ATTACHMENT OF HORSERADISH-PEROXIDASE (HRP) ONTO THE POLY(STYRENE ACROLEIN) LATEXES AND ONTO THEIR DERIVATIVES WITH AMINO-GROUPS ON THE SURFACE - ACTIVITY OF IMMOBILIZED ENZYME/

The polystyrene (P(S)), poly(styrene/acrolein) (P(SA)), and polyacrole in (P(A)) latexes, with varied fraction of polyacrolein in the surface layer (f(A) = 0, 0.50, 0.63, 0.84, 1.00), were used for the attachmen t of horseradish peroxidase. Surfaces of latexes were modified by reac tion with ethylenediamine. In this step the aldehyde groups from polya crolein were blocked and the primary amino groups were introduced. The carbohydrate portion of HRP was oxidized in the reaction leading to f ormation of aldehyde groups. The adsorption and covalent immobilizatio n of HRP onto the P(S), P(SA), and P(A) latexes and of the oxidized HR P (HRP-OX) onto the modified latex particles, with amino groups on the surface (P(SA)-M and P(A)-M), were investigated. The activities of pa rent and oxidized HRP were compared with activities of the correspondi ng enzymes in solution. It has been found that whereas HRP is not suit able for the covalent immobilization on P(SA) latex and loses its acti vity after adsorption onto P(S) latex, HRP-OX can be adsorbed onto P(S ) latex and is readily immobilized covalently onto the ethylenediamine modified P(SA) and P(A) latexes, retaining much of its former enzymat ic reactivity.