Evidence map›Paper›PMID 32127917›Full record

ArticleBiotechnology for biofuels2020

Improvement of the catalytic activity and thermostability of a hyperthermostable endoglucanase by optimizing N-glycosylation sites.

Chao Han, Qunqing Wang, Yanxu Sun, Ruirui Yang, Mengyu Liu, Siqi Wang, Yifan Liu, Lifan Zhou, Duochuan Li

Abstract read
In one paragraph

Article in Biotechnology for biofuels, 2020. 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
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  4. Improved Thermal Stability of a Novel Acidophilic Phytase.Journal of microbiology and biotechnology · 2024
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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

9 authors.

Chao HanShandong Key Laboratory for Agricultural Microbiology, College of Plant Protection, Shandong Agricultural University, Tai'an, 271018 Shandong China.
Qunqing WangShandong Key Laboratory for Agricultural Microbiology, College of Plant Protection, Shandong Agricultural University, Tai'an, 271018 Shandong China.
Yanxu SunShandong Key Laboratory for Agricultural Microbiology, College of Plant Protection, Shandong Agricultural University, Tai'an, 271018 Shandong China.
Ruirui YangShandong Key Laboratory for Agricultural Microbiology, College of Plant Protection, Shandong Agricultural University, Tai'an, 271018 Shandong China.
Mengyu LiuShandong Key Laboratory for Agricultural Microbiology, College of Plant Protection, Shandong Agricultural University, Tai'an, 271018 Shandong China.
Siqi WangShandong Key Laboratory for Agricultural Microbiology, College of Plant Protection, Shandong Agricultural University, Tai'an, 271018 Shandong China.
Yifan LiuShandong Key Laboratory for Agricultural Microbiology, College of Plant Protection, Shandong Agricultural University, Tai'an, 271018 Shandong China.
Lifan ZhouShandong Key Laboratory for Agricultural Microbiology, College of Plant Protection, Shandong Agricultural University, Tai'an, 271018 Shandong China.
Duochuan LiShandong Key Laboratory for Agricultural Microbiology, College of Plant Protection, Shandong Agricultural University, Tai'an, 271018 Shandong China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundEndoglucanase has been extensively employed in industrial processes as a key biocatalyst for lignocellulosic biomass degradation. Thermostable endoglucanases with high catalytic activity at elevated temperatures are preferred in industrial use. To improve the activity and thermostability, site-directed mutagenesis was conducted to modify the N-glycosylation sites of the thermostable β-1,4-endoglucanase CTendo45 from

resultsIn this study, structure-based rational design was performed based on the modification of N-glycosylation sites in CTendo45. Eight single mutants and one double mutant were constructed and successfully expressed in

conclusionsThis study provides initial insight into the biochemical function of N-glycosylation in thermostable endoglucanases. Moreover, the design approach to the optimization of N-glycosylation sites presents an effective and feasible strategy to improve enzymatic activity and thermostability.

Indexed as

EndoglucanaseN-glycosylation siteSpecific activityThermostability

Identifiers

PMID32127917
PMCPMC7045587

What OpenQuestion holds

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Registered trials

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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.