Abstract: Bio-functionalized chromatography—capillary electrophoresis was used in investigating the interaction between semicarbazide-sensitive amine oxidase(SSAO), its substrate benzylamine as well as its inhibitor 2-BrEA. SSAO activity detection showed that SSAO could keep 70%~85% activity of its free form after being immobilized onto liposome. The active immobilized SSAO was added to the PBS. With the increase of the immobilized enzyme concentration,the effective mobility of its specific substrate, benzylamine, decreased from 4.06×10^-4cm²·V^-1·s^-1 to 0.81×10^-4cm²·V^-1·s^-1 at pH=5, and from 3.91×10^-4cm²·V^-1·s^-1 to 0.29×10^-4cm²·V^-1·s^-1 at pH=7. If the concentration of the inhibitor 2-BrEA in the buffer was increased from 10^-6 mol·L^-1 to 10^-1 mol·L^-1, the effective mobility of benzylamine would increase from 1.42×10^-4cm²·V^-1·s^-1 to 2.22×10^-4cm²·V^-1·s^-1.