Purification and enzymic properties of the fructosyltransferase of Streptococcus salivarius ATCC 25975.

@article{Song1999PurificationAE,
  title={Purification and enzymic properties of the fructosyltransferase of Streptococcus salivarius ATCC 25975.},
  author={D D Song and Nicholas A. Jacques},
  journal={The Biochemical journal},
  year={1999},
  volume={341 ( Pt 2)},
  pages={285-91}
}
The recombinant fructosyltransferase (Ftf) of Streptococcus salivarius was expressed in Escherichia coli and purified to electrophoretic homogeneity after a combination of adsorption, ion-exchange and gel-filtration chromatography. The N-terminal signal sequence of the Ftf was removed by E. coli at the same site as in its natural host. The purified Ftf exhibited maximum activity at pH 6.0 and 37 degrees C, was activated by Ca2+, but inhibited by the metal ions Cu2+, Zn2+, Hg2+ and Fe3+. The… CONTINUE READING

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