Evidence map›Paper›PMID 29681022›Full record

ArticleExtremophiles : life under extreme conditions2018

The unique GH5 cellulase member in the extreme halotolerant fungus Aspergillus glaucus CCHA is an endoglucanase with multiple tolerance to salt, alkali and heat: prospects for straw degradation applications.

Zhengqun Li, Xue Pei, Ziyu Zhang, Yi Wei, Yanyue Song, Lina Chen, Shouan Liu, Shi-Hong Zhang

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Article 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 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

14 citing papers in PubMed, 44 citations in OpenAlex.

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  11. Alternative Splicing ofFrontiers in microbiology · 2021
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4 · The record

Corrections and comments

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5 · Who and what money

Authors and funding

8 authors at 1 institution in 1 country.

Zhengqun LiCollege of Plant Sciences, Jilin University, Changchun, 130062, People's Republic of China.
Xue PeiCollege of Plant Sciences, Jilin University, Changchun, 130062, People's Republic of China.
Ziyu ZhangCollege of Plant Sciences, Jilin University, Changchun, 130062, People's Republic of China.
Yi WeiCollege of Plant Sciences, Jilin University, Changchun, 130062, People's Republic of China.
Yanyue SongCollege of Plant Sciences, Jilin University, Changchun, 130062, People's Republic of China.
Lina ChenCollege of Plant Sciences, Jilin University, Changchun, 130062, People's Republic of China.
Shouan LiuCollege of Plant Sciences, Jilin University, Changchun, 130062, People's Republic of China. shouan@jlu.edu.cn.
Shi-Hong ZhangCollege of Plant Sciences, Jilin University, Changchun, 130062, People's Republic of China. zhang_sh@jlu.edu.cn.
Jilin University · CN

Funding

National Natural Science Foundation of China 31171794National Natural Science Foundation of China 31370689National Natural Science Foundation of China 31670141National Natural Science Foundation of China 31671972
6 · The paper itself

Abstract

In a halotolerant fungus Aspergillus glaucus CCHA, several functional proteins with stress-tolerant activity have been studied, but no secretory enzymes have been identified yet. The unique GH5 cellulase candidate from A. glaucus, an endoglucanase termed as AgCMCase, was cloned, expressed in the Pichia pastoris system and the purified enzyme was characterized. A large amount of recombinant enzyme secreted by the P. pastoris GS115 strain was purified to homogeneity. The molecular weight of the purified endoglucanase is about 55.0 kDa. The AgCMCase exhibited optimum catalytic activity at pH 5.0 and 55 °C. However, it remained relatively stable at temperatures ranging from 45 to 80 °C and pH ranging from 4.0 to 9.0. In addition, it showed higher activity at extreme NaCl concentrations from 1.0 to 4.0 M, suggesting it is an enzyme highly stable under heat, acid, alkaline and saline conditions. To evaluate the catalytic activity of AgCMCase, the hydrolysis products of rice and corn straws were successfully studied. In conclusion, the AgCMCase is a thermostable and salt-tolerant cellulase with potential for industrial application.

Indexed as

Salt ToleranceThermotoleranceAspergillusBiotransformationCellulaseCelluloseEnzyme StabilityFungal ProteinsHydrogen-Ion ConcentrationIndustrial MicrobiologyCellulaseCelluloseFungal Proteins4-β-GlucanaseEndo-1,4-β-GlucanaseHalotolerant fungusHeterologous expressionPleiotropic toleranceSalt toleranceThermostable

Identifiers

PMID29681022
OpenAlexW2800342016

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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.