Evidence map›Paper›PMID 31418101›Full record

ArticleBiotechnology letters2019

Characterization of a bifunctional alginate lyase as a new member of the polysaccharide lyase family 17 from a marine strain BP-2.

Guiyuan Huang, Shunhua Wen, Siming Liao, Qiaozhen Wang, Shihan Pan, Rongcan Zhang, Fu Lei, Wei Liao, Jie Feng, Shushi Huang

Open access · hybridAbstract read
In one paragraph

Article in Biotechnology letters, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
6.8field-weighted citation impact, top 3% 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

21 citing papers in PubMed, 46 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 1 country.

Guiyuan HuangGuangxi Key Laboratory of Marine Natural Products and Combinatorial Biosynthesis Chemistry, Guangxi Academy of Sciences, Nanning, China.
Shunhua WenGuangxi Key Laboratory of Marine Natural Products and Combinatorial Biosynthesis Chemistry, Guangxi Academy of Sciences, Nanning, China.
Siming LiaoNational Engineering Research Center for Non-Food Biorefinery, State Key Laboratory of Non-Food Biomass and Enzyme Technology, Guangxi Key Laboratory of Bio-refinery, Guangxi Academy of Sciences, Nanning, China.
Qiaozhen WangGuangxi Key Laboratory of Marine Natural Products and Combinatorial Biosynthesis Chemistry, Guangxi Academy of Sciences, Nanning, China.
Shihan PanGuangxi Key Laboratory of Marine Natural Products and Combinatorial Biosynthesis Chemistry, Guangxi Academy of Sciences, Nanning, China.
Rongcan ZhangGuangxi Key Laboratory of Marine Natural Products and Combinatorial Biosynthesis Chemistry, Guangxi Academy of Sciences, Nanning, China.
Fu LeiGuangxi Key Laboratory of Marine Natural Products and Combinatorial Biosynthesis Chemistry, Guangxi Academy of Sciences, Nanning, China.
Wei LiaoGuangxi Key Laboratory of Marine Natural Products and Combinatorial Biosynthesis Chemistry, Guangxi Academy of Sciences, Nanning, China.
Jie FengSchool of Pharmaceutical Science, Guangxi Medical University, Nanning, 530021, China.
Shushi HuangGuangxi Key Laboratory of Marine Natural Products and Combinatorial Biosynthesis Chemistry, Guangxi Academy of Sciences, Nanning, China. hshushi@gxas.cn.
Guangxi Academy of Sciences · CNGuangxi Medical University · CNGuangxi University · CN

Funding

National Natural Science Foundation of China 31560017
6 · The paper itself

Abstract

objectivesBifunctional alginate lyase can efficiently saccharify alginate biomass and prepare functional oligosaccharides of alginate.

resultsA new BP-2 strain that produces alginate lyase was screened and identified from rotted Sargassum. A new alginate lyase, Alg17B, belonging to the polysaccharide lyase family 17, was isolated and purified from BP-2 fermentation broth by freeze-drying, dialysis, and ion exchange chromatography. The enzymatic properties of the purified lyase were investigated. The molecular weight of Alg17B was approximately 77 kDa, its optimum reaction temperature was 40-45 °C, and its optimum reaction pH was 7.5-8.0. The enzyme was relatively stable at pH 7.0-8.0, with a temperature range of 25-35 °C, and the specific activity of the purified enzyme reached 4036 U/mg. A low Na

conclusionsAlg17B can be used to saccharify the main carbohydrate, alginate, in the ethanolic production of brown algae fuel as well as in preparing and researching oligosaccharides.

Indexed as

AlginatesAlginic AcidAquatic OrganismsEnzyme ActivatorsEnzyme InhibitorsEnzyme StabilityGammaproteobacteriaHydrogen-Ion ConcentrationHydrolysisMolecular WeightMonosaccharidesOligosaccharidesPolysaccharide-LyasesPolysaccharides, BacterialSargassumSubstrate SpecificityAlginatesAlginic AcidEnzyme ActivatorsEnzyme InhibitorsMonosaccharidesOligosaccharidespoly(beta-D-mannuronate) lyasepolyguluronic acidPolysaccharide-LyasesPolysaccharides, BacterialAlginate oligosaccharidesBifunctional alginate lyaseBioenergyMarine strainPolysaccharide lyase family 17

Identifiers

PMID31418101
PMCPMC6742608
OpenAlexW2968837437

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.