Evidence map›Paper›PMID 30455732›Full record

ArticleBiotechnology for biofuels2018

Cloning, purification, and characterization of an organic solvent-tolerant chitinase, MtCh509, from

Hyo-Jung Lee, Yong-Suk Lee, Yong-Lark Choi

Abstract read
In one paragraph

Article in Biotechnology for biofuels, 2018. 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
–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

13 citing papers in PubMed.

  1. Article
  2. Highly efficient chitinase production fromFrontiers in microbiology · 2026
    Article
  3. Article
  4. Article
  5. Polymer degrading marineBeilstein journal of organic chemistry · 2024
    Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Identification of Chitinolytic Enzymes inFrontiers in microbiology · 2020
    Article
  11. A novel bacterial β-Biotechnology for biofuels · 2020
    Article
  12. Article
  13. 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

3 authors.

Hyo-Jung Lee *Department of Biotechnology, Dong-A University, Busan, 49315 Republic of Korea.
Yong-Suk Lee *Department of Biotechnology, Dong-A University, Busan, 49315 Republic of Korea.
Yong-Lark ChoiDepartment of Biotechnology, Dong-A University, Busan, 49315 Republic of Korea.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundThe ability to use organic solvents in enzyme reactions offers a number of industrially useful advantages. However, most enzymes are almost completely inactive in the presence of organic solvents. Thus, organic solvent-tolerant enzymes have potential applications in industrial processes.

resultsA chitinase gene from

conclusionThe results of the hydrolysate analysis and the observed increase in enzyme activity in the presence of organic solvents show that MtCh509 has industrially attractive advantages. This is the first report on an organic solvent-tolerant and transglycosylating chitinase from

Indexed as

DAU221Microbulbifer thermotoleransOrganic solvent-tolerant chitinaseTransglycosylation

Identifiers

PMID30455732
PMCPMC6222997

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

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.