Lipases are the enzymes with the broadest use in biocatalysis. They have been recognized as useful biocatalysts because of their versatility in industrial applications, their stability, low cost and non-requirement for added cofactors. The actinomycetes are relatively poorly studied for lipase production. There are few reports of actinomycetes producing thermostable lipases. The primary screening for lipase production was carried out using rhodamine B agar plate technique. Of the 18 strains, five strains produced significantly higher extracellular lipolytic activities when cultivated in basal medium supplemented with 1% (v/v) olive oil. The extracellular lipases were found to be thermostable with temperature optima in the range 50-60°C. The lipases from Amycolatopsis sulphurea DSM46092 and Streptomyces rochei DSM40231 showed optimum temperature of 50°C, whereas lipases from A. rubida DSM44637, S. griseus subsp. griseus DSM40236 and A. mediterranei DSM43304 were optimally active at 60°C. The lipases showed pH optima ranging from 4.0-8.0. The lipases from A. rubida DSM44637 and S. griseus subsp. griseus DSM40236 showed maximum activity at acidic pH of 4.0, whereas lipases from A. sulphurea DSM46092 and S. rochei DSM40231 were found to be most active at neutral pH of 7.0. The lipase from A. mediterranei DSM43304 was found to be active over a broad pH range of 5.0-9.0 and was most active at pH 8.0. The crude lipase preparations showed stability in a broad range of organic solvents at 25% (v/v) concentration. The present investigation identified lipolytic actinomycetes producing highly thermostable extracellular lipases showing properties suitable for potential applications in organic synthesis.