ArticleBiotechnology for biofuels2014
A novel thermostable xylanase GH10 from Malbranchea pulchella expressed in Aspergillus nidulans with potential applications in biotechnology.
Article in Biotechnology for biofuels, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 80 citations in OpenAlex.
- Harnessing Xylanase Potential inJournal of fungi (Basel, Switzerland) · 2025Article
- Optimization and Characterization of an Ultra-Thermostable, Acidophilic, Cellulase-Free Xylanase from a New Obligate Thermophilic Geobacillus thermoleovorans AKNT10 and its Application in Saccharification of Wheat Bran.Current microbiology · 2024Article
- Recombinant GH3 β-glucosidase stimulated by xylose and tolerant to furfural and 5-hydroxymethylfurfural obtained from Aspergillus nidulans.Bioresources and bioprocessing · 2024Article
- Exploring the potential of a new thermotolerant xylanase from3 Biotech · 2024Article
- Immobilization and Application of the Recombinant Xylanase GH10 ofInternational journal of molecular sciences · 2022Article
- A Fungal Versatile GH10 Endoxylanase and Its Glycosynthase Variant: Synthesis of Xylooligosaccharides and Glycosides of Bioactive Phenolic Compounds.International journal of molecular sciences · 2022Article
- Utilization of Monosaccharides byMicroorganisms · 2021Article
- IncreasedBiotechnology reports (Amsterdam, Netherlands) · 2021Article
- Prospection of Fungal Lignocellulolytic Enzymes Produced from Jatoba (Microorganisms · 2021Article
- Co-cultivation, Co-culture, Mixed Culture, and Microbial Consortium of Fungi: An Understudied Strategy for Biomass Conversion.Frontiers in microbiology · 2021Article
- Expression, Characterization and Its Deinking Potential of a Thermostable Xylanase FromFrontiers in bioengineering and biotechnology · 2021Article
- A Highly Glucose Tolerant ß-Glucosidase from Malbranchea pulchella (MpBg3) Enables Cellulose Saccharification.Scientific reports · 2020Article
- Improvement of the catalytic activity and thermostability of a hyperthermostable endoglucanase by optimizing N-glycosylation sites.Biotechnology for biofuels · 2020Article
- Heterologous expression and functional characterization of a GH10 endoxylanase fromBiotechnology reports (Amsterdam, Netherlands) · 2019Article
- Matrix Discriminant Analysis Evidenced Surface-Lithium as an Important Factor to Increase the Hydrolytic Saccharification of Sugarcane Bagasse.Molecules (Basel, Switzerland) · 2019Article
- Thermostable Xylanase Production byMicroorganisms · 2018Article
- Effect of CBM1 and linker region on enzymatic properties of a novel thermostable dimeric GH10 xylanase (Xyn10A) from filamentous fungus Aspergillus fumigatus Z5.AMB Express · 2018Article
- Effects of substrate binding site residue substitutions of xynA from Bacillus amyloliquefaciens on substrate specificity.BMC biotechnology · 2018Article
- Deletion of Endo-β-1,4-XylanaseFrontiers in plant science · 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
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Authors and funding
14 authors at 5 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundThe search for novel thermostable xylanases for industrial use has intensified in recent years, and thermophilic fungi are a promising source of useful enzymes. The present work reports the heterologous expression and biochemical characterization of a novel thermostable xylanase (GH10) from the thermophilic fungus Malbranchea pulchella, the influence of glycosylation on its stability, and a potential application in sugarcane bagasse hydrolysis.
resultsXylanase MpXyn10A was overexpressed in Aspergillus nidulans and was active against birchwood xylan, presenting an optimum activity at pH 5.8 and 80°C. MpXyn10A was 16% glycosylated and thermostable, preserving 85% activity after 24 hours at 65°C, and deglycosylation did not affect thermostability. Circular dichroism confirmed the high alpha-helical content consistent with the canonical GH10 family (β/α)8 barrel fold observed in molecular modeling. Primary structure analysis revealed the existence of eight cysteine residues which could be involved in four disulfide bonds, and this could explain the high thermostability of this enzyme even in the deglycosylated form. MpXyn10A showed promising results in biomass degradation, increasing the amount of reducing sugars in bagasse in natura and in three pretreated sugarcane bagasses.
conclusionsMpXyn10A was successfully secreted in Aspergillus nidulans, and a potential use for sugarcane bagasse biomass degradation was demonstrated.
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