Evidence map›Paper›PMID 28062919›Full record

ArticleExtremophiles : life under extreme conditions2017

Screening, purification, and characterization of a novel organic solvent-tolerant esterase, Lip2, from Monascus purpureus strain M7.

Li-Jing Kang, Zi-Tong Meng, Chen Hu, Yan Zhang, Hai-Lun Guo, Qing Li, Mu Li

Abstract read
PubMed Publisher
In one paragraph

Article in Extremophiles : life under extreme conditions, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.6field-weighted citation impact, top 35% 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

4 citing papers in PubMed, 9 citations in OpenAlex.

  1. Lipases: An Overview.Methods in molecular biology (Clifton, N.J.) · 2027
    Review
  2. Article
  3. Characterization and Immobilization of a Novel SGNH Family Esterase (International journal of molecular sciences · 2019
    Article
  4. 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

7 authors at 1 institution in 1 country.

Li-Jing KangKey Laboratory of Environment Correlative Dietology, Huazhong Agricultural University, Wuhan, 430070, Hubei, People's Republic of China.
Zi-Tong MengKey Laboratory of Environment Correlative Dietology, Huazhong Agricultural University, Wuhan, 430070, Hubei, People's Republic of China.
Chen HuKey Laboratory of Environment Correlative Dietology, Huazhong Agricultural University, Wuhan, 430070, Hubei, People's Republic of China.
Yan ZhangKey Laboratory of Environment Correlative Dietology, Huazhong Agricultural University, Wuhan, 430070, Hubei, People's Republic of China.
Hai-Lun GuoKey Laboratory of Environment Correlative Dietology, Huazhong Agricultural University, Wuhan, 430070, Hubei, People's Republic of China.
Qing LiSystem Design Institute of Hubei Aerospace Technology Academy, Wuhan, 430040, People's Republic of China.
Mu LiKey Laboratory of Environment Correlative Dietology, Huazhong Agricultural University, Wuhan, 430070, Hubei, People's Republic of China. limu@mail.hzau.edu.cn.
Huazhong Agricultural University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Organic solvent-tolerant esterases are proven to be excellent biocatalysts in chemical and pharmaceutical industries. A novel organic solvent-tolerant esterase gene, lip2, was isolated from filamentous fungi Monascus purpureus M7. The sequence analysis suggested that lip2 has a conserved "GDSL" motif near the active center. The multiple-sequence alignment and phylogenetic analysis revealed that Lip2 displayed two unique amino-acid sequence motifs that clearly separate it from any other previously described lipase family. After incubation in 20% methanol and ethanol for 3 h, the Lip2 displayed 190 and 180% residual activities, respectively. It retained 99-110% relative activity in 20% (v/v) hydrophilic organic solvents after incubation for 1 day. This esterase showed optimal activity at 40 °C and retained about 70% maximal activity at 60 °C. The enzyme also displayed more than 50% residual activity over a range of pH 5-11. In the presence of most of metal ions or additives, Lip2 retained most of the activity. These unique properties of Lip2 make it a promising as biocatalyst for industrial processes.

Indexed as

Amino Acid MotifsEnzyme StabilityFungal ProteinsHot TemperatureHydrogen-Ion ConcentrationLipaseMonascusSolventsFungal ProteinsLipaseSolventsEnzyme applicationEnzymesEnzyme stabilityGene cloning and expressionIsolation and characterization

Identifiers

PMID28062919
OpenAlexW2570730424

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.