Folia Microbiologica

, Volume 46, Issue 6, pp 475–481

Novel, thermostable family-13-like glycoside hydrolase fromMethanococcus jannaschii

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

DOI: 10.1007/BF02817989

Cite this article as:
Kim, J.W., Terc, H.A., Flowers, L.O. et al. Folia Microbiol (2001) 46: 475. doi:10.1007/BF02817989

Abstract

A novel glycoside hydrolase from the hyperthermophilic archaeonMethanococcus jannaschii has been cloned intoEscherichia coli. Extremely thermoactive and thermostable amylolytic activity was confirmed in partially purified enzyme solution. This enzyme exhibited a temperature optimum of 100 °C and a pH optimum pH 5.0–8.0. Hydrolysis of large 1,6-α- and 1,4-α-linked polysaccharides yielded glucose polymers of 1–7 units. Incubation with amylose displayed the highest activity. The catalyst was activated and stabilized by Ca2+ and exhibited extreme thermostability at 100 °C with a half-life of 78 h.

Copyright information

© Folia Microbiologica 2001

Authors and Affiliations

  • J. W. Kim
    • 1
  • H. A. Terc
    • 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