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New catalytic properties of monoamine oxidase immobilized in Langmuir–blodgett films with amphiphilic polyelectrolytes
Author(s) -
Barmin Anatoli V.,
Eremenko Arkadi V.,
Kurochkin llya N.,
Moskvitina Tatyana A.
Publication year - 1994
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.260440710
Subject(s) - polyelectrolyte , amphiphile , polyethylenimine , langmuir–blodgett film , chemistry , chemical engineering , monoamine oxidase , membrane , polymer chemistry , copolymer , organic chemistry , enzyme , polymer , biochemistry , molecule , transfection , engineering , gene
Langmuir‐Blodgett (LB) films of monoamine oxidase (MAO) have been formed on the surface f a polypropylene membrane using amphiphilic polyelectrolytes. The enzyme activity of such protein‐polyelectrolyte films was measured by a Clark electrodes. It was shown that in LB films thus formed the use of amphiphilc polyelectrolytes, MAO activity was higher than in polyelectrolyte‐free LB films. Immobilization of MAO with branched polyethylenimine modified on 12% by laurylchain led to pronounced changes in its catalytic properties. The dependence of the enzyme's kinetic parameters on amphiphilic polyelectrolyte structures was discussed. © 1994 John Wiley & Sons, Inc.