Biochemical and molecular characterization of a lipase from an Algerian isolated Staphylococcus aureus strain.

A Staphylococcus aureus strain, isolated from an Algerian biotope, secretes a non-induced lipase in the culture medium. The S. aureus lipase (SAL) was purified to homogeneity. Pure SAL is a monomeric protein (43kDa). The 20 N-terminal amino acid residues showed a high degree of homology with other staphylococcal lipase sequences. SAL presents specific activities of about 1600 and 555 U mg(-1) using tributyrin and olive oil emulsion as substrates, respectively. In contrast to other staphylococcal lipases previously characterized, SAL was stable at a pH range from 6 to 9 after 1h incubation, and retained 50% of its activity after 10min incubation at 50 degrees C. The purified enzyme was also characterized using monolayer technique. Lipase activity can be measured only when the surface pressure exceeds 15mNm(-1). The critical surface pressure (pi(c)) measured with egg-PC films was estimated at 33 mNm(-1). SAL showed a preference for the distal ester groups of the diglyceride isomers at low surface pressure, for the adjacent ester groups at high surface pressure and a preference for the sn-3 position of the 2,3-sn-enantiomer of dicaprin. Cloned and sequenced gene part, encoding the mature lipase shows, in comparison with S. aureus lipase 3 (SAL3), a deletion of three residues (LKA) at the N-terminal extremity and a substitution of glycine 208 and isoleucine 226 with an arginine and leucine, respectively.