Biochemical Confirmation and Characterization of the Family-57-Like α-Amylase of Methanococcus jannaschii

J. W. Kim, L. O. Flowers, M. Whiteley, T. L. Peeples

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31 Scopus citations

Abstract

The gene encoding a family-57-like α-amylase in the hyperthermophilic archaeon Methanococcus jannaschii, has been cloned into Escherichia coli. Extremely thermoactive α-amylase was confirmed in partially purified enzyme solution of the recombinant culture. This enzyme activity had a temperature optimum of 120°C and a pH optimum 5.0-8.0. The amylase activity is extremely stable against denaturants. Hydrolysis of large sugar polymers with α-1-6 and α-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°C, among the highest reported thermostabilities of natural amylases.

Original languageEnglish (US)
Pages (from-to)467-473
Number of pages7
JournalFolia Microbiologica
Volume46
Issue number6
DOIs
StatePublished - 2001

All Science Journal Classification (ASJC) codes

  • Microbiology

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