The lipase from Chromobacterium was adsorbed on glass beads which was coated with olive oil, liquid paraffin or silicone oil. These adsorption was treated in the Lineweaver-Burk's plot and characters of the adsorption were similar each other regardless of their chemical structure of hydrophobic materials. On the other hand, esterase from porcine liver was not adsorbed on hydrophobic glass beads. The interaction between the lipase and hydrophobic surface conformed to the Langmuir's adsorption isotherm with a dissociation constant K=1.4×10^-7M. At saturation of the surface with the lipase each protein molecule occupies an average area of 4500 A² per molecule. The lipase adsorbed on hydrophobic surface did not inactivated but activated about 3-fold. It was elucidated that the hydrophobic bond play a major role in the adsorption of the lipase on substrate or hydrophobic surface.