CO-immobilization of L-lysine α-oxidase and peroxidase on porous membrane carriers

The qoal of the present study was the development of the optimal method of co-immobilization of two enzymes: L-lysine α-oxidase from Trichoderma sp. and horseradish peroxidase. Commercial nitrocellulose, nylon and N+ nylon membranes were used as carriers. The immobilization was carridont either by absorbtion or by covalent binding with aldehyde groups. The aldehyde groups were attached to the surface of the carriers by UV-irradiation of membranes in the presence of pazidotetrafluorobenzaldehyde. The optimal concentrations of reagents, enzymes and reaction conditions were found. The membranes with the co-immobilised L-lysine α-o.xidase and peroxidase were shown to be useful for the determination of L-lysine concentrations.

Authors
Lukasheva E.V. 1 , Rubtsova M.Ju.2 , Kovba G.V.2 , Berezov T.T. 1 , Egorov A.M.2
Publisher
Научно-исследовательский институт биомедицинской химии им. В.Н. Ореховича
Number of issue
6
Language
Russian
Pages
574-575
Status
Published
Volume
43
Year
1997
Organizations
  • 1 Dpt. of Biochemistry, Russ. Peoples' Friendship University, Mickluho-Maklaya st., 8, 117198, Moscow, Russian Federation
  • 2 Dpt. of Chemical Enzymology, Chemical Faculty, M.V.Lomonosov Moscow State Univ., 119899 Moscow, Russian Federation
Keywords
Determination of L-lysine; Enzyme immobilization; L-lysine-α-oxidase; Membrane carriers; Peroxidase
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