Evidence map›Paper›PMID 30456695›Full record

ArticleMarine biotechnology (New York, N.Y.)2019

Production, Gene Cloning, and Overexpression of a Laccase in the Marine-Derived Yeast Aureobasidium melanogenum Strain 11-1 and Characterization of the Recombinant Laccase.

Thu Aung, Hong Jiang, Cheng-Cheng Chen, Guang-Lei Liu, Zhong Hu, Zhen-Ming Chi, Zhe Chi

Abstract read
PubMed Publisher
In one paragraph

Article in Marine biotechnology (New York, N.Y.), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
3.7field-weighted citation impact, top 7% 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

9 citing papers in PubMed, 23 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Characterization of a New Laccase fromMolecules (Basel, Switzerland) · 2023
    Article
  5. Article
  6. Article
  7. Novel Cold-Adapted Recombinant Laccase KbLcc1 fromInternational journal of molecular sciences · 2021
    Article
  8. Article
  9. Cloning Method for Stress-Resistant Gene ofJournal of healthcare engineering · 2021
    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

7 authors at 3 institutions in 1 country.

Thu AungKey Laboratory of Marine Genetics and Breeding (Ocean University of China), Ministry of Education, Yushan Road, No. 5, Qingdao, China.
Hong JiangKey Laboratory of Marine Genetics and Breeding (Ocean University of China), Ministry of Education, Yushan Road, No. 5, Qingdao, China.
Cheng-Cheng ChenKey Laboratory of Marine Genetics and Breeding (Ocean University of China), Ministry of Education, Yushan Road, No. 5, Qingdao, China.
Guang-Lei LiuKey Laboratory of Marine Genetics and Breeding (Ocean University of China), Ministry of Education, Yushan Road, No. 5, Qingdao, China.
Zhong HuDepartment of Biology, Shantou University, Shantou, China.
Zhen-Ming ChiKey Laboratory of Marine Genetics and Breeding (Ocean University of China), Ministry of Education, Yushan Road, No. 5, Qingdao, China. zhenming@sdu.edu.cn.
Zhe ChiKey Laboratory of Marine Genetics and Breeding (Ocean University of China), Ministry of Education, Yushan Road, No. 5, Qingdao, China. cz1108@ouc.edu.cn.
Ocean University of China · CNQingdao National Laboratory for Marine Science and Technology · CNShantou University · CN

Funding

National Natural Science Foundation of China (CN) 31561163001
6 · The paper itself

Abstract

Aureobasidium melanogenum strain 11-1 with a high laccase activity was isolated from a mangrove ecosystem. Under the optimal conditions, the 11-1 strain yielded the highest laccase activity up to 3120.0 ± 170 mU/ml (1.2 U/mg protein) within 5 days. A laccase gene (LAC1) of the yeast strain 11-1 contained two introns and encoded a protein with 570 amino acids and four conserved copper-binding domains typical of the fungal laccase. Expression of the LAC1 gene in the yeast strain 11-1 made a recombinant yeast strain produce the laccase activity of 6005 ± 140 mU/ml. The molecular weight of the recombinant laccase after removing the sugar was about 62.5 kDa. The optimal temperature and pH of the recombinant laccase were 40 °C and 3.2, respectively, and it was stable at a temperature less than 25 °C. The laccase was inhibited in the presence of sodium dodecyl sulfate (SDS), ethylenediaminetetraacetic acid (EDTA), phenylmethanesulfonyl fluoride (PMSF), and DL-dithiothreitol (DTT). The K

Indexed as

Aquatic OrganismsAmino Acid SequenceBase SequenceCloning, MolecularFungal ProteinsGene ExpressionHydrogen-Ion ConcentrationKineticsLaccaseMolecular WeightPhylogenyPlasmidsRecombinant ProteinsSaccharomycetalesSequence AlignmentSequence Homology, Amino AcidFungal ProteinsLaccaseRecombinant ProteinsAureobasidium melanogenumDecolorizing abilityLAC1 geneLaccaseOverexpression

Identifiers

PMID30456695
OpenAlexW2901953248

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.