Behaviour of firefly luciferase associated with Langmuir-Blodgett films

Molecular recognition was performed through the association of an enzymatic protein with lipidic nanostructures. Firefly luciferase was adsorbed onto Langmuir-Blodgett behenic acid films. The enzyme association was characterized with Fourier transform infrared spectroscopy by the presence of the stretching vibrations of the luciferase peptidic bonds, The amount of adsorbed protein was assessed by values of the amide I peak integration. It was observed that a steady quantity of protein was specifically and tightly linked to the lipidic surface whatever the concentration of enzymatic solution used. Activity was detected through bioluminescence reaction. A comparative study with the free enzyme revealed that immobilization of the luciferase preserved its enzymatic activity but did not protect the enzyme against the aging effect. More, the kinetic behaviour of the associated enzyme was irreversibly modified but without injurious effect on enzymatic activity.