Purification and characterization of cis-aconitic acid decarboxylase from Aspergillus terreus TN484-M1.

@article{Dwiarti2002PurificationAC,
  title={Purification and characterization of cis-aconitic acid decarboxylase from Aspergillus terreus TN484-M1.},
  author={Lies Dwiarti and Ken Yamane and Hitoshi Yamatani and Prihardi Kahar and Mitsuyasu Okabe},
  journal={Journal of bioscience and bioengineering},
  year={2002},
  volume={94 1},
  pages={
          29-33
        }
}
cis-Aconitic acid decarboxylase (CAD) was assumed to be a key enzyme in the production of itaconic acid by comparing the activity of CAD from Aspergillus terreus TN484-M1 with that of CAD from the low-itaconate yielding strain Aspergillus terreus CM85J. The constitutive CAD was purified to homogeneity from A. terreus TN484-M1 by ammonium sulfate fractionation, and column chromatography on DEAE-toyopearl, Butyl-toyopearl, and Sephacryl S200HR, and then characterized. A molecular mass of 55 kDa… CONTINUE READING

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