Biochemical confirmation and characterization of the family-57-like alpha-amylase of 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
11898334
DOI
10.1007/bf02817988
Knihovny.cz E-resources
- MeSH
- alpha-Amylases biosynthesis genetics metabolism MeSH
- Amylose metabolism MeSH
- Escherichia coli metabolism MeSH
- Glucans metabolism MeSH
- Cloning, Molecular MeSH
- Hydrogen-Ion Concentration MeSH
- Carbohydrate Metabolism MeSH
- Methanococcus enzymology genetics MeSH
- Molecular Sequence Data MeSH
- Recombinant Proteins metabolism MeSH
- Amino Acid Sequence MeSH
- Sequence Alignment MeSH
- Temperature 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
- alpha-Amylases MeSH
- Amylose MeSH
- Glucans MeSH
- Recombinant Proteins MeSH
The gene encoding a family-57-like alpha-amylase in the hyperthermophilic archaeon Methanococcus jannaschii, has been cloned into Escherichia coli. Extremely thermoactive alpha-amylase was confirmed in partially purified enzyme solution of the recombinant culture. This enzyme activity had a temperature optimum of 120 degrees C and a pH optimum 5.0-8.0. The amylase activity is extremely stable against denaturants. Hydrolysis of large sugar polymers with alpha-1-6 and alpha-1-4 linkages yields products including glucose polymers of 1-7 units. Highest activity is exhibited on amylose. The catalyst exhibited a half-life of 50 h at 100 degrees C, among the highest reported thermostabilities of natural amylases.
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