A simple, rapid, and economic method of enzyme immobilization was developed for phospholipase LecitaseA (R) ultra (LU) via interfacial adsorption. The effect of nature of the polystyrene supports and the kinetic behavior and stability of immobilized lecitaseA (R) ultra (IM-LU) were evaluated. Six macroporous resins (AB-8, X-5, DA-201, NKA-9, D101, D4006) and two anion resins (D318 and D201) were studied as the supports. DA-201 resin was selected because of its best immobilization effect for LU. Immobilization conditions were investigated, including immobilization time, pH, and enzyme concentration. IM-LU with a lipase activity of 1,652.4 A +/- 8.6 U/g was obtained. The adsorption process was modeled by Langmuir and Freundlich equations, and the experimental data were better fit for the former one. The kinetic constant (K (m)) values were found to be 192.7 A +/- 2.2 mM for the free LU and 249.3 A +/- 5.4 mM for the IM-LU, respectively. The V (max) value of free LU (169.5 A +/- 4.3 mM/min) was higher than that of the IM-LU (53.8 A +/- 1.5 mM/min). Combined strategies of scanning electron micrograph, thermogravimetric analysis, and Fourier transform infrared (FTIR) spectroscopy were employed to characterize the IM-LU. FTIR spectroscopy showed that the secondary conformation of the enzyme had changed after immobilization, through which a decrease of alpha-helix content and an increase of beta-sheet content were observed. The IM-LU possessed an improved thermal stability as well as metal ionic tolerance when compared with its free form. The reusability of IM-LU was also evaluated through catalyzing esterification reaction between oleic acid and glycerol. It exhibited approximately 70 % of relative esterification efficiency after six successive cycles. This immobilized enzyme on hydrophobic support may well be used for the synthesis of structural lipids in lipid area.