Staphylococcus simulans strain secretes a non-induced lipase in the culture
medium. Staphylococcus simulans lipase (SSL), purified to homogeneity, is
a tetrameric protein (160 kDa) corresponding to the association of four lip
ase molecules. The 30 N-terminal amino acid residues were sequenced. This s
equence is identical to the one of Staphylococcus aureus PS54 lipase (SAL P
S54) and exhibits a high degree of homology with Staphylococcus aureus NCTC
8530 lipase (SAL NCTC8530), Staphylococcus hyicus lipase (SHL) and Staphylo
coccus epidermis RP62A lipase (SEL RP62A) sequences. But the cloning and se
quencing of the part of the gene encoding the mature lipase show some diffe
rences from SAL PS54 sequence, which suggest that it is a new sequence. The
lipase activity was maximal at pH 8.5 and 37 degreesC. SSL is able to hydr
olyze triacylglycerols without chain length specificity. A specific activit
y of about 1000 U/mg was measured on tributyrin or triolein as substrate at
37 OC and at pH 8.5 in the presence of 3 rum CaCl2 In contrast to other st
aphylococcal lipases previously characterized, Ce2+ is not required to expr
ess the activity of SSL. SSL was found to be stable between pH 4 and pH 9.
The enzyme is inactivated after a few minutes when incubated at 60 degreesC
. Using tripropionin as substrate, SSL does not present the interfacial act
ivation phenomenon. In contrast to many lipases, SSL is able to hydrolyze i
ts substrate in the presence of bile salts or amphiphilic proteins. (C) 200
1 Societe francaise de biochimie et biologie moleculaire / Editions scienti
fiques et medicales Elsevier SAS. All rights reserved.