ArticleExtremophiles : life under extreme conditions2006
Characterization and gene cloning of a cold-active cellulase from a deep-sea psychrotrophic bacterium Pseudoalteromonas sp. DY3.
Article in Extremophiles : life under extreme conditions, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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22 citing papers in PubMed, 77 citations in OpenAlex.
- Identification and characterization of a novel, low-temperature-active GH8 endo-β-1,4-glucanase exhibiting broad pH stability from AntarcticFrontiers in microbiology · 2025Article
- Complete genome of Nakamurella sp. PAMC28650: genomic insights into its environmental adaptation and biotechnological potential.Functional & integrative genomics · 2022Article
- Exogenous production of cold-active cellulase from polar Nocardiopsis sp. with increased cellulose hydrolysis efficiency.Archives of microbiology · 2022Article
- Novel, acidic, and cold-adapted glycoside hydrolase family 8 endo-β-1,4-glucanase from an Antarctic lichen-associated bacterium,Frontiers in microbiology · 2022Article
- Biotechnological potential of psychrophilic microorganisms as the source of cold-active enzymes in food processing applications.3 Biotech · 2021Review
- The Variety and Inscrutability of Polar Environments as a Resource of Biotechnologically Relevant Molecules.Microorganisms · 2020Review
- De novo genome assembly and comparative annotation reveals metabolic versatility in cellulolytic bacteria from cropland and forest soils.Functional & integrative genomics · 2020Article
- Recent Development of Extremophilic Bacteria and Their Application in Biorefinery.Frontiers in bioengineering and biotechnology · 2020Review
- Secretion of DNases by Marine Bacteria: A Culture Based and Bioinformatics Approach.Frontiers in microbiology · 2019Article
- A Metagenomic Advance for the Cloning and Characterization of a Cellulase from Red Rice Crop Residues.Molecules (Basel, Switzerland) · 2016Article
- Screening and characterization of amylase and cellulase activities in psychrotolerant yeasts.BMC microbiology · 2016Article
- Article
- Identification and characterization of a halotolerant, cold-active marine endo-β-1,4-glucanase by using functional metagenomics of seaweed-associated microbiota.Applied and environmental microbiology · 2014Article
- Thermodynamic and functional characteristics of deep-sea enzymes revealed by pressure effects.Extremophiles : life under extreme conditions · 2013Review
- Article
- Marine metagenomics: new tools for the study and exploitation of marine microbial metabolism.Marine drugs · 2010Review
- Cellulase production from Pseudoalteromonas sp. NO3 isolated from the sea squirt Halocynthia rorentzi.Journal of industrial microbiology & biotechnology · 2009Article
- Identification of cellulase genes from the metagenomes of compost soils and functional characterization of one novel endoglucanase.Current microbiology · 2009Article
- Genomics of deep-sea and sub-seafloor microbes.Microbial biotechnology · 2009Article
- Marine metagenomics: strategies for the discovery of novel enzymes with biotechnological applications from marine environments.Microbial cell factories · 2008Article
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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
The celX gene encoding an extracellular cold-active cellulase was isolated from a psychrotrophic bacterium, which was isolated from deep-sea sediment and identified as a Pseudoalteromonas species. It encoded a protein consisting of 492 amino acids with a calculated molecular mass of 52.7 kDa. The CelX consisted of an N-terminal catalytic domain belonging to glycoside hydrolase family 5 and a C-terminal cellulose-binding domain belonging to carbohydrate-binding module family 5. The long linker sequence connecting both domains was composed of 105 residues. The optimal temperature for cellulase activity of CelX was 40 degrees C. The enzyme was most active at pH 6-7 and showed better resistance to alkaline condition. The zymogram activity analysis indicated that the CelX consisted of single enzyme component. The cellobiose was main hydrolysate of CelX.
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