ArticleApplied and environmental microbiology1999
A cold-active glucanase from the ruminal bacterium Fibrobacter succinogenes S85.
Article in Applied and environmental microbiology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed.
- Antarctic tundra soil metagenome as useful natural resources of cold-active lignocelluolytic enzymes.Journal of microbiology (Seoul, Korea) · 2019Article
- Characterization of Cryptopygus antarcticus endo-β-1,4-glucanase from Bombyx mori expression systems.Molecular biotechnology · 2014Article
- Isolation and characterization of cellulolytic bacteria from the Stain house Lake, Antarctica.Folia microbiologica · 2014Article
- Partial Characterization of α-Galactosidic Activity from the Antarctic Bacterial Isolate, Paenibacillus sp. LX-20 as a Potential Feed Enzyme Source.Asian-Australasian journal of animal sciences · 2012Article
- Effect of environmental factors and influence of rumen and hindgut biogeography on bacterial communities in steers.Applied and environmental microbiology · 2011Article
- 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
- Flavobacterium sp. strain 4221 and Pedobacter sp. strain 4236 beta-1,3-glucanases that are active at low temperatures.Applied and environmental microbiology · 2008Article
- Cold-active winter rye glucanases with ice-binding capacity.Plant physiology · 2006Article
- Characterization and gene cloning of a cold-active cellulase from a deep-sea psychrotrophic bacterium Pseudoalteromonas sp. DY3.Extremophiles : life under extreme conditions · 2006Article
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2 authors.
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Abstract
We previously characterized two endoglucanases, CelG and EGD, from the mesophilic ruminal anaerobe Fibrobacter succinogenes S85. Further comparative experiments have shown that CelG is a cold-active enzyme whose catalytic properties are superior to those of several other intensively studied cold-active enzymes. It has a lower temperature optimum, of 25 degrees C, and retains about 70% of its maximum activity at 0 degrees C, while EGD has a temperature optimum of 35 degrees C and retains only about 18% of its maximal activity at 0 degrees C. When assayed at 4 degrees C, CelG exhibits a 33-fold-higher kcat value and a 73-fold-higher physiological efficiency (kcat/Km) than EGD. CelG has a low thermal stability, as indicated by the effect of temperature on its activity and secondary structure. The presence of small amino acids around the putative catalytic residues may add to the flexibility of the enzyme, thereby increasing its activity at cold temperatures. Its activity is modulated by sodium chloride, with an increase of over 1.8-fold at an ionic strength of 0.03. Possible explanations for the presence of a cold-active enzyme in a mesophile are that cold-active enzymes are more broadly distributed than previously expected, that lateral transfer of the gene from a psychrophile occurred, or that F. succinogenes originated from the marine environment.
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