Purification and characterization of thermostable aspartase from Bacillus sp. YM55-1.

@article{Kawata1999PurificationAC,
  title={Purification and characterization of thermostable aspartase from Bacillus sp. YM55-1.},
  author={Yasushi Kawata and Kunio Tamura and Shigekazu Yano and Tomohiro Mizobata and Junya Nagai and Nobuyoshi Esaki and Kenji Soda and Masanobu Tokushige and Noboru Yumoto},
  journal={Archives of biochemistry and biophysics},
  year={1999},
  volume={366 1},
  pages={40-6}
}
A thermostable aspartase was purified from a thermophile Bacillus sp. YM55-1 and characterized in terms of activity and stability. The enzyme was isolated by a 5-min heat treatment at 75 degrees C in the presence of 11% (w/v) ammonium sulfate and 100 mM aspartate, followed by Q-Sepharose anion-exchange and AF-Red Toyopearl chromatographies. The native molecular weight of aspartase determined by gel filtration was about 200,000, and this enzyme was composed of four identical monomers with… CONTINUE READING
7 Citations
0 References
Similar Papers