Evidence map›Paper›PMID 28689814›Full record

ArticleBrazilian journal of microbiology : [publication of the Brazilian Society for Microbiology]

Isolation and characterization of a novel endo-β-1,4-glucanase from a metagenomic library of the black-goat rumen.

Yun-Hee Song, Kyung-Tai Lee, Jin-Young Baek, Min-Ju Kim, Mi-Ra Kwon, Young-Joo Kim, Mi-Rim Park, Haesu Ko, Jin-Sung Lee, Keun-Sung Kim

Open access · hybridAbstract read
In one paragraph

Article in Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology]. 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
1.8field-weighted citation impact, top 16% 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, 28 citations in OpenAlex.

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  10. Metagenomics as a Tool To Monitor Reclaimed-Water Quality.Applied and environmental microbiology · 2020
    Review
  11. Article
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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

10 authors at 4 institutions in 1 country.

Yun-Hee SongDepartment of Food Science and Technology, Chung-Ang University, Ansung 456-756, South Korea.
Kyung-Tai LeeAnimal Genomics and Bioinformatics Division, National Institute of Animal Science, Rural Development Administration, Wanju, South Korea.
Jin-Young BaekDepartment of Food Science and Technology, Chung-Ang University, Ansung 456-756, South Korea.
Min-Ju KimDepartment of Food Science and Technology, Chung-Ang University, Ansung 456-756, South Korea.
Mi-Ra KwonAnimal Genomics and Bioinformatics Division, National Institute of Animal Science, Rural Development Administration, Wanju, South Korea.
Young-Joo KimAnimal Genomics and Bioinformatics Division, National Institute of Animal Science, Rural Development Administration, Wanju, South Korea.
Mi-Rim ParkAnimal Genomics and Bioinformatics Division, National Institute of Animal Science, Rural Development Administration, Wanju, South Korea.
Haesu KoAnimal Genomics and Bioinformatics Division, National Institute of Animal Science, Rural Development Administration, Wanju, South Korea.
Jin-Sung LeeDepartment of Biological Sciences, Kyonggi University, Suwon, South Korea. Electronic address: lejis@daum.net.
Keun-Sung KimDepartment of Food Science and Technology, Chung-Ang University, Ansung 456-756, South Korea. Electronic address: keunsung@cau.ac.kr.
Chung-Ang University · KRRural Development Administration · KRNational Institute of Animal Science · KRKyonggi University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The various types of lignocellulosic biomass found in plants comprise the most abundant renewable bioresources on Earth. In this study, the ruminal microbial ecosystem of black goats was explored because of their strong ability to digest lignocellulosic forage. A metagenomic fosmid library containing 115,200 clones was prepared from the black-goat rumen and screened for a novel cellulolytic enzyme. The KG35 gene, containing a novel glycosyl hydrolase family 5 cellulase domain, was isolated and functionally characterized. The novel glycosyl hydrolase family 5 cellulase gene is composed of a 963-bp open reading frame encoding a protein of 320 amino acid residues (35.1kDa). The deduced amino acid sequence showed the highest sequence identity (58%) for sequences from the glycosyl hydrolase family 5 cellulases. The novel glycosyl hydrolase family 5 cellulase gene was overexpressed in Escherichia coli. Substrate specificity analysis revealed that this recombinant glycosyl hydrolase family 5 cellulase functions as an endo-β-1,4-glucanase. The recombinant KG35 endo-β-1,4-glucanase showed optimal activity within the range of 30-50°C at a pH of 6-7. The thermostability was retained and the pH was stable in the range of 30-50°C at a pH of 5-7.

Indexed as

AnimalsBacteriaBacterial ProteinsCellulaseCloning, MolecularEnzyme StabilityGastrointestinal MicrobiomeGoatsHydrogen-Ion ConcentrationMetagenomeMetagenomicsRumenBacterial ProteinsCellulaseBlack goatsEndo-β-1,4-glucanaseGlycosyl hydrolase family 5 (GH5)Metagenomic libraryRumen

Identifiers

PMID28689814
PMCPMC5628298
OpenAlexW2715054119

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.