The optimum temperature and pH for the enzyme activity were 45$^{circ}C$ and 10.0, respectively. The enzyme was stable in a pH range of 5 to 10, and 62% of its activity was lost on heat treatment of 60$^{circ}C$ for 20 min. The activity of the purified enzyme was inhibited by $Fe^{2+},;Zn^{2+};and;Pb^{2+}$, and slightly activated by $Mn^{2+};and;Ca^{2+}$. ${gamma}$-Chloromercuribenzoic acid, 2,4-dinitrophenol and $H_{2}O_{2}$ did not show inhibitroy effect on the lipolytic activity of the alkaline lipase but ethylenediaminetetraacetic acid inhibited the enzyem activity. This suggested that the enzyme have metal group in its active site. Sodium salts of bile acids stimulated the enzyme activity. Analysis of hydrolyzates of olive oil after the reaction revealed that Serratia liquefaciens AL-11 produced non-specific lipolytic enzyme.