Evidence map›Paper›PMID 33282856›Full record

ArticleFrontiers in bioengineering and biotechnology2020

Enhancing Enzyme-Mediated Cellulose Hydrolysis by Incorporating Acid Groups Onto the Lignin During Biomass Pretreatment.

Jie Wu, Richard P Chandra, Masatsugu Takada, Li-Yang Liu, Scott Renneckar, Kwang Ho Kim, Chang Soo Kim, Jack N Saddler

Erratum issuedAbstract read
In one paragraph

Article in Frontiers in bioengineering and biotechnology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–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

4 citing papers in PubMed.

  1. Article
  2. Transcriptome Analysis of PostharvestFoods (Basel, Switzerland) · 2026
    Article
  3. Article
  4. Surfactant-assisted alkaline pretreatment and enzymatic hydrolysis ofFrontiers in bioengineering and biotechnology · 2022
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors.

Jie WuForest Product Biotechnology/Bioenergy Group, Department of Wood Science, Faculty of Forestry, University of British Columbia, Vancouver, BC, Canada.
Richard P ChandraForest Product Biotechnology/Bioenergy Group, Department of Wood Science, Faculty of Forestry, University of British Columbia, Vancouver, BC, Canada.
Masatsugu TakadaForest Product Biotechnology/Bioenergy Group, Department of Wood Science, Faculty of Forestry, University of British Columbia, Vancouver, BC, Canada.
Li-Yang LiuAdvanced Renewable Materials Lab, Department of Wood Science, Faculty of Forestry, University of British Columbia, Vancouver, BC, Canada.
Scott RenneckarAdvanced Renewable Materials Lab, Department of Wood Science, Faculty of Forestry, University of British Columbia, Vancouver, BC, Canada.
Kwang Ho KimClean Energy Research Center, Korea Institute of Science and Technology, Seoul, South Korea.
Chang Soo KimClean Energy Research Center, Korea Institute of Science and Technology, Seoul, South Korea.
Jack N SaddlerForest Product Biotechnology/Bioenergy Group, Department of Wood Science, Faculty of Forestry, University of British Columbia, Vancouver, BC, Canada.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lignin is known to limit the enzyme-mediated hydrolysis of biomass by both restricting substrate swelling and binding to the enzymes. Pretreated mechanical pulp (MP) made from Aspen wood chips was incubated with either 16% sodium sulfite or 32% sodium percarbonate to incorporate similar amounts of sulfonic and carboxylic acid groups onto the lignin (60 mmol/kg substrate) present in the pulp without resulting in significant delignification. When Simon's stain was used to assess potential enzyme accessibility to the cellulose, it was apparent that both post-treatments enhanced accessibility and cellulose hydrolysis. To further elucidate how acid group addition might influence potential enzyme binding to lignin, Protease Treated Lignin (PTL) was isolated from the original and modified mechanical pulps and added to a cellulose rich, delignified Kraft pulp. As anticipated, the PTLs from both the oxidized and sulfonated substrates proved less inhibitory and adsorbed less enzymes than did the PTL derived from the original pulp. Subsequent analyses indicated that both the sulfonated and oxidized lignin samples contained less phenolic hydroxyl groups, resulting in enhanced hydrophilicity and a more negative charge which decreased the non-productive binding of the cellulase enzymes to the lignin.

Indexed as

cellulase enzymesligninnon-productive bindingoxidationpHsulfonation

Identifiers

PMID33282856
PMCPMC7691530

What OpenQuestion holds

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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.