Evidence map›Paper›PMID 31286972›Full record

ArticleMicrobial cell factories2019

Characterization of an acetyl xylan esterase from the marine bacterium Ochrovirga pacifica and its synergism with xylanase on beechwood xylan.

Sachithra Amarin Hettiarachchi, Young-Kyung Kwon, Youngdeuk Lee, Eunyoung Jo, Tae-Yang Eom, Yoon-Hyeok Kang, Do-Hyung Kang, Mahanama De Zoysa, Svini Dileepa Marasinghe, Chulhong Oh

Open access · goldAbstract read
In one paragraph

Article in Microbial cell factories, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
2.4field-weighted citation impact, top 12% 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

8 citing papers in PubMed, 36 citations in OpenAlex.

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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 3 institutions in 2 countries.

Sachithra Amarin HettiarachchiKorea Institute of Ocean Science & Technology, 2670, Iljudong-ro, Gujwa-eup, Jeju, Republic of Korea.
Young-Kyung KwonKorea Institute of Ocean Science & Technology, 2670, Iljudong-ro, Gujwa-eup, Jeju, Republic of Korea.
Youngdeuk LeeKorea Institute of Ocean Science & Technology, 2670, Iljudong-ro, Gujwa-eup, Jeju, Republic of Korea.
Eunyoung JoKorea Institute of Ocean Science & Technology, 2670, Iljudong-ro, Gujwa-eup, Jeju, Republic of Korea.
Tae-Yang EomKorea Institute of Ocean Science & Technology, 2670, Iljudong-ro, Gujwa-eup, Jeju, Republic of Korea.
Yoon-Hyeok KangKorea Institute of Ocean Science & Technology, 2670, Iljudong-ro, Gujwa-eup, Jeju, Republic of Korea.
Do-Hyung KangKorea Institute of Ocean Science & Technology, 2670, Iljudong-ro, Gujwa-eup, Jeju, Republic of Korea.
Mahanama De ZoysaCollege of Veterinary Medicine, Chungnam National University, 99 Daehak-ro, Yuseong-gu, Daejeon, Republic of Korea.
Svini Dileepa MarasingheKorea Institute of Ocean Science & Technology, 2670, Iljudong-ro, Gujwa-eup, Jeju, Republic of Korea.
Chulhong OhKorea Institute of Ocean Science & Technology, 2670, Iljudong-ro, Gujwa-eup, Jeju, Republic of Korea. och0101@kiost.ac.kr.ORCID http://orcid.org/0000-0002-9283-3258
Korea Institute of Ocean Science and Technology · KRChungnam National University · KRUniversity of Ruhuna · LK

Funding

Korea Institute of Ocean Science and Technology PE99722
6 · The paper itself

Abstract

backgroundAcetyl xylan esterase plays an important role in the complete enzymatic hydrolysis of lignocellulosic materials. It hydrolyzes the ester linkages of acetic acid in xylan and supports and enhances the activity of xylanase. This study was conducted to identify and overexpress the acetyl xylan esterase (AXE) gene revealed by the genomic sequencing of the marine bacterium Ochrovirga pacifica.

resultsThe AXE gene has an 864-bp open reading frame that encodes 287 aa and consists of an AXE domain from aa 60 to 274. Gene was cloned to pET-16b vector and expressed the recombinant AXE (rAXE) in Escherichia coli BL21 (DE3). The predicted molecular mass was 31.75 kDa. The maximum specific activity (40.08 U/mg) was recorded at the optimal temperature and pH which were 50 °C and pH 8.0, respectively. The thermal stability assay showed that AXE maintains its residual activity almost constantly throughout and after incubation at 45 °C for 120 min. The synergism of AXE with xylanase on beechwood xylan, increased the relative activity 1.41-fold.

conclusionResulted higher relative activity of rAXE with commercially available xylanase on beechwood xylan showed its potential for the use of rAXE in industrial purposes as a de-esterification enzyme to hydrolyze xylan and hemicellulose-like complex substrates.

Indexed as

AcetylesteraseAmino Acid SequenceBacterial ProteinsBase SequenceEndo-1,4-beta XylanasesEnzyme StabilityFagusFlavobacteriaceaeHydrogen-Ion ConcentrationHydrolysisIndustrial MicrobiologyOpen Reading FramesSeawaterSubstrate SpecificityTemperatureXylansAcetylesteraseacetylxylan esteraseBacterial ProteinsEndo-1,4-beta XylanasesXylansAcetyl xylan esteraseBeech wood xylanMarine bacteriaOchrovirga pacificaSynergism

Identifiers

PMID31286972
PMCPMC6615230
OpenAlexW2958536934

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.