Purification and partial characterization of a tripeptidase from Pediococcus pentosaceus K9.2.

@article{Simitsopoulou1997PurificationAP,
  title={Purification and partial characterization of a tripeptidase from Pediococcus pentosaceus K9.2.},
  author={Maria Simitsopoulou and A Vafopoulou and Theodora Choli-Papadopoulou and Efstathios Alichanidis},
  journal={Applied and environmental microbiology},
  year={1997},
  volume={63 12},
  pages={4872-6}
}
A tripeptidase was purified from the cytoplasm of Pediococcus pentosaceus K9.2 by anion-exchange chromatography, gel filtration chromatography, and high-performance liquid chromatography. The molecular mass of the enzyme was estimated by gel filtration at 100,000 Da. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the purified peptidase showed one protein band of 45,000 Da. Optimal enzyme activity was obtained at pH 7.0 and at 50 degrees C. The peptidase hydrolyzed all tripeptides… CONTINUE READING