Evidence map›Paper›PMID 28208644›Full record

ArticleMolecules (Basel, Switzerland)2017

Novel Magnetic Cross-Linked Cellulase Aggregates with a Potential Application in Lignocellulosic Biomass Bioconversion.

Junqi Jia, Weiwei Zhang, Zengjie Yang, Xianling Yang, Na Wang, Xiaoqi Yu

Abstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing 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

18 citing papers in PubMed.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. Article
  10. Review
  11. Review
  12. Crosslinked Enzyme Aggregates (CLEAs) of Laccases fromMolecules (Basel, Switzerland) · 2020
    Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Special Issue: Enzyme Immobilization 2016.Molecules (Basel, Switzerland) · 2017
    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

6 authors.

Junqi JiaKey Laboratory of Green Chemistry Technology, Ministry of Education, College of Chemistry, Sichuan University, Chengdu 610064, China. scujunqi@163.com.
Weiwei ZhangSchool of Chemistry and Chemical Engineering, Ningxia University, Yinchuan 750021, China. zhangww@nxu.edu.cn.
Zengjie YangKey Laboratory of Green Chemistry Technology, Ministry of Education, College of Chemistry, Sichuan University, Chengdu 610064, China. 15864374098@163.com.
Xianling YangKey Laboratory of Green Chemistry Technology, Ministry of Education, College of Chemistry, Sichuan University, Chengdu 610064, China. 13550337266@163.com.
Na WangKey Laboratory of Green Chemistry Technology, Ministry of Education, College of Chemistry, Sichuan University, Chengdu 610064, China. wnchem@scu.edu.cn.
Xiaoqi YuKey Laboratory of Green Chemistry Technology, Ministry of Education, College of Chemistry, Sichuan University, Chengdu 610064, China. xqyu@scu.edu.cn.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The utilization of renewable biomass resources to produce high-value chemicals by enzymatic processes is beneficial for alternative energy production, due to the accelerating depletion of fossil fuels. As immobilization techniques can improve enzyme stability and reusability, a novel magnetic cross-linked cellulase aggregate has been developed and applied for biomass bioconversion. The crosslinked aggregates could purify and immobilize enzymes in a single operation, and could then be combined with magnetic nanoparticles (MNPs), which provides easy separation of the materials. The immobilized cellulase showed a better activity at a wider temperature range and pH values than that of the free cellulase. After six cycles of consecutive reuse, the immobilized cellulase performed successful magnetic separation and retained 74% of its initial activity when carboxylmethyl cellulose (CMC) was used as the model substrate. Furthermore, the structure and morphology of the immobilized cellulase were studied by Fourier transform infrared spectroscopy (FTIR) and scanning electron microscopy (SEM). Moreover, the immobilized cellulase was shown to hydrolyze bamboo biomass with a yield of 21%, and was re-used in biomass conversion up to four cycles with 38% activity retention, which indicated that the immobilized enzyme has good potential for biomass applications.

Indexed as

CellulaseCross-Linking ReagentsEnzymes, ImmobilizedEnzyme StabilityFungal ProteinsGlutaralHydrogen-Ion ConcentrationHydrolysisLigninSasaTrichodermaCellulaseCross-Linking ReagentsEnzymes, ImmobilizedFungal ProteinsGlutaralLigninlignocellulosebiomasscellulasecross-linked enzyme aggregateshydrolysismagnetic nanoparticles

Identifiers

PMID28208644
PMCPMC6155674

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.