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) (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.
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) (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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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 -