Evidence map›Paper›PMID 26791384›Full record

ArticleExtremophiles : life under extreme conditions2016

Characterization of a cold-adapted and salt-tolerant exo-chitinase (ChiC) from Pseudoalteromonas sp. DL-6.

Xiaohui Wang, Naiyu Chi, Fengwu Bai, Yuguang Du, Yong Zhao, Heng Yin

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In one paragraph

Article in Extremophiles : life under extreme conditions, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.0field-weighted citation impact, top 22% 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

13 citing papers in PubMed, 32 citations in OpenAlex.

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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

6 authors at 5 institutions in 1 country.

Xiaohui WangSchool of Life Science and Biotechnology, Dalian University of Technology, Dalian, 116024, People's Republic of China.
Naiyu ChiSchool of Life Science and Biotechnology, Dalian University, Dalian, 116622, People's Republic of China.
Fengwu BaiSchool of Life Science and Biotechnology, Dalian University of Technology, Dalian, 116024, People's Republic of China.
Yuguang DuInstitute of Process Engineering, Chinese Academy of Science, Beijing, 100190, People's Republic of China.
Yong ZhaoNatural Products and Glyco-Biotechnology Research Group, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian, 116023, People's Republic of China. zy1805@dicp.ac.cn.
Heng YinNatural Products and Glyco-Biotechnology Research Group, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian, 116023, People's Republic of China. yinheng@dicp.ac.cn.
Dalian Institute of Chemical Physics · CNChinese Academy of Sciences · CNDalian University · CNDalian University of Technology · CNInstitute of Process Engineering · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We have previously reported a non-processive endo-type chitinase, ChiA, from a newly isolated marine psychrophilic bacterium, Pseudoalteromonas sp. DL-6. In this study, a processive exo-type chitinase, ChiC, was cloned from the same bacterium and characterized in detail. ChiC could hydrolyze crystalline chitin into (GlcNAc)2 as the only observed product. It exhibited high catalytic activity even at low temperatures, e.g. close to 0 °C, or in the presence of 5 M NaCl, suggesting that ChiC was a cold-adapted and highly salt-tolerant chitinase. ChiC could also hydrolyze other substrates, including chitosan and Avicel, indicating its broad substrate specificity. Sequence features indicated that ChiC was a multi-domain protein having a deep substrate-binding groove that was regarded as characteristic of processive exo-chitinases. Enzymatic hydrolysis of chitin by ChiC could be remarkably boosted in the presence of ChiA, suggesting the synergy of ChiC and ChiA. This work provided a new evidence to prove that marine psychrophilic bacteria utilized a synergistic enzyme system to degrade recalcitrant chitin.

Indexed as

Cold TemperatureSalt ToleranceBacterial ProteinsHexosaminidasesPseudoalteromonas1,4-beta-chitobiosidaseBacterial ProteinsHexosaminidasesChitinCold-adaptedExochitinasePseudoalteromonas sp.Salt-tolerant

Identifiers

PMID26791384
OpenAlexW2300681203

What OpenQuestion holds

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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.