Send to

Choose Destination
See comment in PubMed Commons below
FEMS Microbiol Lett. 2007 Sep;274(2):335-41. Epub 2007 Jul 20.

Biochemical characterization of the surface-associated lipase of Staphylococcus saprophyticus.

Author information

Institut für Hygiene und Mikrobiologie, Abteilung für Medizinische Mikrobiologie, Ruhr-Universität Bochum, Bochum, Germany.


Staphylococcus saprophyticus, an important cause of urinary tract infections, produces a surface-associated lipase, Ssp. In contrast to other lipases, Ssp is a protein that is present in high amounts on the surface of the bacteria and it was shown that it is a true lipase. Characterization of S. saprophyticus lipase (Ssp) showed that it is more similar to Staphylococcus aureus lipase and Staphylococcus epidermidis lipase than to Staphylococcus hyicus lipase and Staphylococcus simulans lipase. Ssp showed an optimum of lipolytic activity at pH 6 and lost its activity at pH>8 or pH<5. The present results show that Ssp activity is dependent on Ca(2+). Consequently, activity increased c. 10-fold in the presence of 2 mM Ca(2+). Optimal activity was reached at 30 degrees C. It was also observed that the enzymatic activity of Ssp depends strongly on the acyl chain length of the substrate molecule.

[Indexed for MEDLINE]
Free full text
PubMed Commons home

PubMed Commons

How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Silverchair Information Systems Icon for Wiley
    Loading ...
    Support Center