Evidence map›Paper›PMID 25781945›Full record

ArticlePloS one2015

A highly efficient recombinant laccase from the yeast Yarrowia lipolytica and its application in the hydrolysis of biomass.

Dayanand Kalyani, Manish Kumar Tiwari, Jinglin Li, Sun Chang Kim, Vipin C Kalia, Yun Chan Kang, Jung-Kul Lee

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
9.8field-weighted citation impact, top 2% 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

17 citing papers in PubMed, 58 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Biotin and ZnIndian journal of microbiology · 2021
    Article
  6. Review
  7. Review
  8. Article
  9. Heterologous Expression of Laccase FromFrontiers in microbiology · 2020
    Article
  10. Article
  11. Article
  12. Article
  13. Recovery of laccase-producing gammaproteobacteria from wastewater.Biotechnology reports (Amsterdam, Netherlands) · 2019
    Article
  14. Article
  15. Article
  16. Diverse Metabolic Capacities of Fungi for Bioremediation.Indian journal of microbiology · 2016
    Review
  17. Review
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 4 institutions in 2 countries.

Dayanand KalyaniDepartment of Chemical Engineering, Konkuk University, Seoul, Korea.
Manish Kumar TiwariDepartment of Chemical Engineering, Konkuk University, Seoul, Korea.
Jinglin LiDepartment of Chemical Engineering, Konkuk University, Seoul, Korea.
Sun Chang KimDepartment of Biological Sciences, Korea Advanced Institute of Science and Technology, Yuseong-gu, Daejeon, Korea.
Vipin C KaliaMicrobial Biotechnology and Genomics, CSIR-Institute of Genomics and Integrative Biology, Delhi University Campus, Delhi, India.
Yun Chan KangDepartment of Materials Science and Engineering, Korea University, Anam-Dong, Seongbuk-Gu, Seoul, Korea.
Jung-Kul LeeDepartment of Chemical Engineering, Konkuk University, Seoul, Korea.
Konkuk University · KRInstitute of Genomics and Integrative Biology · INKorea Advanced Institute of Science and Technology · KRKorea University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A modified thermal asymmetric interlaced polymerase chain reaction was performed to obtain the first yeast laccase gene (YlLac) from the isolated yeast Yarrowia lipolytica. The 1557-bp full-length cDNA of YlLac encoded a mature laccase protein containing 519 amino acids preceded by a signal peptide of 19 amino acids, and the YlLac gene was expressed in the yeast Pichia pastoris. YlLac is a monomeric glycoprotein with a molecular mass of ~55 kDa as determined by polyacrylamide-gel electrophoresis. It showed a higher catalytic efficiency towards 2,2-azino-bis(3-ethylbenzothiazoline-6-sulfonate) (kcat/Km = 17.5 s(-1) μM(-1)) and 2,6-dimethoxyphenol (kcat/Km = 16.1 s(-1) μM(-1)) than other reported laccases. The standard redox potential of the T1 site of the enzyme was found to be 772 mV. The highest catalytic efficiency of the yeast recombinant laccase, YlLac, makes it a good candidate for industrial applications: it removes phenolic compounds in acid-pretreated woody biomass (Populus balsamifera) and enhanced saccharification.

Indexed as

BiomassFungal ProteinsHydrolysisLaccasePichiaPopulusRecombinant ProteinsWoodYarrowiaFungal ProteinsLaccaseRecombinant Proteins

Identifiers

PMID25781945
PMCPMC4363317
OpenAlexW1980668517

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.