Evidence map›Paper›PMID 26712627›Full record

ArticleWorld journal of microbiology & biotechnology2016

Isolation and characterization of a non-specific endoglucanase from a metagenomic library of goat rumen.

Jianbo Cheng, Shuai Huang, Haiqin Jiang, Yunhai Zhang, Lvmu Li, Juhua Wang, Caiyun Fan

Abstract read
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Article in World journal of microbiology & biotechnology, 2016. 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.

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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

7 authors.

Jianbo ChengCollege of Animal Science and Technology, Anhui Agricultural University, No. 130 Changjiang West Road, Hefei, 230036, Anhui, People's Republic of China. chengjianbofcy@163.com.
Shuai HuangCollege of Animal Science and Technology, Anhui Agricultural University, No. 130 Changjiang West Road, Hefei, 230036, Anhui, People's Republic of China.
Haiqin JiangCollege of Animal Science and Technology, Anhui Agricultural University, No. 130 Changjiang West Road, Hefei, 230036, Anhui, People's Republic of China.
Yunhai ZhangCollege of Animal Science and Technology, Anhui Agricultural University, No. 130 Changjiang West Road, Hefei, 230036, Anhui, People's Republic of China.
Lvmu LiCollege of Animal Science and Technology, Anhui Agricultural University, No. 130 Changjiang West Road, Hefei, 230036, Anhui, People's Republic of China.
Juhua WangCollege of Animal Science and Technology, Anhui Agricultural University, No. 130 Changjiang West Road, Hefei, 230036, Anhui, People's Republic of China.
Caiyun FanCollege of Animal Science and Technology, Anhui Agricultural University, No. 130 Changjiang West Road, Hefei, 230036, Anhui, People's Republic of China. fancaiyun@ahau.edu.cn.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A cellulase gene (cel28a) was isolated from a rumen microbial metagenome library of goat rumen microorganisms, cloned into E. coli, and expressed in active form. The gene has a length of 1596 bp obtained using a genome walking Kit and encodes a protein of 509 amino acids with a calculated MW of 55 kDa. The deduced amino acid sequence was homologous with cellulases belonging to the glycosyl hydrolase family 5 (GH5). The expressed protein showed activity toward carboxymethylcellulose (CMC) and xylan, suggesting non-specific endoglucanase activity. The optimal conditions for endoglucanase and xylanase activities were 50 °C and pH 5.0. The metal ions (Ca(2+), Fe(2+), Mn(2+) and Co(2+)) stimulated the cellulase activity of cel28a, while the other metal ions and chemicals (Ni(2+), Mg(2+), Zn(2+), Cu(2+), SDS and EDTA) inhibited the cellulase activity. Further examination of substrate preference showed a higher activity with CMC, oat spelt xylan and birchwood xylan than with filter paper and microcrystalline cellulose, again suggesting that the protein was an endoglucanase with xylanase activity.

Indexed as

Amino Acid SequenceAnimalsBacterial ProteinsCarboxymethylcellulose SodiumCellulaseCelluloseCloning, MolecularEnzyme StabilityEscherichia coliGoatsHydrogen-Ion ConcentrationMetagenomicsMolecular Sequence DataPhylogenyRumenSequence AlignmentBacterial ProteinsCarboxymethylcellulose SodiumCellulaseCellulosemicrocrystalline celluloseXylansEndoglucanaseGoat rumenMetagenomeXylanase

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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.