AbstractFLL1 gene encodes an endogenous oil palm lipase that influence the innate quality of palm oil. While the genetic information is well-documented, FLL1 characteristics at the protein level remained unexplored. Therefore, this study aims to express and characterize recombinant protein FLL1 to understand its physical and chemical properties. FLL1 was efficiently expressed in Rosetta_ (DE3) pLysS competent cells using pFLL1-pGEX6P2 at 37 _C with 0.4 mM IPTG at A660 0.9. A purification method for producing high-purity FLL1 protein was established through affinity and ion exchange chromatography, suitable for downstream characterization and application. FLL1 enzyme activity peaked at 40 _C, and demonstrated its thermal stability by retaining 50 % of its activity after four hours of incubation at a similar temperature. FLL1 functioned best at pH 7 (PBS buffer) and remained highly stable at pH 8 (PBS and Tris-HCl buffers). Low LogPo/w organic solvents, especially isopropanol, significantly enha.....