The Langmuir model fitted well the adsorption isotherms of lipase on the hydrophobic resin. The model parameters, Qm and kd, were affected by NaCl concentration: Qm increased from 31 to 80 U g-1 resin, and kd changed from 9.4 to 3 U ml-1. Column modelling and the simulation data were compared with the experimental data with good agreement. The highest achieved column efficiency was 71%. Notations: C: lipase concentration in solution (U ml-1); C*: lipase concentration in solution at equilibrium (U ml-1); Co: lipase concentration in the feed (U ml-1); d: resin particle diameter (cm); D: enzyme molecular diffusivity (cm2 min-1); E: axial dispersion coefficient (cm2 min-1); K: global mass transfer coefficient (cm2 min-1); kd: kinetic constant (U ml-1); k1: adsorption kinetic constant (ml U-1 min-1); k2: desorption kinetic constant (min-1); L: bed height (cm); Q: amount of adsorbed lipase in the resin (U ml-1 resin); Q*: amount of adsorbed lipase in the resin at equilibrium (U ml-1 resin); Qm: maximum adsorption capacity of the resin (U ml-1 resin); R: column radius (cm); Rs: rate of lipase adsorption (U ml-1 resin min-1); υ: superficial velocity (cm min-1); t: time; Z: column length (cm); ε: bed porosity. Subscript: i: time, j: position.2310781786Baillargeon, M.W., McCarthy, S.G., Geotrichum candidum NRRL Y-533 lipase: Purification, characterization and fatty acid specificity (1991) Lipids, 26, pp. 831-836Balcão, V.M., Vieira, M.C., Maleata, F.X., Adsorption of protein from several commercial lipase preparations onto hollow-fiber membrane module (1986) Biotechnol. Progr., 12, pp. 164-172Chase, H.A., Prediction of the performance of preparative affinity chromatography (1984) J. Chromatogr., 297, pp. 179-202Diogo, M.M., Silva, S., Cabral, J.M.S., Queiroz, J., A hydrophobic interaction on chromatography of Chromobacterium viscosum lipase on polypropylene glycol immobilised on Sepharose (1999) J. Chromatogr., 849, pp. 413-419Gitlesen, T., Bauer, M., Adlercreutz, P., Adsorption of lipase on polypropylene powder (1997) Biochim. Biophys. Acta, 1345, pp. 188-196Gustavsson, P.-E., Axelsson, A., Larsson, P.-O., Superporous agarose on bead as hydrophobic interaction chromatography support (1999) J. Chromatogr., 830, pp. 275-284Jacobsen, T., Olsen, J., Allerman, K., Substrate specifities of Geotrichum candidum lipase preparations (1990) Biotechnol. Lett., 12, pp. 121-126Kamimura, E.S., Mendieta, O., Sato, H.H., Pastore, G.M., Maugeri, F., Production of lipase from Geotrichum sp. and adsorption studies on affinity resin (1999) Brazilian J. Chem. Eng., 16, pp. 102-112Macêdo, G.A., Park, Y.K., Pastore, G.M., Partial purification and characterization of an extracellular lipase from a newly isolated strain of Geotrichum sp. (1997) Rev. Microbiol., 28, pp. 90-95Noriega, J., Tejada, A., Magaña, I., Ortega, J., Guzman, R., Modelling column regeneration effects on dye-ligand affinity chromatography (1997) Biotechnol. Prog., 13, pp. 296-300Phillips, A., Pretorious, H.J., Purification and characterization of an extracellular lipase of Galactomyces and Geotrichum (1991) Biotechnol. Lett., 13, pp. 833-838Porath, J., Salt promoted adsorption: Recent developments (1986) J. Chromatogr., 376, pp. 331-341Warwel, S., Borgdorf, R., Substrate selectivity of lipases in the esterification of cis-trans-isomers and positional isomers of conjugated linoleic acid (CLA) (2000) Biotechnol. Lett., 22, pp. 1151-1155