Evidence map›Paper›PMID 29362921›Full record

ArticleMarine biotechnology (New York, N.Y.)2018

Cloning, Expression, and Biochemical Characterization of Two New Oligoalginate Lyases with Synergistic Degradation Capability.

Shangyong Li, Linna Wang, Xuehong Chen, Wenwen Zhao, Mi Sun, Yantao Han

Abstract read
PubMed Publisher
In one paragraph

Article in Marine biotechnology (New York, N.Y.), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
8.2field-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

16 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
  2. Article
  3. Three alginate lyases provide a new gutApplied and environmental microbiology · 2023
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. 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

6 authors at 2 institutions in 1 country.

Shangyong LiDepartment of Pharmacology, College of basic Medicine, Qingdao University, Qingdao, 266071, China.
Linna WangYellow Sea Fisheries Research Institute, Key Laboratory for Sustainable Development of Marine Fisheries, Ministry of Agriculture, Chinese Academy of Fishery Sciences, Qingdao, 266071, China.
Xuehong ChenDepartment of Pharmacology, College of basic Medicine, Qingdao University, Qingdao, 266071, China. chen-xuehong@163.com.
Wenwen ZhaoDepartment of Pharmacology, College of basic Medicine, Qingdao University, Qingdao, 266071, China.
Mi SunYellow Sea Fisheries Research Institute, Key Laboratory for Sustainable Development of Marine Fisheries, Ministry of Agriculture, Chinese Academy of Fishery Sciences, Qingdao, 266071, China.
Yantao HanDepartment of Pharmacology, College of basic Medicine, Qingdao University, Qingdao, 266071, China. hanyt@qdu.edu.cn.
Qingdao University · CNChinese Academy of Fishery Sciences · CN

Funding

National Natural Science Foundation of China 81473384
6 · The paper itself

Abstract

Alginate, the most abundant carbohydrate presents in brown macroalgae, has recently gained increasing attention as an alternative biomass for the production of biofuel. Oligoalginate lyases catalyze the degradation of alginate oligomers into monomers, a prerequisite for bioethanol production. In this study, two new oligoalginate lyase genes, oalC6 and oalC17, were cloned from Cellulophaga sp. SY116, and expressed them in Escherichia coli. The deduced oligoalginate lyases, OalC6 and OalC17, belonged to the polysaccharide lyase (PL) family 6 and 17, respectively. Both showed less than 50% amino acid identity with all of the characterized oligoalginate lyases. Moreover, OalC6 and OalC17 could degrade both alginate polymers and oligomers into monomers in an exolytic mode. Substrate specificity studies demonstrated that OalC6 preferred α-L-guluronate (polyG) blocks, while OalC17 preferred poly β-D-mannuronate (polyM) blocks. The combination of OalC6 and OalC17 showed synergistic degradation ability toward both alginate polymers and oligomers. Finally, an efficient process for the production of alginate monomers was established by combining the new-isolated exotype alginate lyases (i.e., OalC6 and OalC17) and the endotype alginate lyase AlySY08. Overall, our work provides new insights for the development of novel biotechnologies for biofuel production from seaweed.

Indexed as

AlginatesAmino Acid SequenceBacterial ProteinsBiofuelsBiotechnologyCloning, MolecularEscherichia coliFlavobacteriaceaePolysaccharide-LyasesSeaweedSubstrate SpecificityAlginatesBacterial ProteinsBiofuelspoly(beta-D-mannuronate) lyasePolysaccharide-LyasesAlginate monomerCellulophaga sp. SY116Oligoalginate lyasesSynergistic degradation

Identifiers

PMID29362921
OpenAlexW2789570579

What OpenQuestion holds

Textmetadata
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.