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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2022-12-01
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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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