Evidence map›Paper›PMID 24386096›Full record

ArticlePloS one2013

Isolation and characterization of a novel endoglucanase from a Bursaphelenchus xylophilus metagenomic library.

Lin Zhang, Yongxin Fan, Haoying Zheng, Fengguang Du, Ke-qin Zhang, Xiaowei Huang, Linfeng Wang, Man Zhang, Qiuhong Niu

Abstract read
In one paragraph

Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing 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

10 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Characterization of a GH8 β-1,4-Glucanase fromJournal of microbiology and biotechnology · 2021
    Article
  5. Article
  6. Article
  7. Recent Advances in Function-based Metagenomic Screening.Genomics, proteomics & bioinformatics · 2018
    Review
  8. Article
  9. Article
  10. 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

9 authors.

Lin ZhangDepartment of Life Science and Biotechnology, Nanyang Normal University, Nanyang, China.
Yongxin FanDepartment of Life Science and Biotechnology, Nanyang Normal University, Nanyang, China.
Haoying ZhengDepartment of Life Science and Biotechnology, Nanyang Normal University, Nanyang, China.
Fengguang DuState Key Laboratory of Motor Bio-fuel technology, Henan Tianguan Group Co. Ltd., Nanyang, China.
Ke-qin ZhangLaboratory for Conservation and Utilization of Bio-Resources, and Key Laboratory for Microbial Resources of the Ministry of Education, Yunnan University, Kunming, China.
Xiaowei HuangLaboratory for Conservation and Utilization of Bio-Resources, and Key Laboratory for Microbial Resources of the Ministry of Education, Yunnan University, Kunming, China.
Linfeng WangState Key Laboratory of Motor Bio-fuel technology, Henan Tianguan Group Co. Ltd., Nanyang, China.
Man ZhangState Key Laboratory of Motor Bio-fuel technology, Henan Tianguan Group Co. Ltd., Nanyang, China.
Qiuhong NiuDepartment of Life Science and Biotechnology, Nanyang Normal University, Nanyang, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A novel gene (designated as cen219) encoding endoglucanase was isolated from a Bursaphelenchus xylophilus metagenomic library by functional screening. Sequence analysis revealed that cen219 encoded a protein of 367 amino acids. SDS-PAGE analysis of purified endoglucanase suggested that Cen219 was a monomeric enzyme with a molecular mass of 40 kDa. The optimum temperature and pH for endoglucanase activity of Cen219 was separately 50 °C and 6.0. It was stable from 30 to 50 °C, and from pH 4.0 to 7.0. The activity was significantly enhanced by Mn(2+) and dramatically reduced by detergent SDS and metals Fe(3+), Cu(2+) or Hg(2+). The enzyme hydrolyzed a wide range of β-1, 3-, and β-1, 4-linked polysaccharides, with varying activities. Activities towards microcrystalline cellulose and filter paper were relatively high, while the highest activity was towards oat gum. The Km and Vmax of Cen219 towards CMC was 17.37 mg/ml and 333.33 U/mg, respectively. The findings have an insight into understanding the molecular basis of host-parasite interactions in B. xylophilus species. The properties also make Cen219 an interesting enzyme for biotechnological application.

Indexed as

Genomic LibraryAnimalsCellulaseHelminth ProteinsMetagenomeNematodaPhylogenyCellulaseHelminth Proteins

Identifiers

PMID24386096
PMCPMC3873927

What OpenQuestion holds

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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.