LANGMUIR-BLODGETT-FILMS OF MONOAMINE-OXID ASE WITH AMPHIPHILIC POLYELECTROLYTES - STUDY OF CATALYTIC PROPERTIES OF THE ENZYME

The Langmuir-Blodgett (LB) films of monoamine oxidase (MAO) have been formed on the surface of polypropylene membrane with the help of amphi philic polyelectrolytes. The enzyme activity of such protein-polyelect rolyte films was measured by the Clark electrode. It is shown that MAO in the LB films obtained with the help of amphiphilic polyelectrolyte s have been more active than those without polyelectrolytes. Changes i n the catalytic properties of MAO were observed after immobilization o f the enzyme with branched polyethylenimine modified by 12% with the l auryl chain, which may be indicative of new allosteric centers formed. The dependence of the kinetic parameters of the enzyme on the amphiph ilic polyelectrolyte structure is discussed in this paper.