Evidence map›Paper›PMID 29110088›Full record

ReviewExtremophiles : life under extreme conditions2018

Carbohydrate active enzyme domains from extreme thermophiles: components of a modular toolbox for lignocellulose degradation.

Jonathan Botha, Eshchar Mizrachi, Alexander A Myburg, Don A Cowan

Abstract readReview
PubMed Publisher
In one paragraph

Review in Extremophiles : life under extreme conditions, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing 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

8 citing papers in PubMed.

  1. Extremophiles in a changing world.Extremophiles : life under extreme conditions · 2024
    Review
  2. Article
  3. Unveiling lignocellulolytic trait of a goat omasum inhabitant Klebsiella variicola strain HSTU-AAM51 in light of biochemical and genome analyses.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2022
    Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. 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

4 authors.

Jonathan BothaDepartment of Genetics, Centre for Microbial Ecology and Genomics, University of Pretoria, Private Bag X20, Pretoria, 0028, South Africa.
Eshchar MizrachiDepartment of Genetics, University of Pretoria, Private Bag X20, Pretoria, 0028, South Africa.
Alexander A MyburgDepartment of Genetics, University of Pretoria, Private Bag X20, Pretoria, 0028, South Africa.
Don A CowanDepartment of Genetics, Centre for Microbial Ecology and Genomics, University of Pretoria, Private Bag X20, Pretoria, 0028, South Africa. Don.Cowan@up.ac.za.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lignocellulosic biomass is a promising feedstock for the manufacture of biodegradable and renewable bioproducts. However, the complex lignocellulosic polymeric structure of woody tissue is difficult to access without extensive industrial pre-treatment. Enzyme processing of partly depolymerised biomass is an established technology, and there is evidence that high temperature (extremely thermophilic) lignocellulose degrading enzymes [carbohydrate active enzymes (CAZymes)] may enhance processing efficiency. However, wild-type thermophilic CAZymes will not necessarily be functionally optimal under industrial pre-treatment conditions. With recent advances in synthetic biology, it is now potentially possible to build CAZyme constructs from individual protein domains, tailored to the conditions of specific industrial processes. In this review, we identify a 'toolbox' of thermostable CAZyme domains from extremely thermophilic organisms and highlight recent advances in CAZyme engineering which will allow for the rational design of CAZymes tailored to specific aspects of lignocellulose digestion.

Indexed as

Catalytic DomainThermotoleranceBacteriaExtreme HeatHydrolasesLigninLyasesPlantsHydrolasesLigninlignocelluloseLyasesCAZymeExtreme thermophilesLignocelluloseProtein domainsSynthetic biology

Identifiers

What OpenQuestion holds

Textmetadata
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.