In today’s bio-based industry, lipase-catalyzed processes hold eminent commercial worth, yet their use is restricted owing to low yields, high production cost, inconsistent reproducibility, and poor performance in native form. Cloning and expression of multiple lipase genes in various systems have been investigated in order to produce enzymes for the food and detergent industries more cheaply since the development of recombinant DNA technology. The identification of novel lipases is still hampered by the rather difficult expression of these enzymes. The expression of lipases still requires a case-to case optimization. However, the unbiased choice of the appropriate promoter system and host for a specific protein of interest remains difficult. Here, we concisely expressed TLIP (Lipase from Thermomyces lanuginosus; mainly used in the detergent industry) in the frequently used conventional and alternative host systems, with their unique features, along with different promoters (T5, T7, aprE and hp4d) to produce recombinant products. Screening of expression was done among both prokaryotic ( Escherichia coli, Bacillus subtilis) and eukaryotic ( Yarrowia lipolytica) hosts consisting of both intracellular and secretory expression. E. coli (BL21 Shuffle) and Y. lipolytica (extracellular) were found to be the best expression systems for lipase production.