Twenty-six carriers from three series of acrylic copolymers were evalu
ated for trypsin immobilisation. The following monomers were used to p
repare polymer matrices: ethylene glycol dimethacrylate, trimethylolpr
opane triacrylate, ethyl acrylate, butyl acrylate, hydroxypropyl metha
crylate, acrylonitrile, and divinylbenzene. The carriers with trimethy
lolpropane triacrylate as the cross-linking agent were selected as the
most profitable matrices for expressing enzyme activity. Considering
the influence of inert diluents on the carrier's superstructure and tr
ypsin immobilisation it was shown that cyclohexanol as co-diluent prod
uced a good microenvironment for enzyme activity while toluene created
an unsuitable carrier structure. The most effective carrier was a cop
olymer of acrylonitrile/trimethylolpropane triacrylate synthesised in
the presence of cyclohexanol and 2-ethylhexanol. A comparison of the p
roperties of the enzyme-carrier preparation and native trypsin demonst
rated that the binding of the protein to the carrier caused an increas
e of the storage and pH-stability of the bound enzyme. (C) 1998 Elsevi
er Science Ltd. All rights reserved.