Characterization of a novel endo-levanase and its gene from Bacillus sp. L7.
A novel endo-levanase producing bacterium belonging to the Bacillus family has been isolated from soil. The enzyme was characterized and found to have no exo-beta-fructofuranosidase activity. The endo-levanase gene was cloned and sequenced. Homology searches have shown that the C-terminal domain of the enzyme is homologous to a number of known beta-fructofuranosidases, including exo-levanase from Bacillus subtilis and yeast invertases. The N-terminal region of the endo-levanase which is homologous to the C-terminal sequence of the B. subtilis levanase appears to be a levan-binding domain.
Miasnikov
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Cultor Ltd. Technology center, Kantvik, Finland. Andrei.Miasnikov@cultor.fi
D001412:Bacillus subtilis / Q000201:enzymology* / Q000235:genetics*; D001426:Bacterial Proteins; D003001:Cloning, Molecular; D004269:DNA, Bacterial / Q000032:analysis; D006026:Glycoside Hydrolases / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D008969:Molecular Sequence Data; D017422:Sequence Analysis, DNA; D013379:Substrate Specificity; D013696:Temperature; D043324:beta-Fructofuranosidase
D001426:Bacterial Proteins; D004269:DNA, Bacterial; D006026:Glycoside Hydrolases; D043324:beta-Fructofuranosidase; C021512:levanase