Open AccessBiochemical characterization of the surface‐associated lipase of Staphylococcus saprophyticus
Author(s) -
Sakinç Türkân,
Kleine Britta,
Gatermann Sören G.
Publication year - 2007
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2007.00857.x
Subject(s) - staphylococcus saprophyticus , lipase , staphylococcus epidermidis , staphylococcus aureus , staphylococcus xylosus , triacylglycerol lipase , staphylococcus , microbiology and biotechnology , biochemistry , chemistry , bacteria , enzyme , biology , genetics
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°C. It was also observed that the enzymatic activity of Ssp depends strongly on the acyl chain length of the substrate molecule.