Purification and characterization of a cephalosporin esterase from Rhodosporidium toruloides.

@article{Politino1997PurificationAC,
  title={Purification and characterization of a cephalosporin esterase from Rhodosporidium toruloides.},
  author={Michael Politino and S M Tonzi and William V. Burnett and Guna Romancik and John J. Usher},
  journal={Applied and environmental microbiology},
  year={1997},
  volume={63 12},
  pages={
          4807-11
        }
}
A novel cephalosporin esterase (EC 3.1.1.41) from Rhodosporidium toruloides was purified to gel electrophoretic homogeneity. The enzyme is a glycoprotein with a molecular mass of 80 kDa. Upon deglycosylation, several forms of the enzyme were observed with a molecular mass range between 60 and 66 kDa. The isoelectric point of the enzyme is approximately 5.6, with the pH optimum for activity occurring at 6.0. The optimal activity of the enzyme occurred at 25 degrees C, with the enzyme rapidly… CONTINUE READING

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