Folia Microbiologica

, Volume 46, Issue 6, pp 467–473

Biochemical confirmation and characterization of the family-57-like α-amylase ofMethanococcus jannaschii

  • J. W. Kim
  • L. O. Flowers
  • M. Whiteley
  • T. L. Peeples
Papers

DOI: 10.1007/BF02817988

Cite this article as:
Kim, J.W., Flowers, L.O., Whiteley, M. et al. Folia Microbiol (2001) 46: 467. doi:10.1007/BF02817988
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Abstract

The gene encoding a family-57-like α-amylase in the hyperthermophilic archaeonMethanococcus jannaschii, has been cloned intoEscherichia 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.

Copyright information

© Folia Microbiologica 2001

Authors and Affiliations

  • J. W. Kim
    • 1
  • L. O. Flowers
    • 1
  • M. Whiteley
    • 1
  • T. L. Peeples
    • 1
  1. 1.Department of Chemical and Biochemical EngineeringThe University of IowaIowa CityUSA
  2. 2.Department of Biological and Agricultural EngineeringThe University of ArkansasFayettevilleUSA

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