The aim of this study was to purify, characterize, and evaluate the potential of the immobilized extracellular lipase from Aureobasidium pullulans NAC8 (ApL) for the biodegradation of oil-contaminated wastewater. ApL was purified using aqueous two-phase partitioning (ATPS) and its biochemical properties determined. The enzyme was then covalently immobilized and characterized through Fourier transform infrared (FTIR) spectroscopy and scanning electron microscopy (SEM). The performance of immobilized ApL in oil-contaminated wastewater was tested for its ability to remove chemical oxygen demand (COD), hydrolyze lipids, and produce free fatty acids. The purification fold and yield of ApL were 3.5 and 66 %, respectively. The purified enzyme had a subunit molecular weight of 30 kDa, with an optimum pH of 6.5 and an optimum temperature of 50 °C. The enzyme's catalytic efficiency for pNPP and pNPB was 1.53 × 10