ArticleFrontiers in bioengineering and biotechnology2015
Functional Screening of Hydrolytic Activities Reveals an Extremely Thermostable Cellulase from a Deep-Sea Archaeon.
Article in Frontiers in bioengineering and biotechnology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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15 citing papers in PubMed, 32 citations in OpenAlex.
- A twin xanthan lyase-dependent xanthan degradation system in Paenibacillus taichungensis I5.Applied microbiology and biotechnology · 2026Article
- Cloning and Characterization of the Novel Endoglucanase Identified in Deep Subsurface Thermal Well of Biragzang (North Ossetia) by Metagenomic Analysis.Biomolecules · 2025Article
- Structural and functional insights into extreme thermal stability and activity of two GH12 domains of a multidomain glycosidase from a hyperthermophilic euryarchaeon.The FEBS journal · 2025Article
- Archaea as a Model System for Molecular Biology and Biotechnology.Biomolecules · 2023Review
- Two-step functional screen on multiple proteinaceous substrates reveals temperature-robust proteases with a broad-substrate range.Applied microbiology and biotechnology · 2021Article
- Cellulolytic thermophilic microorganisms in white biotechnology: a review.Folia microbiologica · 2020Review
- Biomass-degrading glycoside hydrolases of archaeal origin.Biotechnology for biofuels · 2020Review
- Properties and Applications of Extremozymes from Deep-Sea Extremophilic Microorganisms: A Mini Review.Marine drugs · 2019Review
- A hydrolase with esterase activity expressed from a fosmid gene bank prepared from DNA of a North West Himalayan glacier frozen soil sample.3 Biotech · 2019Article
- Novel Hyperthermophilic CrenarchaeonFrontiers in microbiology · 2019Article
- Cellulases from Thermophiles Found by Metagenomics.Microorganisms · 2018Review
- Article
- Isolation and Characterization of the First Xylanolytic Hyperthermophilic Euryarchaeon Thermococcus sp. Strain 2319x1 and Its Unusual Multidomain Glycosidase.Frontiers in microbiology · 2016Article
- Combined Whole-Cell High-Throughput Functional Screening for Identification of New Nicotinamidases/Pyrazinamidases in Metagenomic/Polygenomic Libraries.Frontiers in microbiology · 2016Article
- Discovery of new cellulases from the metagenome by a metagenomics-guided strategy.Biotechnology for biofuels · 2016Article
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Authors and funding
10 authors at 5 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Extreme habitats serve as a source of enzymes that are active under extreme conditions and are candidates for industrial applications. In this work, six large-insert mixed genomic libraries were screened for hydrolase activities in a broad temperature range (8-70°C). Among a variety of hydrolytic activities, one fosmid clone, derived from a library of pooled isolates of hyperthermophilic archaea from deep sea vents, displayed hydrolytic activity on carboxymethyl cellulose substrate plates at 70°C but not at lower temperatures. Sequence analysis of the fosmid insert revealed a gene encoding a novel glycoside hydrolase family 12 (GHF12) endo-1,4-β-glucanase, termed Cel12E. The enzyme shares 45% sequence identity with a protein from the archaeon Thermococcus sp. AM4 and displays a unique multidomain architecture. Biochemical characterization of Cel12E revealed a remarkably thermostable protein, which appears to be of archaeal origin. The enzyme displayed maximum activity at 92°C and was active on a variety of linear 1,4-β-glucans like carboxymethyl cellulose, β-glucan, lichenan, and phosphoric acid swollen cellulose. The protein is able to bind to various insoluble β-glucans. Product pattern analysis indicated that Cel12E is an endo-cleaving β-glucanase. Cel12E expands the toolbox of hyperthermostable archaeal cellulases with biotechnological potential.
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