ArticleExtremophiles : life under extreme conditions2013
Isolation of cold-active, acidic endocellulase from Ladakh soil by functional metagenomics.
Article in Extremophiles : life under extreme conditions, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 50 citations in OpenAlex.
- Enhancing Cold Adaptation of Bidomain Amylases by High-Throughput Computational Engineering.Angewandte Chemie (International ed. in English) · 2025Article
- Identification and characterization of a novel, low-temperature-active GH8 endo-β-1,4-glucanase exhibiting broad pH stability from AntarcticFrontiers in microbiology · 2025Article
- Metagenomic exploration of cold-active enzymes for detergent applications: Characterization of a novel, cold-active and alkali-stable GH8 endoglucanase from ikaite columns in SW Greenland.Microbial biotechnology · 2024Article
- Cold-active microbial enzymes and their biotechnological applications.Microbial biotechnology · 2024Review
- Biodiversity and Bioactive Potential of Actinomycetes from Unexplored High Altitude Regions of Kargil, India.Indian journal of microbiology · 2024Article
- Novel, cold-adapted D-laminaribiose- and D-glucose-releasing GH16 endo-β-1,3-glucanase fromFrontiers in microbiology · 2024Article
- Cold-Adapted Proteases: An Efficient and Energy-Saving Biocatalyst.International journal of molecular sciences · 2023Review
- Novel, acidic, and cold-adapted glycoside hydrolase family 8 endo-β-1,4-glucanase from an Antarctic lichen-associated bacterium,Frontiers in microbiology · 2022Article
- Characterization of a GH8 β-1,4-Glucanase fromJournal of microbiology and biotechnology · 2021Article
- Microbial Ecology from the Himalayan Cryosphere Perspective.Microorganisms · 2020Review
- A Novel Cold-Adaptive Endo-1,4-β-Glucanase FromFrontiers in microbiology · 2019Article
- Structure and function of a novel GH8 endoglucanase from the bacterial cellulose synthase complex of Raoultella ornithinolytica.PloS one · 2017Article
- Article
- NaCl-, protease-tolerant and cold-active endoglucanase from Paenibacillus sp. YD236 isolated from the feces of Bos frontalis.SpringerPlus · 2016Article
- Draft Genome Sequence of the Cellulolytic Bacterium Clavibacter sp. CF11, a Strain Producing Cold-Active Cellulase.Genome announcements · 2015Article
- Synthetic biology approaches to improve biocatalyst identification in metagenomic library screening.Microbial biotechnology · 2015Review
- Structural Insight of a Trimodular Halophilic Cellulase with a Family 46 Carbohydrate-Binding Module.PloS one · 2015Article
- Improved cultivation and metagenomics as new tools for bioprospecting in cold environments.Extremophiles : life under extreme conditions · 2015Review
- Discovery of novel enzymes with industrial potential from a cold and alkaline environment by a combination of functional metagenomics and culturing.Microbial cell factories · 2014Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mining of soil sample from cold desert of Ladakh by functional metagenomics led to the isolation of cold-adapted endocellulase (CEL8M) that hydrolyses carboxymethyl cellulose (CMC). Mature CEL8M, a 347-residue polypeptide with a molecular mass of 38.9 kDa showed similarity to β-1,3-1,4 D-glucanase from Klebsiella sp. The enzyme contains the catalytic module of glycosyl hydrolase family 8 but does not possess a carbohydrate-binding domain. 3D structural model of the enzyme built by homology modeling showed an architecture of (α/α)6-barrel fold. The purified enzyme was found to be active against CMC, xylan, colloidal chitosan and lichenan but not active against avicel. Glucose was not among the initial hydrolysis products, indicating an endo mode of action. CEL8M displayed maximal activity at pH 4.5 and remained significantly active (~28 %) when the temperature decreased to 10 °C. Cold-active endocellulase CEL8M may find applications in textile industry at low temperature which can result in energy savings.
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