Trametes villosa Lignin Peroxidase (TvLiP): Genetic and Molecular Characterization

• Published in: Journal of microbiology and biotechnology Vol. 27; no. 1; pp. 179 - 188
• Main Authors: de Oliveira Carneiro, Rita Terezinha, Lopes, Maíza Alves, Silva, Marília Lordelo Cardoso, Santos, Verônica da Silva, de Souza, Volnei Brito, de Sousa, Aurizangela Oliveira, Pirovani, Carlos Priminho, Koblitz, Maria Gabriela Bello, Benevides, Raquel Guimarães, Góes-Neto, Aristóteles
• Format: Journal Article
• Language: English
• Published: Korea (South) 한국미생물·생명공학회 28.01.2017
• Subjects: 생물학; white-rot basidiomycetes; Lignin; ligninolytic enzymes
• ISSN: 1017-7825; 1738-8872
• DOI: 10.4014/jmb.1606.06055

White-rot basidiomycetes are the organisms that decompose lignin most efficiently, and is a promising species for ligninolytic enzyme production. There are several publications on applications for lignin degradation regarding the expression and secretion of laccase and manganese peroxidase (MnP) but no reports on the identification and characterization of lignin peroxidase (LiP), a relevant enzyme for the efficient breakdown of lignin. The object of this study was to identify and partially characterize, for the first time, gDNA, mRNA, and the corresponding lignin peroxidase (TvLiP) protein from strain CCMB561 from the Brazilian semiarid region. The presence of ligninolytic enzymes produced by this strain grown in inducer media was qualitatively and quantitatively analyzed by spectrophotometry, qPCR, and dye fading using Remazol Brilliant Blue R. The spectrophotometric analysis showed that LiP activity was higher than that of MnP. The greatest LiP expression as measured by qPCR occurred on the 7 day, and the ABSA medium (agar, sugarcane bagasse, and ammonium sulfate) was the best that favored LiP expression. The amplification of the gene median region covering approximately 50% of the gene (87% identity); the presence of Trp199, Leu115, Asp193, Trp199, and Ala203 in the translated amplicon of the mRNA; and the close phylogenetic relationship between TvLiP and LiP all indicate that the target enzyme is a lignin peroxidase. Therefore, CCMB561 has great potential for use as a LiP, MnP, and Lac producer for industrial applications.