ArticleBiotechnology for biofuels2011
Thermostable recombinant xylanases from Nonomuraea flexuosa and Thermoascus aurantiacus show distinct properties in the hydrolysis of xylans and pretreated wheat straw.
Article in Biotechnology for biofuels, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 97 citations in OpenAlex.
- Strategies for GH functional annotation: toward harmonized and predictive CAZymology.Biotechnology for biofuels and bioproducts · 2026Article
- Mechanism that allows manno-oligosaccharide to promote cellulose degradation by the bacterial community and the composting of cow manure with straw.Environmental science and pollution research international · 2022Article
- Characterization and structural analysis of a thermophilic GH11 xylanase from compost metatranscriptome.Applied microbiology and biotechnology · 2021Article
- Feed endoxylanase type and dose affect arabinoxylan hydrolysis and fermentation in ageing broilers.Animal nutrition (Zhongguo xu mu shou yi xue hui) · 2021Article
- Efficient Enzymatic Hydrolysis of Biomass Hemicellulose in the Absence of Bulk Water.Molecules (Basel, Switzerland) · 2019Article
- High-Level Heterologous Expression of Endo-1,4-β-Xylanase fromMolecules (Basel, Switzerland) · 2019Article
- Biochemical Characteristics of Microbial Enzymes and Their Significance from Industrial Perspectives.Molecular biotechnology · 2019Review
- Discovery of a Thermostable GH10 Xylanase with Broad Substrate Specificity from the Arctic Mid-Ocean Ridge Vent System.Applied and environmental microbiology · 2019Article
- Improvement in catalytic activity and thermostability of a GH10 xylanase and its synergistic degradation of biomass with cellulase.Biotechnology for biofuels · 2019Article
- Characterization of a novel thermostable and xylose-tolerant GH 39 β-xylosidase from Dictyoglomus thermophilum.BMC biotechnology · 2018Article
- Insight into the cold adaptation and hemicellulose utilization of Cladosporium neopsychrotolerans from genome analysis and biochemical characterization.Scientific reports · 2018Article
- Review: Engineering of thermostable enzymes for industrial applications.APL bioengineering · 2018Review
- Expression of a RecombinantFrontiers in microbiology · 2018Article
- A novel trifunctional, family GH10 enzyme from Acidothermus cellulolyticus 11B, exhibiting endo-xylanase, arabinofuranosidase and acetyl xylan esterase activities.Extremophiles : life under extreme conditions · 2018Article
- Insight into the functional roles of Glu175 in the hyperthermostable xylanase XYL10C-ΔN through structural analysis and site-saturation mutagenesis.Biotechnology for biofuels · 2018Article
- Article
- Purification, characterization, gene cloning and expression of GH-10 xylanase (Penicillium citrinum isolate HZN13).3 Biotech · 2016Article
- Article
- Heterogeneous Expression and Functional Characterization of Cellulose-Degrading Enzymes from Aspergillus niger for Enzymatic Hydrolysis of Alkali Pretreated Bamboo Biomass.Molecular biotechnology · 2015Article
- Characterization of a xylanase-producing Cellvibrio mixtus strain J3-8 and its genome analysis.Scientific reports · 2015Article
Corrections and comments
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Authors and funding
6 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundIn 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.
resultsThe xylanases from Nonomuraea flexuosa (Nf Xyn11A) and from Thermoascus aurantiacus (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.
conclusionsBecause of its high catalytic activity and good thermostability, T. aurantiacus xylanase shows great potential for applications aimed at total hydrolysis of lignocellulosic materials for platform sugars, whereas N. flexuosa xylanase shows more significant potential for the production of XOSs.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.