Catalyzes the hydrolysis of p-nitrophenyl esters, alpha- and beta-naphthyl esters, and triacylglycerols, with a preference for medium acyl chain length (C8-C12). Shows a much higher hydrolysis rate of glycerol esters of unsaturated C16 and C18 fatty acids than that of their saturated counterparts, and a preference for cis double bond. Is also able to hydrolyze several natural oils and Tween detergents. Also displays thioesterase and phospholipase activities, towards palmitoyl-coenzyme A and diheptanoyl glycerophosphocholine, respectively. Shows transesterification activity of racemic 1-phenyl ethanol with vinyl acetate in hexane, proceeding with partial (R)-enantioselectivity. a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H(+) H2O + hexadecanoyl-CoA = CoA + H(+) + hexadecanoate Inhibited by 3,4-dichloroisocoumarin and tetrahydrolipstatin in the absence of substrate, but by phenylmethylsulfonyl fluoride (PMSF) only in the presence of substrate. Several water-miscible solvents enhance the lipase hydrolytic activity in vitro. Tetrahydrofuran and N,N-dimethylformamide (both 50%) inactivate the enzyme with t1/2 of 5 minutes and t1/2 of 2 hours, respectively. Optimum pH is 9.5. Optimum temperature is 55 degrees Celsius at pH 8.0. Monomer. Expressed once the cells enter stationary phase, with a maximum at the late stationary phase. Value for wild-type lipase. Value for lipase overexpressed in S.rimosus. Belongs to the 'GDSL' lipolytic enzyme family. In PubMed:17137716 the protein has been overexpressed in S.lividans, where it is incorrectly processed and has 2 additional N-terminal amino acids.