ArticleJournal of bacteriology2012
Cellulose degradation by Sulfolobus solfataricus requires a cell-anchored endo-β-1-4-glucanase.
Article in Journal of bacteriology, 2012. 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, 50 citations in OpenAlex.
- Sulfolobales: Acidothermophilic archaea as models for biology and biotechnological applications.Engineering microbiology · 2026Review
- Polysaccharide-degrading archaea dominate acidic hot springs: genomic and cultivation insights into a novelmSystems · 2025Article
- Genome-guided isolation of the hyperthermophilic aerobe Fervidibacter sacchari reveals conserved polysaccharide metabolism in the Armatimonadota.Nature communications · 2024Article
- Acidophilic heterotrophs: basic aspects and technological applications.Frontiers in microbiology · 2024Review
- Lignocellulosics in plant cell wall and their potential biological degradation.Folia microbiologica · 2022Review
- Genomic attributes of thermophilic and hyperthermophilic bacteria and archaea.World journal of microbiology & biotechnology · 2022Review
- Engineering ofJournal of microbiology and biotechnology · 2022Article
- Glycoside Hydrolases and Glycosyltransferases from Hyperthermophilic Archaea: Insights on Their Characteristics and Applications in Biotechnology.Biomolecules · 2021Review
- Evaluation of Cellulolytic Endo-1,4-β-D-Glucanase Activity in the Digestive Fluid of Adult Phytophagous BeetleTropical life sciences research · 2021Article
- The biology of thermoacidophilic archaea from the order Sulfolobales.FEMS microbiology reviews · 2021Article
- High Potential for Biomass-Degrading Enzymes Revealed by Hot Spring Metagenomics.Frontiers in microbiology · 2021Article
- Thermostable endoglucanase gene derived by amplification from the genomic DNA of a cellulose-enriched mixed culture from mudspring water of Mt. Makiling, Laguna, Philippines.World journal of microbiology & biotechnology · 2020Article
- Cellulolytic thermophilic microorganisms in white biotechnology: a review.Folia microbiologica · 2020Review
- Novel Hyperthermophilic CrenarchaeonFrontiers in microbiology · 2019Article
- Expression and characterisation of a thermophilic endo-1,4-β-glucanase from Sulfolobus shibatae of potential industrial application.Molecular biology reports · 2018Article
- Biotechnology of extremely thermophilic archaea.FEMS microbiology reviews · 2018Review
- Cellulases from Thermophiles Found by Metagenomics.Microorganisms · 2018Review
- Functional Screening of Hydrolytic Activities Reveals an Extremely Thermostable Cellulase from a Deep-Sea Archaeon.Frontiers in bioengineering and biotechnology · 2015Article
- Extremely thermophilic microorganisms as metabolic engineering platforms for production of fuels and industrial chemicals.Frontiers in microbiology · 2015Review
- Isolation of Extracellular Polymeric Substances from Biofilms of the Thermoacidophilic Archaeon Sulfolobus acidocaldarius.Frontiers in bioengineering and biotechnology · 2015Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A sequence encoding a putative extracellular endoglucanase (sso1354) was identified in the complete genome sequence of Sulfolobus solfataricus. The encoded protein shares signature motifs with members of glycoside hydrolases family 12. After an unsuccessful first attempt at cloning the full-length coding sequences in Escherichia coli, an active but unstable recombinant enzyme lacking a 27-residue N-terminal sequence was generated. This 27-amino-acid sequence shows significant similarity with corresponding regions in the sugar binding proteins AraS, GlcS, and TreS of S. solfataricus that are responsible for anchoring them to the plasma membrane. A strategy based on an effective vector/host genetic system for Sulfolobus and on expression control by the promoter of the S. solfataricus gene which encodes the glucose binding protein allowed production of the enzyme in sufficient quantities for study. In fact, the enzyme expressed in S. solfataricus was stable and highly thermoresistant and showed optimal activity at low pH and high temperature. The protein was detected mainly in the plasma membrane fraction, confirming the structural similarity to the sugar binding proteins. The results of the protein expression in the two different hosts showed that the SSO1354 enzyme is endowed with an endo-β-1-4-glucanase activity and specifically hydrolyzes cellulose. Moreover, it also shows significant but distinguishable specificity toward several other sugar polymers, such as lichenan, xylan, debranched arabinan, pachyman, and curdlan.
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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.