Assemblies BIA, F-44316, Nantes, France.
Estelle BonninINRAE, UR 1268, Biopolymers Interactions Assemblies BIA, F-44316, Nantes, France. estelle.bonnin@inrae.fr.ORCID http://orcid.org/0000-0002-8268-9408
Institut National de Recherche pour l'Agriculture, l'Alimentation et l'Environnement · FRCity College of New York · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundPectin plays a role in the recalcitrance of plant biomass by affecting the accessibility of other cell wall components to enzymatic degradation. Elimination of pectin consequently has a positive impact on the saccharification of pectin-rich biomass. This work thus focused on the behaviour of different pectin-degrading enzymes in the presence of low (5%) to high (35%) solid loading of lemon peel.

resultsHigh solid loading of lemon peel affected pectin solubilisation differently depending on the pectinase used. Pectin lyase was less sensitive to a reduction of water content than was a mixture of endopolygalacturonase and pectin methylesterase, regardless of whether or not the latter's mode of action is processive or not. Marked changes in water mobility were observed along with enzymatic degradation depending on the enzyme used. However, the pectin lyase resulted in less pronounced shifts in water distribution than polygalacturonase-pectin methylesterase mixtures. At similar pectin concentration, pectin solutions hindered the diffusion of hydrolases more than the solid substrate. This can be attributed to the high viscosity of the highly concentrated pectin solutions while the solid substrate may provide continuous diffusion paths through pores.

conclusionsThe increase in solid substrate loading reduced the efficiency of pectin-degrading enzymes catalysing hydrolysis more significantly than those catalysing β-elimination. LF-NMR experiments highlighted the impact of solid loading on water mobility. Compared to other enzymes and whatever the solid loading, pectin lyase led to longer relaxation times linked with the most destructuration of the solid substrate. This new information could benefit the biorefinery processing of pectin-rich plant material when enzymes are used in the treatment.

Indexed as

Glycoside hydrolasesHigh-solids loadingPectin lyasePolygalacturonaseWater mobility

Identifiers

PMID33910612
PMCPMC8082855
OpenAlexW3157967996

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.