Investigation on semicarbazide-sensitive amine oxidase bio-functionalized chromatography

A model of semicarbazide-sensitive amine oxidase (SSAO) bio-functionalized chromatography was developed using capillary electrophoresis. SSAO was immobilized on liposome, a carrier that simulated cell membrane. The experiment of the effect of pH value on the stability of immobilized enzyme showed that pH 5.0 was the perfect condition for immobilization. SSAO activity detection displayed that the specific activity of SSAO both in free form and immobilized form were 0.0404 and 0.0347 mmol g^-1 min^-1 respectively. The active immobilized SSAO was added to the PBS(10 mmol/L, pH 5) as pseudo-stationary phase. With the concentration of immobilized enzyme increasing from 0. 004 g/L to 0. 856 g/L, the effective mobility of its specific substrate, benzylamine, decreased from 4. 06 × 10^-4 (cm ² /V · s) to 0. 81 × 10^-4 (cm² /V · s). Subsequently, the established bio-functionalized chromatographic method provides a new technology for investigating interactions among the biological molecules.