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.

• 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