Please use this identifier to cite or link to this item: http://hdl.handle.net/1843/55171
Type: Artigo de Periódico
Title: Trametes villosa Lignin Peroxidase (TvLiP): genetic and molecular characterization
Authors: Rita Terezinha de Oliveira Carneiro
Maíza Alves Lopes
Marília Lôrdelo Cardoso Silva
Verônica da Silva Santos
Volnei Brito de Souza
Aurizângela Oliveira de Sousa
Carlos Priminho Pirovani
Maria Gabriela Bello Koblitz
Raquel Guimarães Benevides
Aristóteles Góes Neto
Abstract: White-rot basidiomycetes are the organisms that decompose lignin most efficiently, and Trametes villosa is a promising species for ligninolytic enzyme production. There are several publications on T. villosa 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 T. villosa 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 7th day, and the ABSA medium (agar, sugarcane bagasse, and ammonium sulfate) was the best that favored LiP expression. The amplification of the TvLiP gene median region covering approximately 50% of the T. versicolor LPGIV gene (87% identity); the presence of Trp199, Leu115, Asp193, Trp199, and Ala203 in the translated amplicon of the T. villosa mRNA; and the close phylogenetic relationship between TvLiP and T. versicolor LiP all indicate that the target enzyme is a lignin peroxidase. Therefore, T. villosa CCMB561 has great potential for use as a LiP, MnP, and Lac producer for industrial applications.
Subject: Lignina
Enzimas
Basidiomycota - enzimologia
language: eng
metadata.dc.publisher.country: Brasil
Publisher: Universidade Federal de Minas Gerais
Publisher Initials: UFMG
metadata.dc.publisher.department: ICB - DEPARTAMENTO DE MICROBIOLOGIA
Rights: Acesso Aberto
metadata.dc.identifier.doi: http://dx.doi.org/10.4014/jmb.1606.06055
URI: http://hdl.handle.net/1843/55171
Issue Date: 2017
metadata.dc.url.externa: https://www.jmb.or.kr/journal/view.html?doi=10.4014/jmb.1606.06055
metadata.dc.relation.ispartof: Journal of microbiology and biotechnology
Appears in Collections:Artigo de Periódico

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