Evidence map›Paper›PMID 35184224›Full record

ArticleBioprocess and biosystems engineering2022

Cross-linked enzyme aggregates (CLEAs) of cellulase with improved catalytic activity, adaptability and reusability.

Tiantian Li, Xiaowu Gong, Gaoshan Yang, Qin Li, Jin Huang, Na Zhou, Xin Jia

Abstract read
PubMed Publisher
In one paragraph

Article in Bioprocess and biosystems engineering, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

6 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Immobilized Cellulase on NHApplied biochemistry and biotechnology · 2024
    Article
  5. Article
  6. 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

7 authors at 2 institutions in 1 country.

Tiantian LiKey Laboratory for Green Processing of Chemical Engineering of Xinjiang Bingtuan, School of Chemistry and Chemical Engineering, Shihezi University, Beisi Road, Shihezi, 800032, Xinjiang, China.
Xiaowu GongKey Laboratory for Green Processing of Chemical Engineering of Xinjiang Bingtuan, School of Chemistry and Chemical Engineering, Shihezi University, Beisi Road, Shihezi, 800032, Xinjiang, China. gxw_tea@shzu.edu.cn.
Gaoshan YangKey Laboratory for Green Processing of Chemical Engineering of Xinjiang Bingtuan, School of Chemistry and Chemical Engineering, Shihezi University, Beisi Road, Shihezi, 800032, Xinjiang, China.
Qin LiKey Laboratory for Green Processing of Chemical Engineering of Xinjiang Bingtuan, School of Chemistry and Chemical Engineering, Shihezi University, Beisi Road, Shihezi, 800032, Xinjiang, China.
Jin HuangKey Laboratory for Green Processing of Chemical Engineering of Xinjiang Bingtuan, School of Chemistry and Chemical Engineering, Shihezi University, Beisi Road, Shihezi, 800032, Xinjiang, China.
Na ZhouKey Laboratory for Green Processing of Chemical Engineering of Xinjiang Bingtuan, School of Chemistry and Chemical Engineering, Shihezi University, Beisi Road, Shihezi, 800032, Xinjiang, China. jndxzzl@163.com.
Xin JiaKey Laboratory for Green Processing of Chemical Engineering of Xinjiang Bingtuan, School of Chemistry and Chemical Engineering, Shihezi University, Beisi Road, Shihezi, 800032, Xinjiang, China.
Shihezi University · CNXinjiang Production and Construction Corps · CN

Funding

General Science and Technology Project of "Double First Class University Plan" Construction of Shihezi University SHYL-DK201803National Natural Science Foundation of China 21464011
6 · The paper itself

Abstract

In this study, cross-linked cellulase aggregates (C-CLEAs) were synthesized by precipitation of cellulase with ammonium sulfate and then cross-linking with glutaraldehyde. The results revealed that the optimal pH of C-CLEAs shifted toward a more acidic environment by 2.0 pH units, and the optimal temperature shifted toward higher temperature by 20 °C after immobilization. The half-life (t

Indexed as

CellulaseEnzymes, ImmobilizedCross-Linking ReagentsEnzyme StabilityGlutaralTemperatureCellulaseCross-Linking ReagentsEnzymes, ImmobilizedGlutaralCatalytic activityCross-linked cellulase aggregatesEnzymatic saccharificationThermal stability

Identifiers

PMID35184224
OpenAlexW4213046552

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.