β-Xylosidase SRBX1 Activity from <i>Sporisorium reilianum</i> and Its Synergism with Xylanase SRXL1 in Xylose Release from Corn Hemicellulose

<i>Sposisorium reilianum</i> is the causal agent of corn ear smut disease. Eleven genes have been identified in its genome that code for enzymes that could constitute its hemicellulosic system, three of which have been associated with two Endo-β-1,4-xylanases and one with α-L-arabinofura...

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Main Authors: Yuridia Mercado-Flores, Alejandro Téllez-Jurado, Carlos Iván Lopéz-Gil, Miguel Angel Anducho-Reyes
Format: Article
Language:English
Published: MDPI AG 2022-12-01
Series:Journal of Fungi
Subjects:
Online Access:https://www.mdpi.com/2309-608X/8/12/1295
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author Yuridia Mercado-Flores
Alejandro Téllez-Jurado
Carlos Iván Lopéz-Gil
Miguel Angel Anducho-Reyes
author_facet Yuridia Mercado-Flores
Alejandro Téllez-Jurado
Carlos Iván Lopéz-Gil
Miguel Angel Anducho-Reyes
author_sort Yuridia Mercado-Flores
collection DOAJ
description <i>Sposisorium reilianum</i> is the causal agent of corn ear smut disease. Eleven genes have been identified in its genome that code for enzymes that could constitute its hemicellulosic system, three of which have been associated with two Endo-β-1,4-xylanases and one with α-L-arabinofuranosidase activity. In this study, the native protein extracellular with β-xylosidase activity, called SRBX1, produced by this basidiomycete was analyzed by performing production kinetics and its subsequent purification by gel filtration. The enzyme was characterized biochemically and sequenced. Finally, its synergism with Xylanase SRXL1 was determined. Its activity was higher in a medium with corn hemicellulose and glucose as carbon sources. The purified protein was a monomer associated with the <i>sr16700</i> gene, with a molecular weight of 117 kDa and optimal activity at 60 °C in a pH range of 4–7, which had the ability to hydrolyze the ρ-nitrophenyl β-D-xylanopyranoside and ρ-Nitrophenyl α-L-arabinofuranoside substrates. Its activity was strongly inhibited by silver ions and presented <i>Km</i> and <i>Vmax</i> values of 2.5 mM and 0.2 μmol/min/mg, respectively, using ρ-nitrophenyl β-D-xylanopyranoside as a substrate. The enzyme degrades corn hemicellulose and birch xylan in combination and in sequential synergism with the xylanase SRXL1.
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spelling doaj.art-b5a9a9e6cf60453fbe4bfd44db2c61bb2023-11-24T16:00:02ZengMDPI AGJournal of Fungi2309-608X2022-12-01812129510.3390/jof8121295β-Xylosidase SRBX1 Activity from <i>Sporisorium reilianum</i> and Its Synergism with Xylanase SRXL1 in Xylose Release from Corn HemicelluloseYuridia Mercado-Flores0Alejandro Téllez-Jurado1Carlos Iván Lopéz-Gil2Miguel Angel Anducho-Reyes3Dirección de Investigación, Innovación y Posgrado, Carretera Pachuca-Cd. Sahagún Km 20, Ex-Hacienda de Santa Bárbara, Universidad Politécnica de Pachuca, Zempoala 43830, Hidalgo, MexicoDirección de Investigación, Innovación y Posgrado, Carretera Pachuca-Cd. Sahagún Km 20, Ex-Hacienda de Santa Bárbara, Universidad Politécnica de Pachuca, Zempoala 43830, Hidalgo, MexicoDirección de Investigación, Innovación y Posgrado, Carretera Pachuca-Cd. Sahagún Km 20, Ex-Hacienda de Santa Bárbara, Universidad Politécnica de Pachuca, Zempoala 43830, Hidalgo, MexicoDirección de Investigación, Innovación y Posgrado, Carretera Pachuca-Cd. Sahagún Km 20, Ex-Hacienda de Santa Bárbara, Universidad Politécnica de Pachuca, Zempoala 43830, Hidalgo, Mexico<i>Sposisorium reilianum</i> is the causal agent of corn ear smut disease. Eleven genes have been identified in its genome that code for enzymes that could constitute its hemicellulosic system, three of which have been associated with two Endo-β-1,4-xylanases and one with α-L-arabinofuranosidase activity. In this study, the native protein extracellular with β-xylosidase activity, called SRBX1, produced by this basidiomycete was analyzed by performing production kinetics and its subsequent purification by gel filtration. The enzyme was characterized biochemically and sequenced. Finally, its synergism with Xylanase SRXL1 was determined. Its activity was higher in a medium with corn hemicellulose and glucose as carbon sources. The purified protein was a monomer associated with the <i>sr16700</i> gene, with a molecular weight of 117 kDa and optimal activity at 60 °C in a pH range of 4–7, which had the ability to hydrolyze the ρ-nitrophenyl β-D-xylanopyranoside and ρ-Nitrophenyl α-L-arabinofuranoside substrates. Its activity was strongly inhibited by silver ions and presented <i>Km</i> and <i>Vmax</i> values of 2.5 mM and 0.2 μmol/min/mg, respectively, using ρ-nitrophenyl β-D-xylanopyranoside as a substrate. The enzyme degrades corn hemicellulose and birch xylan in combination and in sequential synergism with the xylanase SRXL1.https://www.mdpi.com/2309-608X/8/12/1295head smutphytopathogenglycosyl hydrolasemultifunctional enzymes
spellingShingle Yuridia Mercado-Flores
Alejandro Téllez-Jurado
Carlos Iván Lopéz-Gil
Miguel Angel Anducho-Reyes
β-Xylosidase SRBX1 Activity from <i>Sporisorium reilianum</i> and Its Synergism with Xylanase SRXL1 in Xylose Release from Corn Hemicellulose
Journal of Fungi
head smut
phytopathogen
glycosyl hydrolase
multifunctional enzymes
title β-Xylosidase SRBX1 Activity from <i>Sporisorium reilianum</i> and Its Synergism with Xylanase SRXL1 in Xylose Release from Corn Hemicellulose
title_full β-Xylosidase SRBX1 Activity from <i>Sporisorium reilianum</i> and Its Synergism with Xylanase SRXL1 in Xylose Release from Corn Hemicellulose
title_fullStr β-Xylosidase SRBX1 Activity from <i>Sporisorium reilianum</i> and Its Synergism with Xylanase SRXL1 in Xylose Release from Corn Hemicellulose
title_full_unstemmed β-Xylosidase SRBX1 Activity from <i>Sporisorium reilianum</i> and Its Synergism with Xylanase SRXL1 in Xylose Release from Corn Hemicellulose
title_short β-Xylosidase SRBX1 Activity from <i>Sporisorium reilianum</i> and Its Synergism with Xylanase SRXL1 in Xylose Release from Corn Hemicellulose
title_sort β xylosidase srbx1 activity from i sporisorium reilianum i and its synergism with xylanase srxl1 in xylose release from corn hemicellulose
topic head smut
phytopathogen
glycosyl hydrolase
multifunctional enzymes
url https://www.mdpi.com/2309-608X/8/12/1295
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