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Cited by 60Enzyme-mediated dye degradationBiofuel production and bioconversionEnzyme Production and Characterization

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A Highly Efficient Recombinant Laccase from the Yeast Yarrowia lipolytica and Its Application in the Hydrolysis of Biomass

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Kalyani, Dayanand, Tiwari, Manish Kumar, Li, Jinglin, Kim, Sun Chang, Kalia, Vipin C., Kang, Yun Chan, Lee, Jung-Kul·2015·PLOS ONE
DOI 10.1371/journal.pone.0120156PMC PMC4363317
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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.

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  • Laccases have been expressed in hosts including Saccharomyces cerevisiae, Yarrowia lipolytica, Pichia pastoris, Kluyveromyces lactis, Aspergillus niger, Aspergillus sojae, and Trichoderma reesei.

    “Laccases have expressed in hosts as Saccharomyces cerevisiae [228], Yarrowia lipolytica [229], Pichia pastoris [44,204,230,231,232], Kluyveromyces lactis [233] and even filamentous fungi such as Aspergillus niger [234], Aspergillus sojae [235], and Trichoderma reesei [236].”

    From A Brief History of Colour, the Environmental Impact of Synthetic Dyes and Removal by Using Laccases (2021) · cites this paper as [229]

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Metadata

Authors
Kalyani, D., Tiwari, M. K., Li, J., Kim, S. C., Kalia, V. C., Kang, Y. C., & Lee, J.-K.
Affiliations
  • Konkuk University (KR)
  • Korea Advanced Institute of Science and Technology (KR)
  • University of Delhi (IN)
  • Korea University (KR)
Corresponding author
  • Kang, Yun Chan
  • Lee, Jung-Kul
ORCID
Venue
PLOS ONE
Publisher
Public Library of Science (PLoS)
Published
2015-03-17
Volume
10
Issue
3
Pages
e0120156
ISSN
1932-6203 (ISSN-L)
DOI
10.1371/journal.pone.0120156
PMC
PMC4363317
OpenAlex
W1980668517
Cited by
60
References
1
Citations by year
2026: 4 · 2025: 3 · 2024: 5 · 2023: 7 · 2022: 3 · 2021: 10 · 2020: 4 · 2019: 5 · 2018: 3 · 2017: 8 · 2016: 5 · 2015: 3
FWCI
7.66
Type
journal article
Language
en
Open access
Licence
Locations
  • PLoS ONE (publishedVersion, cc-by)
  • Europe PMC (PubMed Central) (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
  • Figshare (submittedVersion, cc-by)
Funders
  • Konkuk University
  • Ministry of Science, ICT and Future Planning (2011-0031955)
  • Korea Institute of Energy Technology Evaluation and Planning (201320200000420)
Topics
  • Life Sciences › Immunology and Microbiology › Applied Microbiology and Biotechnology › Enzyme-mediated dye degradation
  • Physical Sciences › Engineering › Biomedical Engineering › Biofuel production and bioconversion
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Enzyme Production and Characterization
Keywords
laccase, Yarrowia lipolytica, recombinant laccase, Pichia pastoris expression, cDNA cloning, catalytic efficiency, redox potential, phenol removal, Populus balsamifera, saccharification, lignocellulose hydrolysis
MeSH terms
Fungal Proteins, Hydrolysis, Pichia, Recombinant Proteins, Wood, Biomass, Yarrowia, Populus, Laccase

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