Oriented immobilization of galactose oxidase to bead and magnetic bead cellulose and poly(HEMA-co-EDMA) and magnetic poly(HEMA-co-EDMA) microspheres

• Published in: Journal of chromatography. B, Analytical technologies in the biomedical and life sciences Analytical technologies in the biomedical and life sciences, 2002-04, Vol.770 (1), p.25-34
• Main Authors: Bı́lková, Zuzana, Slováková, Marcela, Lyčka, Antonı́n, Horák, Daniel, Lenfeld, Jiřı́, Turková, Jaroslava, Churáček, Jaroslav
• Format: Article
• Language: English
• Subjects: Animals; Cellulose - chemistry; Enzymes; Enzymes, Immobilized - chemistry; Galactose oxidase; Galactose Oxidase - chemistry; Immunoglobulin G - chemistry; Magnetics; Methacrylates - chemistry; Microspheres; Nuclear Magnetic Resonance, Biomolecular; Periodic Acid - chemistry; Polyhydroxyethyl Methacrylate - chemistry; Swine
• ISSN: 1570-0232; 1873-376X
• DOI: 10.1016/S0378-4347(01)00439-X

In order to obtain an active and stable oxidation reactor for daily use in biochemical laboratory we decided to immobilize galactose oxidase orientedly through a carbohydrate chain to the magnetic carriers. We used hydrazide derivatives of non-magnetic and magnetic bead cellulose and of magnetic and non-magnetic poly(HEMA-co-EDMA) microspheres. Activation of the enzyme molecules was done by sodium periodate in the presence of supplements (fucose, CuSO 4, catalase). Orientedly immobilized galactose oxidase presents high storage stability and lower susceptibility to inappropriate microenvironmental conditions. Reactor reactivated by three pulses of d-galactose retained practically 100% of its native activity after 6 months. The positive properties of both magnetic carriers were entirely confirmed.