Purification and characterization of a catechol 1,2-dioxygenase from a phenol degrading Candida albicans TL3

@article{Tsai2006PurificationAC,
  title={Purification and characterization of a catechol 1,2-dioxygenase from a phenol degrading Candida albicans TL3},
  author={San-Chin Tsai and Yaw-Kuen Li},
  journal={Archives of Microbiology},
  year={2006},
  volume={187},
  pages={199-206}
}
A eukaryotic catechol 1,2-dioxygenase (1,2-CTD) was produced from a Candida albicans TL3 that possesses high tolerance for phenol and strong phenol degrading activity. The 1,2-CTD was purified via ammonium sulfate precipitation, Sephadex G-75 gel filtration, and HiTrap Q Sepharose column chromatography. The enzyme was purified to homogeneity and found to be a homodimer with a subunit molecular weight of 32,000. Each subunit contained one iron. The optimal temperature and pH were 25°C and 8.0… CONTINUE READING

References

Publications referenced by this paper.
Showing 1-10 of 48 references

A rapid and sensitive methods for the quantitation of microgram quantities of protein utilizing the principle for protein–dye binding

  • MM Bradford
  • Anal Biochem
  • 1976
Highly Influential
4 Excerpts

Puri W cation and properties of catechol 1 , 2 - dioxygenase ( pyrocatechase ) from Pseudomonas putida mt2 in comparison with that from Pseudomonas arvilla C - 1

  • C Nakai, K Horiike, S Kuramitsu, H Kagamiyama, M Nozaki
  • Arch Biochem Biophys
  • 1990
Highly Influential
5 Excerpts

Two catechol 1,2-dioxygenase from aniline-assimilating bacterium, Frateuria species ANA-18

  • K Aoki, T Konohana, R Shinke
  • Agric Biol Chem
  • 1984
Highly Influential
7 Excerpts

Similar Papers

Loading similar papers…