Biochemical confirmation and characterization of the family-57-like alpha-amylase of Methanococcus jannaschii
Jazyk angličtina Země Spojené státy americké Médium print
Typ dokumentu srovnávací studie, časopisecké články, práce podpořená grantem, Research Support, U.S. Gov't, Non-P.H.S.
PubMed
11898334
DOI
10.1007/bf02817988
Knihovny.cz E-zdroje
- MeSH
- alfa-amylasy biosyntéza genetika metabolismus MeSH
- amylosa metabolismus MeSH
- Escherichia coli metabolismus MeSH
- glukany metabolismus MeSH
- klonování DNA MeSH
- koncentrace vodíkových iontů MeSH
- metabolismus sacharidů MeSH
- Methanococcus enzymologie genetika MeSH
- molekulární sekvence - údaje MeSH
- rekombinantní proteiny metabolismus MeSH
- sekvence aminokyselin MeSH
- sekvenční seřazení MeSH
- teplota MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Research Support, U.S. Gov't, Non-P.H.S. MeSH
- srovnávací studie MeSH
- Názvy látek
- alfa-amylasy MeSH
- amylosa MeSH
- glukany MeSH
- rekombinantní proteiny 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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