ArticleBMC biotechnology2014
Highly thermostable GH39 β-xylosidase from a Geobacillus sp. strain WSUCF1.
Article in BMC biotechnology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Genomic and functional insights into the thermophilic strain Geobacillus sp. Geo 8.1: a source of thermostable xylanase for sustainable bioprocesses.World journal of microbiology & biotechnology · 2026Article
- A Thermotolerant YeastJournal of fungi (Basel, Switzerland) · 2024Article
- Review
- Ultrahigh-Throughput Screening of High-β-Xylosidase-ProducingJournal of fungi (Basel, Switzerland) · 2022Article
- Characterization of a highly xylose tolerant β-xylosidase isolated from high temperature horse manure compost.BMC biotechnology · 2021Article
- Novel xylanase producing3 Biotech · 2020Article
- Adaptive Enrichment of a Thermophilic Bacterial Isolate for Enhanced Enzymatic Activity.Microorganisms · 2020Article
- Co-production of Xylooligosaccharides and Xylose From Poplar Sawdust by Recombinant Endo-1,4-β-Xylanase and β-Xylosidase Mixture Hydrolysis.Frontiers in bioengineering and biotechnology · 2020Article
- β-Xylosidases: Structural Diversity, Catalytic Mechanism, and Inhibition by Monosaccharides.International journal of molecular sciences · 2019Review
- Expression of thermostable β-xylosidase in Escherichia coli for use in saccharification of plant biomass.Bioengineered · 2017Article
- Genome-Centric Analysis of a Thermophilic and Cellulolytic Bacterial Consortium Derived from Composting.Frontiers in microbiology · 2017Article
- Purification and characterization of an extracellular β-xylosidase from Pseudozyma hubeiensis NCIM 3574 (PhXyl), an unexplored yeast.AMB Express · 2016Article
- A multifunctional GH39 glycoside hydrolase from the anaerobic gut fungus Orpinomyces sp. strain C1A.PeerJ · 2016Article
- Highly Thermostable Xylanase Production from A Thermophilic Geobacillus sp. Strain WSUCF1 Utilizing Lignocellulosic Biomass.Frontiers in bioengineering and biotechnology · 2015Article
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundComplete enzymatic hydrolysis of xylan to xylose requires the action of endoxylanase and β-xylosidase. β-xylosidases play an important part in hydrolyzing xylo-oligosaccharides to xylose. Thermostable β-xylosidases have been a focus of attention as industrially important enzymes due to their long shelf life and role in the relief of end-product inhibition of xylanases caused by xylo-oligosaccharides. Therefore, a highly thermostable β-xylosidase with high specific activity has significant potential in lignocellulose bioconversion.
resultsA gene encoding a highly thermostable GH39 β-xylosidase was cloned from Geobacillus sp. strain WSUCF1 and expressed in Escherichia coli. Recombinant β-xylosidase was active over a wide range of temperatures and pH with optimum temperature of 70 °C and pH 6.5. It exhibited very high thermostability, retaining 50% activity at 70 °C after 9 days. WSUCF1 β-xylosidase is more thermostable than β-xylosidases reported from other thermophiles (growth temperature ≤ 70 °C). Specific activity was 133 U/mg when incubated with p-nitrophenyl xylopyranoside, with Km and Vmax values of 2.38 mM and 147 U/mg, respectively. SDS-PAGE analysis indicated that the recombinant enzyme had a mass of 58 kDa, but omitting heating prior to electrophoresis increased the apparent mass to 230 kDa, suggesting the enzyme exists as a tetramer. Enzyme exhibited high tolerance to xylose, retained approximately 70% of relative activity at 210 mM xylose concentration. Thin layer chromatography showed that the enzyme had potential to convert xylo-oligomers (xylobiose, triose, tetraose, and pentaose) into fermentable xylose. WSUCF1 β-xylosidase along with WSUCF1 endo-xylanase synergistically converted the xylan into fermentable xylose with more than 90% conversion.
conclusionsProperties of the WSUCF1 β-xylosidase i.e. high tolerance to elevated temperatures, high specific activity, conversion of xylo-oligomers to xylose, and resistance to inhibition from xylose, make this enzyme potentially suitable for various biotechnological applications.
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