Immobilization of beta-galactosidase, albumin, and gamma-globulin on epoxy-activated acrylic beads.
A comparative study was conducted into the immobilization of beta-galactosidase, albumin, and gamma-globulin on an epoxy-activated polyacrylic matrix (oxirane C, Röhm-Pharma GmbH, Darmstadt). The kinetic parameters of the immobilized beta-galactosidase were investigated with three kinds of miniaturized analytical reactors; namely, stirred batch, continuous stirred-tank, and packed-bed reactors. The optimum binding conditions, saturation activity and Michaelis constant of immobilized beta-galactosidase are given, together with determinations of the binding capacity of the oxirane C matrix for the three proteins investigated. For beta-galactosidase a saturation activity of 1300 U/g oxirane C was reached. The maximum binding, achieved by experiment, was 140 mg/g with 0.69 yield for albumin, 120 mg/g with 0.61 yield for gamma-globulin, and 40 mg/g with 0.42 yield for beta-galactosidase. From these data the inner surface of the matrix as a function of the size of the bound proteins was estimated.
D000179:Acrylates; D000818:Animals; D002417:Cattle; D004800:Enzymes, Immobilized; D004852:Epoxy Compounds; D005696:Galactosidases; D007700:Kinetics; D011485:Protein Binding; D012212:Rheology; D012709:Serum Albumin; D013499:Surface Properties; D001616:beta-Galactosidase; D005719:gamma-Globulins
D000179:Acrylates; D004800:Enzymes, Immobilized; D004852:Epoxy Compounds; D012709:Serum Albumin; D005719:gamma-Globulins; D005696:Galactosidases; D001616:beta-Galactosidase