Purification and characterization of a cell wall peptidase from Lactococcus lactis subsp. cremoris IMN-C12.

@article{Sahlstrm1993PurificationAC,
  title={Purification and characterization of a cell wall peptidase from Lactococcus lactis subsp. cremoris IMN-C12.},
  author={S Sahlstr\om and J{\'o}zefa Chrzanowska and Terje S\orhaug},
  journal={Applied and environmental microbiology},
  year={1993},
  volume={59 9},
  pages={
          3076-82
        }
}
A peptidase from the cell wall fraction of Lactococcus lactis subsp. cremoris IMN-C12 has been purified to homogeneity by hydrophobic interaction chromatography, two steps of anion-exchange chromatography, and gel filtration. The molecular mass of the purified enzyme was estimated to be 72 kDa by gel filtration and 23 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The enzyme has a pI of 4.0, and it has the following N-terminal sequence from the 2nd to the 17th amino acid… CONTINUE READING