Evidence map›Paper›PMID 25746227›Full record

ArticlePloS one2015

Properties of a newly identified esterase from Bacillus sp. K91 and its novel function in diisobutyl phthalate degradation.

Junmei Ding, Chaofan Wang, Zhenrong Xie, Junjun Li, Yunjuan Yang, Yuelin Mu, Xianghua Tang, Bo Xu, Junpei Zhou, Zunxi Huang

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
3.3field-weighted citation impact, top 9% 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

24 citing papers in PubMed, 100 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Whole-genome analysis of3 Biotech · 2023
    Article
  11. Article
  12. Article
  13. Phthalate Esters Metabolic StrainMicroorganisms · 2022
    Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. 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

10 authors at 1 institution in 1 country.

Junmei DingEngineering Research Center of Sustainable Development and Utilization of Biomass Energy, Ministry of Education, Yunnan Normal University, Kunming 650500, Yunnan, China; Key Laboratory of Enzyme Engineering, Yunnan Normal University, Kunming 650500, Yunnan, China.
Chaofan WangEngineering Research Center of Sustainable Development and Utilization of Biomass Energy, Ministry of Education, Yunnan Normal University, Kunming 650500, Yunnan, China; Key Laboratory of Enzyme Engineering, Yunnan Normal University, Kunming 650500, Yunnan, China.
Zhenrong XieEngineering Research Center of Sustainable Development and Utilization of Biomass Energy, Ministry of Education, Yunnan Normal University, Kunming 650500, Yunnan, China.
Junjun LiEngineering Research Center of Sustainable Development and Utilization of Biomass Energy, Ministry of Education, Yunnan Normal University, Kunming 650500, Yunnan, China; Key Laboratory of Enzyme Engineering, Yunnan Normal University, Kunming 650500, Yunnan, China.
Yunjuan YangEngineering Research Center of Sustainable Development and Utilization of Biomass Energy, Ministry of Education, Yunnan Normal University, Kunming 650500, Yunnan, China; Key Laboratory of Enzyme Engineering, Yunnan Normal University, Kunming 650500, Yunnan, China.
Yuelin MuEngineering Research Center of Sustainable Development and Utilization of Biomass Energy, Ministry of Education, Yunnan Normal University, Kunming 650500, Yunnan, China; Key Laboratory of Enzyme Engineering, Yunnan Normal University, Kunming 650500, Yunnan, China.
Xianghua TangEngineering Research Center of Sustainable Development and Utilization of Biomass Energy, Ministry of Education, Yunnan Normal University, Kunming 650500, Yunnan, China; Key Laboratory of Enzyme Engineering, Yunnan Normal University, Kunming 650500, Yunnan, China.
Bo XuEngineering Research Center of Sustainable Development and Utilization of Biomass Energy, Ministry of Education, Yunnan Normal University, Kunming 650500, Yunnan, China; Key Laboratory of Enzyme Engineering, Yunnan Normal University, Kunming 650500, Yunnan, China.
Junpei ZhouEngineering Research Center of Sustainable Development and Utilization of Biomass Energy, Ministry of Education, Yunnan Normal University, Kunming 650500, Yunnan, China.
Zunxi HuangEngineering Research Center of Sustainable Development and Utilization of Biomass Energy, Ministry of Education, Yunnan Normal University, Kunming 650500, Yunnan, China; Key Laboratory of Enzyme Engineering, Yunnan Normal University, Kunming 650500, Yunnan, China.
Yunnan Normal University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The widely used plasticizer phthalate esters (PAEs) have become a public concern because of their effects on environmental contamination and toxicity on mammals. However, the biodegradation of PAEs, especially diisobutyl phthalate (DiBP), remains poorly understood. In particular, genes involved in the hydrolysis of these compounds were not conclusively identified. In this study, the CarEW gene, which encodes an enzyme that is capable of hydrolyzing ρ-nitrophenyl esters of fatty acids, was cloned from a thermophilic bacterium Bacillus sp. K91 and heterologously expressed in Escherichia coli BL21 using the pEASY-E2 expression system. The enzyme showed a monomeric structure with a molecular mass of approximately 53.76 kDa and pI of 4.88. The enzyme exhibited maximal activity at pH 7.5 and 45 °C, with ρ-NP butyrate as the best substrate. The enzyme was fairly stable within the pH range from 7.0 to 8.5. High-pressure liquid chromatography (HPLC) and electrospray ionization mass spectrometry (ESI-MS) were employed to detect the catabolic pathway of DiBP. Two intermediate products were identified, and a potential biodegradation pathway was proposed. Altogether, our findings present a novel DiBP degradation enzyme and indicate that the purified enzyme may be a promising candidate for DiBP detoxification and for environmental protection.

Indexed as

Amino Acid SequenceBacillusChromatography, High Pressure LiquidDibutyl PhthalateElectrophoresis, Polyacrylamide GelEsterasesHydrogen-Ion ConcentrationHydrolysisMolecular Sequence DataPhylogenySequence Homology, Amino AcidSpectrometry, Mass, Electrospray IonizationSubstrate SpecificityTemperatureDibutyl Phthalatediisobutyl phthalateEsterases

Identifiers

PMID25746227
PMCPMC4352063
OpenAlexW1993044653

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.