NEW CATALYTIC PROPERTIES OF MONOAMINE-OXIDASE IMMOBILIZED IN LANGMUIR-BLODGETT-FILMS WITH AMPHIPHILIC POLYELECTROLYTES

Langmuir-Blodgett (LB) films of monoamine oxidase (MAO) have been form ed on the surface of a polypropylene membrane using amphiphilic polyel ectrolytes. The enzyme activity of such protein-polyelectrolyte films was measured by a Clark electrode. It was shown that in LB films thus formed with the use of amphiphilic polyelectrolytes, MAO activity was higher than in polyelectrolyte-free LB films. Immobilization of MAO wi th branched polyethylenimine modified on 12% by lauryl chain led to pr onounced changes in its catalytic properties. The dependence of the en zyme's kinetic parameters on amphiphilic polyelectrolyte structures wa s discussed. (C) 1994 John Wiley & Sons, Inc.