Extracellular alpha-amylase from Thermus filiformis Ork A2: purification and biochemical characterization.

@article{Egas1998ExtracellularAF,
  title={Extracellular alpha-amylase from Thermus filiformis Ork A2: purification and biochemical characterization.},
  author={M. C. V. Egas and Milton S. da Costa and Donald Arthur Cowan and Euclides Manuel Vieira Pires},
  journal={Extremophiles : life under extreme conditions},
  year={1998},
  volume={2 1},
  pages={
          23-32
        }
}
An extracellular alpha-amylase produced by the thermophilic bacterium Thermus filiformis Ork A2 was purified from cell-free culture supernatant by ion exchange chromatography. The molecular mass was estimated to be 60,000 Da by sodium dodecyl sulfate polyacrylamide gel electrophoresis. The enzyme was rich in both basic and hydrophobic amino acids, presenting the following NH2-terminal amino acid sequence: Thr-Ala-Asp-Leu-Ile-Val-Lys-Ile-Asn-Phe. Amylolytic activity on soluble starch was optimal… CONTINUE READING

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