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

doi:10.1371/journal.pone.0120156

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

Department of Materials Science and Engineering

Research output: Contribution to journal › Article

29 Citations (Scopus)

Abstract

(JKL) 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) (k _cat /K _m = 17.5 s ^-1 μM ^-1 ) and 2,6-dimethoxyphenol (k _cat /K _m = 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.

Original language	English
Article number	e0120156
Journal	PloS one
Volume	10
Issue number	3
DOIs	https://doi.org/10.1371/journal.pone.0120156
Publication status	Published - 2015 Mar 17

Fingerprint

ASJC Scopus subject areas

Biochemistry, Genetics and Molecular Biology(all)
Agricultural and Biological Sciences(all)

Cite this

Kalyani, D., Tiwari, M. K., Li, J., Kim, S. C., Kalia, V. C., Kang, Y. C., & Lee, J. K. (2015). A highly efficient recombinant laccase from the yeast Yarrowia lipolytica and its application in the hydrolysis of biomass. PloS one, 10(3), [e0120156]. https://doi.org/10.1371/journal.pone.0120156

@article{cbacfe25a343449dbf394c2ef685c5c2,

title = "A highly efficient recombinant laccase from the yeast Yarrowia lipolytica and its application in the hydrolysis of biomass",

abstract = " (JKL) 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) (k cat /K m = 17.5 s -1 μM -1 ) and 2,6-dimethoxyphenol (k cat /K m = 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. ",

author = "Dayanand Kalyani and Tiwari, {Manish Kumar} and Jinglin Li and Kim, {Sun Chang} and Kalia, {Vipin C.} and Kang, {Yun Chan} and Lee, {Jung Kul}",

year = "2015",

month = mar

day = "17",

doi = "10.1371/journal.pone.0120156",

language = "English",

volume = "10",

journal = "PLoS One",

issn = "1932-6203",

publisher = "Public Library of Science",

number = "3",

}

TY - JOUR

T1 - A highly efficient recombinant laccase from the yeast Yarrowia lipolytica and its application in the hydrolysis of biomass

AU - Kalyani, Dayanand

AU - Tiwari, Manish Kumar

AU - Li, Jinglin

AU - Kim, Sun Chang

AU - Kalia, Vipin C.

AU - Kang, Yun Chan

AU - Lee, Jung Kul

PY - 2015/3/17

Y1 - 2015/3/17

N2 - (JKL) 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) (k cat /K m = 17.5 s -1 μM -1 ) and 2,6-dimethoxyphenol (k cat /K m = 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.

AB - (JKL) 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) (k cat /K m = 17.5 s -1 μM -1 ) and 2,6-dimethoxyphenol (k cat /K m = 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.

UR - http://www.scopus.com/inward/record.url?scp=84924940447&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84924940447&partnerID=8YFLogxK

U2 - 10.1371/journal.pone.0120156

DO - 10.1371/journal.pone.0120156

M3 - Article

C2 - 25781945

AN - SCOPUS:84924940447

VL - 10

JO - PLoS One

JF - PLoS One

SN - 1932-6203

IS - 3

M1 - e0120156

ER -

Access to Document

10.1371/journal.pone.0120156