Characterization of thermostable α-glucosidase from Clostridium thermohydrosulfuricum 39E

@article{Saha2004CharacterizationOT,
  title={Characterization of thermostable α-glucosidase from Clostridium thermohydrosulfuricum 39E},
  author={Badal C Saha and J. Gregory Zeikus},
  journal={Applied Microbiology and Biotechnology},
  year={2004},
  volume={35},
  pages={568-571}
}
Clostridium thermohydrosulfuricum 39E produced a cell-bound α-glucosidase. It was partially purified 140-fold by solubilizing with Triton X-100, ammonium sulfate treatment, DEAE-Sepharose CL-6B, octyl-Sepharose and acarbose-Sepharose affinity chromatography. The optimum temperature for the action of the enzyme was at 75°C. It had a half-life of 35 min at 75°C, 110 min at 70°C and 46 h at 60°C. The enzyme was stable at pH 5.0–6.0 and had an optimum pH at 5.0–5.5. It hydrolyzed the α-1,4-linkages… CONTINUE READING

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