Structural and functional characterization of recombinant medaka fish alpha-amylase expressed in yeast Pichia pastoris.

@article{Mizutani2012StructuralAF,
  title={Structural and functional characterization of recombinant medaka fish alpha-amylase expressed in yeast Pichia pastoris.},
  author={Kimihiko Mizutani and Mayuko Toyoda and Yuichiro Otake and Soshi Yoshioka and Nobuyuki Takahashi and Bunzo Mikami},
  journal={Biochimica et biophysica acta},
  year={2012},
  volume={1824 8},
  pages={954-62}
}
The medaka fish α-amylase was expressed and purified. The expression systems were constructed using methylotrophic yeast Pichia pastoris, and the recombinant proteins were secreted into the culture medium. Purified recombinant α-amylase exhibited starch hydrolysis activity. The optimal pH, denaturation temperature, and K(M) and V(max) values were determined; chloride ions were essential for enzyme activity. The purified protein was also crystallized and examined by X-ray crystallography. The… CONTINUE READING

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