Catalyzes the hydrolysis of fatty acid esters with a preference for mid-length acyl chain (C10-C16). Is able to hydrolyze the triacylglycerol triolein and mixed triacylglycerols from a wide range of natural oils; better activity is obtained with corn-, wheat germ- and olive oil that have higher content of linoleic and/or oleic acid (C18:2; C18:1, cis). Tween detergents are also substrates for this enzyme. Displays arylesterase activity towards p-nitrophenyl alkanoate esters and alpha- and beta-naphthyl esters. a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H(+) Strongly inhibited by Ag(+). The cations Ca(2+), Mg(2+), Co(2+) and Cu(2+) do not significantly reduce the lipolytic activity of SCO1725. Is also inhibited by DTT in vitro, but not by EDTA or by the reagent masking SH-groups, p-hydroxymercuribenzoate (pHMB). Is resistant to PMSF inhibition, except in the presence of Ca(2+). Is also strongly inhibited by 3,4-dichloroisocoumarin (DCI), another inhibitor of serine hydrolases. Addition of tetrahydrofuran and 1,4-dioxane significantly increases (2- and 4- fold, respectively) hydrolytic activity of lipase towards p-nitrophenyl caprylate. Optimum pH is 8.5. Shows high stability over a broad range of pH 4-9.5 (80-100% of enzyme activity). Becomes unstable at pH over 10, where the activity drops to 34% at pH 10.5 and to 8% at pH 11. Optimum temperature is 20-30 degrees Celsius (DOI=10.1016/j.enzmictec.2008.01.009). The His-tagged protein shows a higher optimum temperature of 55 degrees Celsius, and a thermal denaturation midpoint (Tm) of 66.63 degrees Celsius (PubMed:19041687). Is stable when incubated for 30 minutes at temperatures in the range of 30-70 degrees Celsius at pH 7 (DOI=10.1016/j.enzmictec.2008.01.009). Monomer. Belongs to the 'GDSL' lipolytic enzyme family.