Biochemical confirmation and characterization of the family-57-like alpha-amylase of Methanococcus jannaschii.

@article{Kim2001BiochemicalCA,
  title={Biochemical confirmation and characterization of the family-57-like alpha-amylase of Methanococcus jannaschii.},
  author={J W Kim and Lawrence O. Flowers and Marvin Whiteley and Tonya L Peeples},
  journal={Folia microbiologica},
  year={2001},
  volume={46 6},
  pages={467-73}
}
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… CONTINUE READING