Thermostable recombinant xylanases from <it>Nonomuraea flexuosa </it>and <it>Thermoascus aurantiacus </it>show distinct properties in the hydrolysis of xylans and pretreated wheat straw

<p>Abstract</p> <p>Background</p> <p>In the hydrolysis of lignocellulosic materials, thermostable enzymes decrease the amount of enzyme needed due to higher specific activity and elongate the hydrolysis time due to improved stability. For cost-efficient use of enzymes i...

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Main Authors: Tenkanen Maija, Tang Ming, Puranen Terhi, Siika-aho Matti, Zhang Junhua, Viikari Liisa
Format: Article
Language:English
Published: BMC 2011-05-01
Series:Biotechnology for Biofuels
Online Access:http://www.biotechnologyforbiofuels.com/content/4/1/12
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author Tenkanen Maija
Tang Ming
Puranen Terhi
Siika-aho Matti
Zhang Junhua
Viikari Liisa
author_facet Tenkanen Maija
Tang Ming
Puranen Terhi
Siika-aho Matti
Zhang Junhua
Viikari Liisa
author_sort Tenkanen Maija
collection DOAJ
description <p>Abstract</p> <p>Background</p> <p>In the hydrolysis of lignocellulosic materials, thermostable enzymes decrease the amount of enzyme needed due to higher specific activity and elongate the hydrolysis time due to improved stability. For cost-efficient use of enzymes in large-scale industrial applications, high-level expression of enzymes in recombinant hosts is usually a prerequisite. The main aim of the present study was to compare the biochemical and hydrolytic properties of two thermostable recombinant glycosyl hydrolase families 10 and 11 (GH10 and GH11, respectively) xylanases with respect to their potential application in the hydrolysis of lignocellulosic substrates.</p> <p>Results</p> <p>The xylanases from <it>Nonomuraea flexuosa </it>(Nf Xyn11A) and from <it>Thermoascus aurantiacus </it>(Ta Xyn10A) were purified by heat treatment and gel permeation chromatography. Ta Xyn10A exhibited higher hydrolytic efficiency than Nf Xyn11A toward birchwood glucuronoxylan, insoluble oat spelt arabinoxylan and hydrothermally pretreated wheat straw, and it produced more reducing sugars. Oligosaccharides from xylobiose to xylopentaose as well as higher degree of polymerization (DP) xylooligosaccharides (XOSs), but not xylose, were released during the initial hydrolysis of xylans by Nf Xyn11A, indicating its potential for the production of XOS. The mode of action of Nf Xyn11A and Ta Xyn10A on glucuronoxylan and arabinoxylan showed typical production patterns of endoxylanases belonging to GH11 and GH10, respectively.</p> <p>Conclusions</p> <p>Because of its high catalytic activity and good thermostability, <it>T. aurantiacus </it>xylanase shows great potential for applications aimed at total hydrolysis of lignocellulosic materials for platform sugars, whereas <it>N. flexuosa </it>xylanase shows more significant potential for the production of XOSs.</p>
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spelling doaj.art-d539e228410e4c25b2c8c957ace14dbf2022-12-22T02:34:41ZengBMCBiotechnology for Biofuels1754-68342011-05-01411210.1186/1754-6834-4-12Thermostable recombinant xylanases from <it>Nonomuraea flexuosa </it>and <it>Thermoascus aurantiacus </it>show distinct properties in the hydrolysis of xylans and pretreated wheat strawTenkanen MaijaTang MingPuranen TerhiSiika-aho MattiZhang JunhuaViikari Liisa<p>Abstract</p> <p>Background</p> <p>In the hydrolysis of lignocellulosic materials, thermostable enzymes decrease the amount of enzyme needed due to higher specific activity and elongate the hydrolysis time due to improved stability. For cost-efficient use of enzymes in large-scale industrial applications, high-level expression of enzymes in recombinant hosts is usually a prerequisite. The main aim of the present study was to compare the biochemical and hydrolytic properties of two thermostable recombinant glycosyl hydrolase families 10 and 11 (GH10 and GH11, respectively) xylanases with respect to their potential application in the hydrolysis of lignocellulosic substrates.</p> <p>Results</p> <p>The xylanases from <it>Nonomuraea flexuosa </it>(Nf Xyn11A) and from <it>Thermoascus aurantiacus </it>(Ta Xyn10A) were purified by heat treatment and gel permeation chromatography. Ta Xyn10A exhibited higher hydrolytic efficiency than Nf Xyn11A toward birchwood glucuronoxylan, insoluble oat spelt arabinoxylan and hydrothermally pretreated wheat straw, and it produced more reducing sugars. Oligosaccharides from xylobiose to xylopentaose as well as higher degree of polymerization (DP) xylooligosaccharides (XOSs), but not xylose, were released during the initial hydrolysis of xylans by Nf Xyn11A, indicating its potential for the production of XOS. The mode of action of Nf Xyn11A and Ta Xyn10A on glucuronoxylan and arabinoxylan showed typical production patterns of endoxylanases belonging to GH11 and GH10, respectively.</p> <p>Conclusions</p> <p>Because of its high catalytic activity and good thermostability, <it>T. aurantiacus </it>xylanase shows great potential for applications aimed at total hydrolysis of lignocellulosic materials for platform sugars, whereas <it>N. flexuosa </it>xylanase shows more significant potential for the production of XOSs.</p>http://www.biotechnologyforbiofuels.com/content/4/1/12
spellingShingle Tenkanen Maija
Tang Ming
Puranen Terhi
Siika-aho Matti
Zhang Junhua
Viikari Liisa
Thermostable recombinant xylanases from <it>Nonomuraea flexuosa </it>and <it>Thermoascus aurantiacus </it>show distinct properties in the hydrolysis of xylans and pretreated wheat straw
Biotechnology for Biofuels
title Thermostable recombinant xylanases from <it>Nonomuraea flexuosa </it>and <it>Thermoascus aurantiacus </it>show distinct properties in the hydrolysis of xylans and pretreated wheat straw
title_full Thermostable recombinant xylanases from <it>Nonomuraea flexuosa </it>and <it>Thermoascus aurantiacus </it>show distinct properties in the hydrolysis of xylans and pretreated wheat straw
title_fullStr Thermostable recombinant xylanases from <it>Nonomuraea flexuosa </it>and <it>Thermoascus aurantiacus </it>show distinct properties in the hydrolysis of xylans and pretreated wheat straw
title_full_unstemmed Thermostable recombinant xylanases from <it>Nonomuraea flexuosa </it>and <it>Thermoascus aurantiacus </it>show distinct properties in the hydrolysis of xylans and pretreated wheat straw
title_short Thermostable recombinant xylanases from <it>Nonomuraea flexuosa </it>and <it>Thermoascus aurantiacus </it>show distinct properties in the hydrolysis of xylans and pretreated wheat straw
title_sort thermostable recombinant xylanases from it nonomuraea flexuosa it and it thermoascus aurantiacus it show distinct properties in the hydrolysis of xylans and pretreated wheat straw
url http://www.biotechnologyforbiofuels.com/content/4/1/12
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