Open AccessSesquiterpene farnesol as a competitive inhibitor of lipase activity of Staphylococcus aureus
Author(s) -
Kuroda Makoto,
Nagasaki Sanae,
Ito Ryuta,
Ohta Toshiko
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.1574-6968.2007.00772.x
Subject(s) - farnesol , lipase , staphylococcus aureus , chemistry , triacylglycerol lipase , biochemistry , substrate (aquarium) , microbiology and biotechnology , enzyme , biology , bacteria , ecology , genetics
Abstract Staphylococcus aureus lipase (SAL) is known to possess broad substrate specificity for triacylglycerides. We found that a sub‐minimum inhibitory concentration of farnesol (1000 mg L −1 ) inhibits this lipase activity on a Mueller–Hinton agar containing 1% Tween substrates. A quantitative lipase assay using p‐ nitrophenyl palmitate ( p NPP) revealed that the inhibitory action of farnesol appears to be the result of the inhibition of lipase activity rather than of its secretion into the culture medium. The inhibition was observed in all the tested 8 methicillin‐susceptible S. aureus and 31 methicillin‐resistant S. aureus clinical isolates. Using homogeneous lipase purified by hydrophobic interaction chromatography, it was revealed that farnesol could competitively inhibit the lipase activity against the substrate p NPP.