Novel, thermostable family-13-like glycoside hydrolase from Methanococcus jannaschii
Language English Country United States Media print
Document type Comparative Study, Journal Article, Research Support, Non-U.S. Gov't, Research Support, U.S. Gov't, Non-P.H.S.
PubMed
11898335
DOI
10.1007/bf02817989
Knihovny.cz E-resources
- MeSH
- Escherichia coli metabolism MeSH
- Glucans chemistry MeSH
- Glycoside Hydrolases chemistry genetics metabolism MeSH
- Cloning, Molecular MeSH
- Hydrogen-Ion Concentration MeSH
- Methanococcus enzymology genetics MeSH
- Molecular Sequence Data MeSH
- Molecular Weight MeSH
- Polysaccharides chemistry MeSH
- Amino Acid Sequence MeSH
- Sequence Alignment MeSH
- Enzyme Stability MeSH
- Temperature MeSH
- Calcium pharmacology MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Research Support, U.S. Gov't, Non-P.H.S. MeSH
- Comparative Study MeSH
- Names of Substances
- Glucans MeSH
- Glycoside Hydrolases MeSH
- Polysaccharides MeSH
- Calcium MeSH
A novel glycoside hydrolase from the hyperthermophilic archaeon Methanococcus jannaschii has been cloned into Escherichia coli. Extremely thermoactive and thermostable amylolytic activity was confirmed in partially purified enzyme solution. This enzyme exhibited a temperature optimum of 100 degrees C and a pH optimum pH 5.0-8.0. Hydrolysis of large 1,6-alpha- and 1,4-alpha-linked polysaccharides yielded glucose polymers of 1-7 units. Incubation with amylose displayed the highest activity. The catalyst was activated and stabilized by Ca2+ and exhibited extreme thermostability at 100 degrees C with a half-life of 78 h.
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